|
Name |
Accession |
Description |
Interval |
E-value |
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
110-828 |
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: 1056.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 110 GQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGR 189
Cdd:pfam09730 1 GQSVSSHKKVAADGESREESLLQESASKEAYYAQRILELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 190 LRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEE 269
Cdd:pfam09730 81 MRDEIKEYKVREARLLQDYSELEEENISLQKQVSVLKQNQVEFEGLKHEITRKEEETELLNSQLEEAIRLREIAERQLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 270 ALETLKTEREQKNSLRKELSHYMSINDSFYTSHLHVSLDGLKFSDD---AAEPNNDAEALvNGFEHG--GLAKLPLDNKT 344
Cdd:pfam09730 161 ALETLKTEREQKNSLRKELSHYMTLNDFDYVSHLSISLDGLKFSEDegaGTEPNNDGEAM-DGGENGggGLKNSGLDNRT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 345 STPKKEGLAPPSPSLVSDLLSELNISEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSAL 424
Cdd:pfam09730 240 STPRKSEVFPPAPSLVSDLLSELNISEIQKLKQQLIQVEREKVSLLSTLQESQKQLEQAKGALSEQQEKVNRLTENLEAM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 425 RRLQASKERQTALDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAE 504
Cdd:pfam09730 320 RGLQASKERQDALDSEKDRDSHEDGDYYEVDINGPEILECKYRVAVEEAGELREELKALKARYNTLEERYKEEKTRWEAE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 505 GQALTEKVSLLEKASRQDRELLARLEKELKKVSDVAGETQGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYY 584
Cdd:pfam09730 400 AQDLAEKIRQLEKASHQDQERIAHLEKELGKTRKVAGESEGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYY 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 585 REGQGGAGRtspggRTSPEARGRRSPILLPKGLLAPEAGRADGGtGDSSPSPGSSLPSPLSDPRREPMNIYNLIAIIRDQ 664
Cdd:pfam09730 480 REGAGARAR-----KSHQEPRGLRSPRLLTRGLFMGEVGTADTT-SNSPSPCSSCPGSPTSDFRREPMNIYNLVAIIRDQ 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 665 IKHLQAAVDRTTELSRQRIASQELGPAVDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSKYEN 744
Cdd:pfam09730 554 IKHLQVAVDRTTELSRQRGAALELSTESDKDKEALMEEILKLKSLLSTKREQIATLRTVLKANKQTAEVALANLKSKYEN 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 745 EKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLE 824
Cdd:pfam09730 634 EKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLE 713
|
....
gi 1034664654 825 LLEL 828
Cdd:pfam09730 714 DLEF 717
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
22-562 |
2.42e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 22 LRAEVKRLSHELAETTREKIQAAEYGLAvlEEKHQLKLQFEELEVDYEAIRSEMEQLKEVSRAAlpcdprpapgpvgvvp 101
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELE--AELEELEAELEELEAELAELEAELEELRLELEEL---------------- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 102 gTRAAKAFGQAHTNHKKVAADGESREESLIQESASKEQyyvrKVLELQTELKQLRNVLTNTQSE----NERLASVAQELK 177
Cdd:COG1196 280 -ELELEEAQAEEYELLAELARLEQDIARLEERRRELEE----RLEELEEELAELEEELEELEEEleelEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 178 EINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAI 257
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 258 RLKEISERQLEEALETLKTEREQKNSLRKELShymsiNDSFYTSHLHVSLDGLKFSDDAAEPN----NDAEALVNGFEHG 333
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLA-----ELLEEAALLEAALAELLEELAEAAARllllLEAEADYEGFLEG 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 334 GLAKLPLDNKTSTPKKEGLAPPSPSLVSD--------LLSELNISEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRG 405
Cdd:COG1196 510 VKAALLLAGLRGLAGAVAVLIGVEAAYEAaleaalaaALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALA 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 406 SLSEQ--QEKVTRLTENLSALRRLQASKERQTALDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGEL-REQLKA 482
Cdd:COG1196 590 AALARgaIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLtGGSRRE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 483 LRSTHEAREAQHAEEKGRYEAEGQALTEKVSLLEKASRQDRELLARLEKELKKVSDVAGETQGSLSVAQDELVTFSEELA 562
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6-291 |
2.57e-08 |
|
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: 57.76 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 6 EEEEYARLVMEAQPEWLRAEVKRLSHELAETTREkIQAAEYGLAVLEEKH-QLKLQFEELEVDYEAIRSEMEQLK-EVSR 83
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEE-LEELTAELQELEEKLeELRLEVSELEEEIEELQKELYALAnEISR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 84 AalpcdprpapgpvgvvpgtraaKAFGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQ 163
Cdd:TIGR02168 300 L----------------------EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 164 SENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQ--VEFEGLKHEIKR 241
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeeLLKKLEEAELKE 437
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1034664654 242 LEