|
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: 1050.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 83 GQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGR 162
Cdd:pfam09730 1 GQSVSSHKKVAADGESREESLLQESASKEAYYAQRILELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 163 LRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEE 242
Cdd:pfam09730 81 MRDEIKEYKVREARLLQDYSELEEENISLQKQVSVLKQNQVEFEGLKHEITRKEEETELLNSQLEEAIRLREIAERQLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 243 ALETLKTEREQKNSLRKELSHYMSINDSFYTSHLHVSLDGLKFSDD---AAEPNNDAEALvNGFEHG--GLAKLPLDNKT 317
Cdd:pfam09730 161 ALETLKTEREQKNSLRKELSHYMTLNDFDYVSHLSISLDGLKFSEDegaGTEPNNDGEAM-DGGENGggGLKNSGLDNRT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 318 STPKKEGLAPPSPSLVSDLLSELNISEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSAL 397
Cdd:pfam09730 240 STPRKSEVFPPAPSLVSDLLSELNISEIQKLKQQLIQVEREKVSLLSTLQESQKQLEQAKGALSEQQEKVNRLTENLEAM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 398 RRLQASKERQTALDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAE 477
Cdd:pfam09730 320 RGLQASKERQDALDSEKDRDSHEDGDYYEVDINGPEILECKYRVAVEEAGELREELKALKARYNTLEERYKEEKTRWEAE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 478 GQALTEKVSLLEKASRQDRELLARLEKELKKVSDVAGETQGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYY 557
Cdd:pfam09730 400 AQDLAEKIRQLEKASHQDQERIAHLEKELGKTRKVAGESEGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYY 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 558 REGQGGAGRtspggRTSPEARGRRSPILLPKGLLAPEAGRADGGtGDSSPSPGSSLPSPLSDPRREPMNIYNLIAIIRDQ 637
Cdd:pfam09730 480 REGAGARAR-----KSHQEPRGLRSPRLLTRGLFMGEVGTADTT-SNSPSPCSSCPGSPTSDFRREPMNIYNLVAIIRDQ 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 638 IKHLQAAVDRTTELSRQRIASQELGPAVDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSKYEN 717
Cdd:pfam09730 554 IKHLQVAVDRTTELSRQRGAALELSTESDKDKEALMEEILKLKSLLSTKREQIATLRTVLKANKQTAEVALANLKSKYEN 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 718 EKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLE 797
Cdd:pfam09730 634 EKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLE 713
|
....
gi 119583233 798 LLEL 801
Cdd:pfam09730 714 DLEF 717
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
5-535 |
1.86e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.12 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 5 SEEEEYARLVMEAQPEWLRAEVKRLSHELAETTREKIQAAEyglavleEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQ 84
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA-------ELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 85 AHTNHKKVAADGESREESLIQESASKEqyyvrkvlELQTELKQLRNVLTNTQSE----NERLASVAQELKEINQNVEIQR 160
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLE--------ELEEELAELEEELEELEEEleelEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 161 GRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQL 240
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 241 EEALETLKTEREQKNSLRKELShymsiNDSFYTSHLHVSLDGLKFSDDAAEPN----NDAEALVNGFEHGGLAKLPLDNK 316
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLA-----ELLEEAALLEAALAELLEELAEAAARllllLEAEADYEGFLEGVKAALLLAGL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 317 TSTPKKEGLAPPSPSLVSD--------LLSELNISEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQ--QEK 386
Cdd:COG1196 520 RGLAGAVAVLIGVEAAYEAaleaalaaALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARgaIGA 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 387 VTRLTENLSALRRLQASKERQTALDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGEL-REQLKALRSTHEAREA 465
Cdd:COG1196 600 AVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLtGGSRRELLAALLEAEA 679
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 466 QHAEEKGRYEAEGQALTEKVSLLEKASRQDRELLARLEKELKKVSDVAGETQGSLSVAQDELVTFSEELA 535
Cdd:COG1196 680 ELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6-264 |
7.83e-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: 66.23 E-value: 7.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 6 EEEEYARLVMEAQPEWLRAEVKRLSHELAETTREkIQAAEYGLAVLEEKH-QLKLQFEELEVDYEAIRSEMEQLK----- 79
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEE-LEELTAELQELEEKLeELRLEVSELEEEIEELQKELYALAneisr 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 80 -EAFGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEI 158
Cdd:TIGR02168 300 lEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 159 QRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQ--VEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEIS 236
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeeLLKKLEEAELKELQAELEELEEELEELQEELERL 459
|
250 260
....*....|....*....|....*...
gi 119583233 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 |
8.17e-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: 66.23 E-value: 8.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 23 RAEVKRLSHELAETTrEKIQAAEYGLAVLEEKHQ-LKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGEsREE 101
Cdd:TIGR02168 676 RREIEELEEKIEELE-EKIAELEKALAELRKELEeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA-QLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 102 SLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDY 181
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 182 SELEEENISLQKQvsvLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKEL 261
Cdd:TIGR02168 834 AATERRLEDLEEQ---IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
.
gi 119583233 262 S 262
Cdd:TIGR02168 911 S 911
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
38-261 |
4.09e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 38 REKIQAAEYgLAVLEEKHQLK-----LQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREESLIQESAskeq 112
Cdd:COG1196 207 RQAEKAERY-RELKEELKELEaelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL---- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 113 yyvrKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQ 192
Cdd:COG1196 282 ----ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119583233 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 |
4.96e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 5 SEEEEYARLVMEAQPEWLRAEVKRLSHELaETTREKIQAAEYGLAVLE-EKHQLKLQFEELEVDYEAIRSEMEQLKeafg 83
Cdd:TIGR02169 204 RREREKAERYQALLKEKREYEGYELLKEK-EALERQKEAIERQLASLEeELEKLTEEISELEKRLEEIEQLLEELN---- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 84 qahtnhKKVAADGESREESL---IQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEinqNVEIQR 160
Cdd:TIGR02169 279 ------KKIKDLGEEEQLRVkekIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELER---EIEEER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 161 GRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEI--------------KRLEEETEYLNSQL 226
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREInelkreldrlqeelQRLSEELADLNAAI 429
|
250 260 270
....*....|....*....|....*....|....*...
gi 119583233 227 EDAIRLKEISERQLEEALETLKTEREQKNSLRKELSHY 264
Cdd:TIGR02169 430 AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
76-813 |
6.05e-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: 53.52 E-value: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 76 EQLKEAFGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSE----NERLASVAQELKE 151
Cdd:TIGR02168 220 AELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEieelQKELYALANEISR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 152 INQNVEIQRGRLRDDIKEYKFREARLLQDYS----------ELEEENISLQKqvsvlrqnqvEFEGLKHEIKRLEEETEY 221
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELESkldelaeelaELEEKLEELKE----------ELESLEAELEELEAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 222 LNSQLEDAirlkeisERQLEEALETLKTEREQKNSLRKELShymsindsfytshlhvSLDGLKFSDDAAEPNNDAEalvn 301
Cdd:TIGR02168 370 LESRLEEL-------EEQLETLRSKVAQLELQIASLNNEIE----------------RLEARLERLEDRRERLQQE---- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 302 gfehgglaklpldnktstpkkeglappspslVSDLLSELNISEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLS 381
Cdd:TIGR02168 423 -------------------------------IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 382 EQQEKVTRLTENLSALRRLQASKERQ------------TALDNEKDRDSHED--GDYYEVDingpeilaCKYHVAVAEAG 447
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLqenlegfsegvkALLKNQSGLSGILGvlSELISVD--------EGYEAAIEAAL 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 448 ELREQLKALRSTHEAREAQhaeekgryEAEGQALTEKVSLLEKASRQDRELLARLEKELKKVSDVAGetqgslsvAQDEL 527
Cdd:TIGR02168 544 GGRLQAVVVENLNAAKKAI--------AFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLG--------VAKDL 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 528 VTFSEE----LANLYHHVCMCNNETPNRVMLDYYREGQG----GAGRTSPGGRTSPEARGRRSPILLPKGLLAPEAGRAD 599
Cdd:TIGR02168 608 VKFDPKlrkaLSYLLGGVLVVDDLDNALELAKKLRPGYRivtlDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIE 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 600 GGTGDSS----------------PSPGSSLPSPLSDPRREPMNIYNLIAIIRDQIKHLQAAVDRT-----------TELS 652
Cdd:TIGR02168 688 ELEEKIAelekalaelrkeleelEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLskelteleaeiEELE 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 653 RQRIASQELGPAVDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSkYENEKAMVTETMMKLRNE 732
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES-LERRIAATERRLEDLEEQ 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 733 LKALKEDAATFSSLRAMFATRCDEYITQLDE-------MQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLELLELDHEQ 805
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEAllnerasLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
....*...
gi 119583233 806 TRRGRAKA 813
Cdd:TIGR02168 927 LELRLEGL 934
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
22-250 |
1.59e-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: 51.99 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 22 LRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREE 101
Cdd:TIGR02169 707 LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 102 SLiqeSASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDY 181
Cdd:TIGR02169 787 RL---SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK 863
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119583233 182 SELEEENISLQKQVSVLRQnqvEFEGLKHEIKRLEEETEYLNS---QLEDAIRLKEISERQLEEALETLKTE 250
Cdd:TIGR02169 864 EELEEELEELEAALRDLES---RLGDLKKERDELEAQLRELERkieELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
6-200 |
2.08e-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: 50.92 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 6 EEEEYARLVMEAQPEWLRAEVKRLSHELAETTReKIQAAEYGLAVLEEK-HQLKLQFEELEVDYEAIRSEM-EQLKEAFG 83
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALAR-RIRALEQELAALEAElAELEKEIAELRAELEAQKEELaELLRALYR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 84 QAHTNHKKVAADGESreeslIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRL 163
Cdd:COG4942 116 LGRQPPLALLLSPED-----FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190
....*....|....*....|....*....|....*..
gi 119583233 164 RDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQ 200
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6-247 |
3.45e-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: 50.83 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 6 EEEEYARLVMEAQPEWLRAEVKRLS-HELAETTREKIQAAEYGLAVLEEKHQ-LKLQFEELEVDYEAIRSEMEQLKEAFG 83
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEElEAQIEQLKEELKALREALDELRAELTlLNEEAANLRERLESLERRIAATERRLE 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 84 QAHTNHKKVAADGESREESLIQESASKEqyyvrkvlELQTELKQLRNVLTNTQSE----NERLASVAQELKEINQNV--- 156
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELIE--------ELESELEALLNERASLEEAlallRSELEELSEELRELESKRsel 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 157 EIQRGRLRDDIKEYKFREARLLQDYSEL-----EEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAI- 230
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLqerlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIe 993
|
250 260
....*....|....*....|....*.
gi 119583233 231 RLKEISERQ---------LEEALETL 247
Cdd:TIGR02168 994 EYEELKERYdfltaqkedLTEAKETL 1019
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
97-537 |
4.11e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 97 ESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDdiKEYKFREAR 176
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK--LEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 177 LLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIR-LKEISERQLEEALETLKTEREQKN 255
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEELQQRLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 256 SLRKELSHYMSINDSfytshLHVSLDGLKFSDDAAEPNNDAEALVNGFEHGGLAKLPLDNKTSTPKKEGLAPPSPSLVSD 335
Cdd:COG4717 210 ELEEELEEAQEELEE-----LEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 336 LLseLNISEIQKLKQQLMQMEREKAGLLATLQD-TQKQLEHTRGSLS-EQQEKVTRLTENLSALRRLQASKERQTALDNE 413
Cdd:COG4717 285 LL--ALLFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 414 KDRDSHED---GDYYEVDINGPEIL------ACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEkgRYEAEGQALTEK 484
Cdd:COG4717 363 LQLEELEQeiaALLAEAGVEDEEELraaleqAEEYQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEE 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 119583233 485 VSLLEKASRQDRELLARLEKELKKVsdvagETQGSLSVAQDELVTFSEELANL 537
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQL-----EEDGELAELLQELEELKAELREL 488
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
20-299 |
4.38e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 50.67 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 20 EWLRAEVKRLSHELAET-TREKIQAAEYGLAVLEEKHQLKLQfEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGES 98
Cdd:PLN02939 166 EALQGKINILEMRLSETdARIKLAAQEKIHVEILEEQLEKLR-NELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQF 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 99 REESLIQESASKEQYYVrkvLE-----LQTELKQLRNVLTNTQSENERLASVAQE-LKEINQNVEIQRGRLRDDIKEYkf 172
Cdd:PLN02939 245 LKAELIEVAETEERVFK---LEkerslLDASLRELESKFIVAQEDVSKLSPLQYDcWWEKVENLQDLLDRATNQVEKA-- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 173 reARLLQDYSELEEENISLQ---KQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKT 249
Cdd:PLN02939 320 --ALVLDQNQDLRDKVDKLEaslKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKE 397
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 119583233 250 EREqknslRKELSHYMSINDSFYTSHLHVSLDGlkFSDDAAEPNNDAEAL 299
Cdd:PLN02939 398 ESK-----KRSLEHPADDMPSEFWSRILLLIDG--WLLEKKISNNDAKLL 440
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
32-261 |
6.27e-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: 50.11 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 32 ELAETTREKIQAAEYGLAVLEEKHQLKL-QFEELEVDYEAIRSEMEQLKEAFGQAHT------NHKKVAADGESREESL- 103
Cdd:pfam05483 363 ELLRTEQQRLEKNEDQLKIITMELQKKSsELEEMTKFKNNKEVELEELKKILAEDEKlldekkQFEKIAEELKGKEQELi 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 104 --------------IQESASK--EQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDI 167
Cdd:pfam05483 443 fllqarekeihdleIQLTAIKtsEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDI 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 168 KEYKFREARLLQDYSELEEENISLQKQVSVLRQnqvEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETL 247
Cdd:pfam05483 523 INCKKQEERMLKQIENLEEKEMNLRDELESVRE---EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNL 599
|
250
....*....|....
gi 119583233 248 KTEREQKNSLRKEL 261
Cdd:pfam05483 600 KKQIENKNKNIEEL 613
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
343-537 |
8.35e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 8.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 343 SEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSALRRLQASKERQTALDNEKDRDSHEDG 422
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 423 dyyevdingpEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAEGQALTEKVSLLEKASRQDRELLARL 502
Cdd:COG1196 347 ----------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
170 180 190
....*....|....*....|....*....|....*
gi 119583233 503 EKELKKVSDVAGETQGSLSVAQDELVTFSEELANL 537
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
20-229 |
9.43e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 9.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 20 EWLRAEVKRLSHELAETtREKIQA--AEYGLAVLEEKHQLKL-QFEELEVDYEAIRSEMEQLKEAFGQAhtnhKKVAADG 96
Cdd:COG3206 178 EFLEEQLPELRKELEEA-EAALEEfrQKNGLVDLSEEAKLLLqQLSELESQLAEARAELAEAEARLAAL----RAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 97 ESREESLIQESAskEQYYVRKVLELQTELKQLRNVLTntqSENERLASVAQELKEINQNVEIQRGRLRDDIK-EYKFREA 175
Cdd:COG3206 253 PDALPELLQSPV--IQQLRAQLAELEAELAELSARYT---PNHPDVIALRAQIAALRAQLQQEAQRILASLEaELEALQA 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 119583233 176 RLlqdySELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDA 229
Cdd:COG3206 328 RE----ASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6-534 |
2.52e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 6 EEEEYARLVMEAQPEWLRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAfGQA 85
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ-IAS 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 86 HTNH----KKVAADGESREESLIQESASKEQYYVR-KVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQR 160
Cdd:TIGR02168 398 LNNEierlEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 161 GRLRDDIKEYKFREARLlqdySELEEENISLQKQVSVLRQNQVEFEGLKH---EIKRLEEETE-------------YLNS 224
Cdd:TIGR02168 478 DAAERELAQLQARLDSL----ERLQENLEGFSEGVKALLKNQSGLSGILGvlsELISVDEGYEaaieaalggrlqaVVVE 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 225 QLEDAIR-----------------LKEISERQLEEALETLKTEREQKNSLRKELSHYmsinDSFYTSHLHVSLDGLKFSD 287
Cdd:TIGR02168 554 NLNAAKKaiaflkqnelgrvtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKF----DPKLRKALSYLLGGVLVVD 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 288 DAAEPNNDAEALvngfeHGGLAKLPLDNKTSTPKkeGLAPPSPSLVSDLLSELNIsEIQKLKQQLMQMEREKAGLLATLQ 367
Cdd:TIGR02168 630 DLDNALELAKKL-----RPGYRIVTLDGDLVRPG--GVITGGSAKTNSSILERRR-EIEELEEKIEELEEKIAELEKALA 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 368 DTQKQLE----HTRGSLSEQQEKVTRLTENLSALRRLQASKERQTALDNEKDRDSHEDGDYYEVDINGPEILACKYHVAV 443
Cdd:TIGR02168 702 ELRKELEeleeELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE 781
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 444 AEAGELREQLKALRSTHEAREAQHAEEKGRYEAEGQALTEKVSLLEKASRQDRELLARLEkELKKVSDVAGETQGSLSVA 523
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE-DLEEQIEELSEDIESLAAE 860
|
570
....*....|.
gi 119583233 524 QDELVTFSEEL 534
Cdd:TIGR02168 861 IEELEELIEEL 871
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
6-271 |
3.59e-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: 47.76 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 6 EEEEYARLVMEAQPEwLRAEVKRLSHELAETtREKIQAAEyglAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQa 85
Cdd:TIGR02169 781 LNDLEARLSHSRIPE-IQAELSKLEEEVSRI-EARLREIE---QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK- 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 86 htnhkkvaadgesREESLIQESASKEQyyvrKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRD 165
Cdd:TIGR02169 855 -------------EIENLNGKKEELEE----ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 166 DIKEYKFREARLLQDYSELEEENISLQKQVSvlrqNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISER---QLEE 242
Cdd:TIGR02169 918 RLSELKAKLEALEEELSEIEDPKGEDEEIPE----EELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKrldELKE 993
|
250 260 270
....*....|....*....|....*....|....*...
gi 119583233 243 ALETLKTER-------EQKNSLRKE--LSHYMSINDSF 271
Cdd:TIGR02169 994 KRAKLEEERkaileriEEYEKKKREvfMEAFEAINENF 1031
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
116-253 |
4.63e-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: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 116 RKVLELQTELKQLRNVLTNTQSENERLASVAQELKeinqnveiQRGRLRDDIKEYKFREarllQDYSELEEENISLQKQV 195
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQ--------ERREALQRLAEYSWDE----IDVASAEREIAELEAEL 677
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 119583233 196 SVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQ 253
Cdd:COG4913 678 ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
343-508 |
5.76e-05 |
|
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: 45.30 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 343 SEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSALR-RLQASKERQTALDNEKDRDSHED 421
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEaRIKKYEEQLGNVRNNKEYEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 422 gdyyEVDINGPEILACKYHV--AVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAEGQALTEKVSLLEKASrqdRELL 499
Cdd:COG1579 97 ----EIESLKRRISDLEDEIleLMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER---EELA 169
|
....*....
gi 119583233 500 ARLEKELKK 508
Cdd:COG1579 170 AKIPPELLA 178
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
22-262 |
6.02e-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: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 22 LRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREE 101
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 102 SLIQESASKEQYYVRKVlELQTELKQLRNVLTNTQSE--NERLASVAQELKEINQNVEIQRGRLRD---DIKEYKFREAR 176
Cdd:TIGR02169 752 EIENVKSELKELEARIE-ELEEDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREieqKLNRLTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 177 LLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYlnsqledairlkeiSERQLEEALETLKTEREQkns 256
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA--------------ALRDLESRLGDLKKERDE--- 893
|
....*.
gi 119583233 257 LRKELS 262
Cdd:TIGR02169 894 LEAQLR 899
|
|
| 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 119583233 100 EESLIQESASKEQYYVRKVLELQTELKQLRnvltntqsenerlaSVAQELKEINQNVEIQRGRLRDDIKEYKfreaRLLQ 179
Cdd:COG5022 938 NNIDLEEGPSIEYVKLPELNKLHEVESKLK--------------ETSEEYEDLLKKSTILVREGNKANSELK----NFKK 999
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 180 DYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQ--LEDAIRLKEISERQLEEALETLKTEREqkNSL 257
Cdd:COG5022 1000 ELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILkpLQKLKGLLLLENNQLQARYKALKLRRE--NSL 1077
|
....*..
gi 119583233 258 RKELSHY 264
Cdd:COG5022 1078 LDDKQLY 1084
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
344-511 |
7.99e-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: 45.91 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 344 EIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSALRR----LQASKERQTA---------- 409
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKeiaeLRAELEAQKEelaellraly 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 410 -----------LDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAEG 478
Cdd:COG4942 115 rlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190
....*....|....*....|....*....|...
gi 119583233 479 QALTEKVSLLEKASRQDRELLARLEKELKKVSD 511
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
26-508 |
2.03e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 26 VKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAhtnhkkvaadgESREESLIQ 105
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL-----------EAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 106 ESASKEQyyVRKVLELQTELKQLRNVLtntQSENERLASVAQELKEInQNVEIQRGRLRDDIKEYKFREARLLQDYSELE 185
Cdd:COG4717 117 ELEKLEK--LLQLLPLYQELEALEAEL---AELPERLEELEERLEEL-RELEEELEELEAELAELQEELEELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 186 EENIS-LQKQVSVLRQNQVEfegLKHEIKRLEEETEYLNSQLEdairlkEISERQLEEALETLKTEREQKNSLRKELSHY 264
Cdd:COG4717 191 EEELQdLAEELEELQQRLAE---LEEELEEAQEELEELEEELE------QLENELEAAALEERLKEARLLLLIAAALLAL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 265 MSINDSFYTSHLHV-----------SLDGLKFSDDAAEPNNDAEALVNGFEHGGLAKLPLDnktSTPKKEGLAPP-SPSL 332
Cdd:COG4717 262 LGLGGSLLSLILTIagvlflvlgllALLFLLLAREKASLGKEAEELQALPALEELEEEELE---ELLAALGLPPDlSPEE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 333 VSDLLSElnISEIQKLKQQLMQMEREKAglLATLQDTQKQLEHTRGSLSEQQekvtrLTENLSALRRLQASKERQTALdn 412
Cdd:COG4717 339 LLELLDR--IEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVEDEEE-----LRAALEQAEEYQELKEELEEL-- 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 413 EKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQ--HAEEKGRYEAEGQALTEKVSLLEK 490
Cdd:COG4717 408 EEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEleQLEEDGELAELLQELEELKAELRE 487
|
490 500
....*....|....*....|....
gi 119583233 491 ASRQD------RELLARLEKELKK 508
Cdd:COG4717 488 LAEEWaalklaLELLEEAREEYRE 511
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
118-512 |
2.08e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 118 VLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVsv 197
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI-- 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 198 lRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKELShymsindsfytshlh 277
Cdd:TIGR02168 750 -AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT--------------- 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 278 vsldglKFSDDAAEPNNDAEALVNgfehgglaklpldnktstpkkeglappspslvsdllselnisEIQKLKQQLMQMER 357
Cdd:TIGR02168 814 ------LLNEEAANLRERLESLER------------------------------------------RIAATERRLEDLEE 845
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 358 EKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSAL-RRLQASKERQTALDNEKDRDSHEDGDyyevdingpeila 436
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLeEALALLRSELEELSEELRELESKRSE------------- 912
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 437 ckyhvAVAEAGELREQLKALRSTHEAREAQHAEEKGR----YEAEGQALTEKVSLLEKASRQDRELLARLEKELKKVSDV 512
Cdd:TIGR02168 913 -----LRRELEELREKLAQLELRLEGLEVRIDNLQERlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPV 987
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
62-261 |
2.35e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 62 EELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREESLIQESaskeqyyvRKVLELQTELKQLRNVLTNTQSENER 141
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA--------RRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 142 LASVAQELKE--INQNVEIQRGRLRDDIK--------EYKFREARLLQDYSELEEENI-SLQKQVSVLRQNQVEFEGLKH 210
Cdd:COG4942 95 LRAELEAQKEelAELLRALYRLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAeELRADLAELAALRAELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 119583233 211 EIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKEL 261
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
22-537 |
2.54e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 22 LRAEVKRLSHELAETTREKIQAAEY---GLAVLEEKHQLKLQFEELEVDYEAIR---SEMEQLKEAFGQAHTNHKKVAAD 95
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETrdeADEVLEEHEERREELETLEAEIEDLRetiAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 96 GESREESLIQE----SASKEQYYVRKVlELQTELKQLRnvltntqsenERLASVAQELKEINQNVEiqrgRLRDDIKEYK 171
Cdd:PRK02224 291 LEEERDDLLAEagldDADAEAVEARRE-ELEDRDEELR----------DRLEECRVAAQAHNEEAE----SLREDADDLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 172 FREARLLQDYSELEEEnisLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAirlkeisERQLEEALETLKTER 251
Cdd:PRK02224 356 ERAEELREEAAELESE---LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA-------EDFLEELREERDELR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 252 EQKNSLRKELShymsindsfytshlhvsldglkfsdDAAEPNNDAEALVNgfehgglaklpldnktstpkkeglAPPSPS 331
Cdd:PRK02224 426 EREAELEATLR-------------------------TARERVEEAEALLE------------------------AGKCPE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 332 LVSDLLSELNISEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRgSLSEQQEKVTRLTENLSALRRLQASKERQTALD 411
Cdd:PRK02224 457 CGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEK 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 412 NEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEA----GELREQLKALRSTHEA--REAQHAEEKGRYEAEGQALTEKV 485
Cdd:PRK02224 536 RERAEELRERAAELEAEAEEKREAAAEAEEEAEEAreevAELNSKLAELKERIESleRIRTLLAAIADAEDEIERLREKR 615
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 119583233 486 SLLEKASRQDREllaRLEKELKKVSDVAGETQGS-LSVAQDELVTFSEELANL 537
Cdd:PRK02224 616 EALAELNDERRE---RLAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQV 665
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
113-265 |
2.54e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 113 YYVRKVLeLQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGR------LRDDIKEYKFREARLLQDYSELEE 186
Cdd:PRK12704 22 YFVRKKI-AEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRnefekeLRERRNELQKLEKRLLQKEENLDR 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119583233 187 ENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDaiRLKEISERQLEEALETLKTEREQKnsLRKELSHYM 265
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ--ELERISGLTAEEAKEILLEKVEEE--ARHEAAVLI 175
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
22-205 |
3.10e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 22 LRAEVKRLS-----HELAETTREKIQAAEYGLAVL------EEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTN-- 88
Cdd:COG4913 247 AREQIELLEpirelAERYAAARERLAELEYLRAALrlwfaqRRLELLEAELEELRAELARLEAELERLEARLDALREEld 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 89 --HKKVAADGESREESLIQESASKEQYY---VRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEinqNVEIQRGRL 163
Cdd:COG4913 327 elEAQIRGNGGDRLEQLEREIERLERELeerERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE---ALEEELEAL 403
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 119583233 164 RDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEF 205
Cdd:COG4913 404 EEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
60-263 |
4.18e-04 |
|
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: 43.96 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 60 QFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREESLIQESASKEQyyvrKVLELQTELKQLRNVLTNTQSEN 139
Cdd:pfam05557 59 LLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKN----ELSELRRQIQRAELELQSTNSEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 140 ERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLlqdySELEEEnISLQKQ----VSVLRQNQVEFEGLKHEIKRL 215
Cdd:pfam05557 135 EELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRI----KELEFE-IQSQEQdseiVKNSKSELARIPELEKELERL 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 119583233 216 EEETEYLNSQLEDAIRLKEISErQLEEALETLKTEREQKNSLRKELSH 263
Cdd:pfam05557 210 REHNKHLNENIENKLLLKEEVE-DLKRKLEREEKYREEAATLELEKEK 256
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
22-253 |
6.89e-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: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 22 LRAEVKRLS--HELAETTREKIQAaeygLAVLEEKHQlklQFEELEVDYEAIRSEMEQLKEAFGQahtnhkKVAADGESR 99
Cdd:COG4913 230 LVEHFDDLEraHEALEDAREQIEL----LEPIRELAE---RYAAARERLAELEYLRAALRLWFAQ------RRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 100 EESLIQESASKEQyyvrKVLELQTELKQLRNVLTNTqsENERLASVAQELKEINQnveiQRGRLRDDIKEYKFREARLLQ 179
Cdd:COG4913 297 LEELRAELARLEA----ELERLEARLDALREELDEL--EAQIRGNGGDRLEQLER----EIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119583233 180 DYSELEEEnislqkqvsvLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQ 253
Cdd:COG4913 367 LLAALGLP----------LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
49-262 |
7.69e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.99 E-value: 7.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 49 AVLEEKHQLKL-QFEEL--EVDYEAIRSEME----------QLKEAFGQAHTNHKKVAADGESREESLIQESASKEQYYV 115
Cdd:PRK05771 20 EVLEALHELGVvHIEDLkeELSNERLRKLRSlltklsealdKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 116 RKVLELQTELKQLRNVLTNTQSENERL---ASVAQELKEINQ--NVEIQRGRlrddIKEYKFREARLLQDYSELEEENIS 190
Cdd:PRK05771 100 KEIKELEEEISELENEIKELEQEIERLepwGNFDLDLSLLLGfkYVSVFVGT----VPEDKLEELKLESDVENVEYISTD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 191 LQKQVSVL-------------------RQNQVEFEG-LKHEIKRLEEETEYLNSQLEDAI-RLKEISERQLEEAL---ET 246
Cdd:PRK05771 176 KGYVYVVVvvlkelsdeveeelkklgfERLELEEEGtPSELIREIKEELEEIEKERESLLeELKELAKKYLEELLalyEY 255
|
250
....*....|....*.
gi 119583233 247 LKTEREQKNSLRKELS 262
Cdd:PRK05771 256 LEIELERAEALSKFLK 271
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
23-260 |
9.00e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 23 RAEVKRLSHELAETTREKIQAAEYGLAVLEEK--HQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESRE 100
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 101 ESLIQESASKEQYyVRKVLELQT--ELK---QLRNVLTNTQSENERLASV--AQELKEINQNVEIQRGRLRDDIKEYKFR 173
Cdd:PTZ00121 1532 EAKKADEAKKAEE-KKKADELKKaeELKkaeEKKKAEEAKKAEEDKNMALrkAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 174 EARLLQDYSELEEE---NISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEdaiRLKEISERQLEEALETLKTE 250
Cdd:PTZ00121 1611 EAKKAEEAKIKAEElkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA---KKAEEDKKKAEEAKKAEEDE 1687
|
250
....*....|
gi 119583233 251 REQKNSLRKE 260
Cdd:PTZ00121 1688 KKAAEALKKE 1697
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
343-537 |
9.21e-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: 42.44 E-value: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 343 SEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSAL--------RRLQASKERQTALDNEK 414
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALeqelaaleAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 415 DRDSHEDGD-----YYEVDINGPEILackyhVAVAEAGELREQLKALRSTHEAREAQHAEekgrYEAEGQALTEKVSLLE 489
Cdd:COG4942 100 EAQKEELAEllralYRLGRQPPLALL-----LSPEDFLDAVRRLQYLKYLAPARREQAEE----LRADLAELAALRAELE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 119583233 490 KASRQDRELLARLEKELKKVSDVAGETQGSLSVAQDELVTFSEELANL 537
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
22-254 |
9.79e-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: 42.44 E-value: 9.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 22 LRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAhtnhkkvaadgESREE 101
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL-----------EKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 102 SLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEykfrearLLQDY 181
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-------LAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119583233 182 SELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQK 254
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
120-261 |
2.53e-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: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 120 ELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLR 199
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119583233 200 QnqvEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKEL 261
Cdd:TIGR04523 433 E---TIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
116-261 |
2.57e-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: 40.29 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 116 RKVLELQTELKQLRNVLTNTQsenERLASVAQELKEINQNVEIQRGRLRDDikEYKFREARLLQDYSELEEENISLQKQV 195
Cdd:COG1579 31 AELAELEDELAALEARLEAAK---TELEDLEKEIKRLELEIEEVEARIKKY--EEQLGNVRNNKEYEALQKEIESLKRRI 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119583233 196 SVLRQNQVEFEglkHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKEL 261
Cdd:COG1579 106 SDLEDEILELM---ERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
23-469 |
3.80e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 23 RAEVKRLSHELAETTREKIQAAEYGLAVLE----EKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGES 98
Cdd:PRK02224 274 REELAEEVRDLRERLEELEEERDDLLAEAGlddaDAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADD 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 99 RE-------------ESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRD 165
Cdd:PRK02224 354 LEeraeelreeaaelESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEA 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 166 DIKEYK--FREARLLQDYSELEE--ENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEI------ 235
Cdd:PRK02224 434 TLRTARerVEEAEALLEAGKCPEcgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAedrier 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 236 -------SERQLEEALETLKTEREQKNSLRKELSHYMSindsfytshlhvslDGLKFSDDAAEPNNDAEAlvngfEHGGL 308
Cdd:PRK02224 514 leerredLEELIAERRETIEEKRERAEELRERAAELEA--------------EAEEKREAAAEAEEEAEE-----AREEV 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 309 AKLPLDNKTSTPKKEGLAPpspslVSDLLSEL--NISEIQKLkqqlmqmeREKAGLLATLQDTQKQlehtrgSLSEQQEK 386
Cdd:PRK02224 575 AELNSKLAELKERIESLER-----IRTLLAAIadAEDEIERL--------REKREALAELNDERRE------RLAEKRER 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 387 VTRLTENLSALRRLQASKERQTALD-----NEKDRDSHEDGDYYEVDINGPEilackyhVAVAEAGELREQLKALRSTHE 461
Cdd:PRK02224 636 KRELEAEFDEARIEEAREDKERAEEyleqvEEKLDELREERDDLQAEIGAVE-------NELEELEELRERREALENRVE 708
|
....*...
gi 119583233 462 AREAQHAE 469
Cdd:PRK02224 709 ALEALYDE 716
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
634-813 |
3.93e-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: 40.81 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 634 IRDQIKHLQAA--VDRTTELSRQRIASQElgpavdkDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANL 711
Cdd:TIGR02168 218 LKAELRELELAllVLRLEELREELEELQE-------ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 712 KSKYeNEKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLA 791
Cdd:TIGR02168 291 YALA-NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
170 180
....*....|....*....|..
gi 119583233 792 LTQRLELLELDHEQTRRGRAKA 813
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQL 391
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
24-269 |
4.22e-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: 40.87 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 24 AEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREESL 103
Cdd:pfam15921 618 AKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKL 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 104 IQESASKeqyyvrkvlelQTELKQLRNVLTNTQSENERLASVAQELKeinQNVEIQRGRLRDDIKEYKFREARLLQDYSE 183
Cdd:pfam15921 698 KMQLKSA-----------QSELEQTRNTLKSMEGSDGHAMKVAMGMQ---KQITAKRGQIDALQSKIQFLEEAMTNANKE 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 184 ---LEEENISLQKQVSVL--RQNQV--EFEGLKHEIKRLEEETEYLNSQLEDAirlkeisERQLEEALETLktEREQKNS 256
Cdd:pfam15921 764 khfLKEEKNKLSQELSTVatEKNKMagELEVLRSQERRLKEKVANMEVALDKA-------SLQFAECQDII--QRQEQES 834
|
250
....*....|...
gi 119583233 257 LRKELSHYMSIND 269
Cdd:pfam15921 835 VRLKLQHTLDVKE 847
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
22-261 |
4.55e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 22 LRAEVKRLSHELA--ETTREKIQAAEYGLA-VLEEKHQLKLQFEELEVDYEAIRSEMEQLKEafgqahtnHKKVAADGES 98
Cdd:PRK03918 174 IKRRIERLEKFIKrtENIEELIKEKEKELEeVLREINEISSELPELREELEKLEKEVKELEE--------LKEEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 99 REESLIQESASkeqyyvrkvleLQTELKQLRNVLTNTQSENERLASVAQELKEINQNVE--IQRGRLRDDIKEYKFREAR 176
Cdd:PRK03918 246 ELESLEGSKRK-----------LEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEeyIKLSEFYEEYLDELREIEK 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 177 LLQDYSE----LEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTERE 252
Cdd:PRK03918 315 RLSRLEEeingIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE 394
|
....*....
gi 119583233 253 QKNSLRKEL 261
Cdd:PRK03918 395 ELEKAKEEI 403
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
5-258 |
5.13e-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: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 5 SEEEEYARLVMEAQPEWLR---AEVKRLSHELAETTREKIQAAEYGLAVLEekHQLKLQFEELEVDYEAIRsemEQLKEA 81
Cdd:pfam12128 638 SREETFARTALKNARLDLRrlfDEKQSEKDKKNKALAERKDSANERLNSLE--AQLKQLDKKHQAWLEEQK---EQKREA 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 82 FGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKqlrNVLTNTQSENERLASVAQELKEINQNVEIQRG 161
Cdd:pfam12128 713 RTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYK---RDLASLGVDPDVIAKLKREIRTLERKIERIAV 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 162 RlRDDIKEY-KFREARLLQdyseleeENISLQKQVSVLRQNQVEfegLKHEIKRLEEETEYLNSQLEDAIRLKEISERQL 240
Cdd:pfam12128 790 R-RQEVLRYfDWYQETWLQ-------RRPRLATQLSNIERAISE---LQQQLARLIADTKLRRAKLEMERKASEKQQVRL 858
|
250
....*....|....*...
gi 119583233 241 EEALETLKTEREQKNSLR 258
Cdd:pfam12128 859 SENLRGLRCEMSKLATLK 876
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
105-414 |
5.52e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.81 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 105 QESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQ----------ELKEINQNVEIQRGRLRDDIKEYKFRE 174
Cdd:TIGR01612 1499 KDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKtkkdseiiikEIKDAHKKFILEAEKSEQKIKEIKKEK 1578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 175 ARLLQDYSELEEEN---ISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQL--------EDAIRLKEISERQLEEA 243
Cdd:TIGR01612 1579 FRIEDDAAKNDKSNkaaIDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKIssfsidsqDTELKENGDNLNSLQEF 1658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 244 LETLKTEREQKNSLRKELSHYMSINDSFytshlhvsldglkfsddaaepNNDAEALVNGFEHGGLAKLPLDNKTSTPKKE 323
Cdd:TIGR01612 1659 LESLKDQKKNIEDKKKELDELDSEIEKI---------------------EIDVDQHKKNYEIGIIEKIKEIAIANKEEIE 1717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 324 GLAPPSPSLVSDLLSELNI----------------SEIQKLKQQLMQMEREKAGLLATLqdtqkqlehTRGSLSEQQEKV 387
Cdd:TIGR01612 1718 SIKELIEPTIENLISSFNTndlegidpnekleeynTEIGDIYEEFIELYNIIAGCLETV---------SKEPITYDEIKN 1788
|
330 340
....*....|....*....|....*..
gi 119583233 388 TRLTENLSALRRLQASKERQTALDNEK 414
Cdd:TIGR01612 1789 TRINAQNEFLKIIEIEKKSKSYLDDIE 1815
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
17-247 |
5.71e-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: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 17 AQPEWLRAEVKRLSHELAETtREKIQAAEYGLAVLEEkhqLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHkkvaadg 96
Cdd:COG4913 654 AEYSWDEIDVASAEREIAEL-EAELERLDASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGRLEKEL------- 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 97 ESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREAR 176
Cdd:COG4913 723 EQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPA 802
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119583233 177 LLQDYSELEEENISLQKQVSVLRQN-----QVEFEGLKHEikRLEEETEYLNSQLEDAIRlkEISER--QLEEALETL 247
Cdd:COG4913 803 ETADLDADLESLPEYLALLDRLEEDglpeyEERFKELLNE--NSIEFVADLLSKLRRAIR--EIKERidPLNDSLKRI 876
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
350-537 |
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 119583233 350 QQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTEnLSALRRLQASKERQTALDNEKDRdsHEDgdyyEVDI 429
Cdd:COG4913 241 HEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRL-WFAQRRLELLEAELEELRAELAR--LEA----ELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 430 NGPEILACKYHVAVAEA------GELREQLKALRSTHEAREAQHAEEKGRYEAEGQALTEKVSL----LEKASRQDRELL 499
Cdd:COG4913 314 LEARLDALREELDELEAqirgngGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAsaeeFAALRAEAAALL 393
|
170 180 190
....*....|....*....|....*....|....*...
gi 119583233 500 ARLEKELKKVSDVAGETQGSLSVAQDELVTFSEELANL 537
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
22-513 |
7.71e-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: 40.21 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 22 LRAEVKRLSHELA---ETTREKIQAAEYGLAVLEEKHQ--LKLQFEELEVDYE---AIRSEMEQLKEAFGQAHTNHKKVA 93
Cdd:pfam12128 295 LDDQWKEKRDELNgelSAADAAVAKDRSELEALEDQHGafLDADIETAAADQEqlpSWQSELENLEERLKALTGKHQDVT 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 94 ADGESREESLiqesaskeqyyvrkVLELQTELKQLRNVLTNTQSENERLASVA-----QELKEINQNVEIQRGRLRDDIK 168
Cdd:pfam12128 375 AKYNRRRSKI--------------KEQNNRDIAGIKDKLAKIREARDRQLAVAeddlqALESELREQLEAGKLEFNEEEY 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 169 EYKFR--EARLLQDYSELEEENIsLQKQVSVLRQN--QVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEAL 244
Cdd:pfam12128 441 RLKSRlgELKLRLNQATATPELL-LQLENFDERIEraREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQ 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 245 ETLKTEREQKNSLRKELSHYMSINDSFYTSHLHVSLDGLKFSDDAAEPNNDAEALVNGFEHGGLaKLPLDNKTstpkkeg 324
Cdd:pfam12128 520 SALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGV-KLDLKRID------- 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 325 lAPPSPSLVSDLLSELNISE--IQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSAL----- 397
Cdd:pfam12128 592 -VPEWAASEEELRERLDKAEeaLQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEkdkkn 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 398 ----RRLQASKERQTALDNEKDRDSHEDGDYYE-VDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEE-- 470
Cdd:pfam12128 671 kalaERKDSANERLNSLEAQLKQLDKKHQAWLEeQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAElk 750
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 119583233 471 --KGRYEAEGQALTEKVSLLEKASRQDRELLARLEKELKKVSDVA 513
Cdd:pfam12128 751 alETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVL 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
346-538 |
8.74e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 346 QKLKQQLMqmEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSALR-RLQASKERQTALDNEKDRDSHEdgdy 424
Cdd:COG1196 216 RELKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEaELEELRLELEELELELEEAQAE---- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583233 425 yevdingpeilackYHVAVAEAGELREQLKALrsthEAREAQHAEEKGRYEAEGQALTEKVSLLEKASRQDRELLARLEK 504
Cdd:COG1196 290 --------------EYELLAELARLEQDIARL----EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190
....*....|....*....|....*....|....
gi 119583233 505 ELKKVSDVAGETQGSLSVAQDELVTFSEELANLY 538
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
|
| |
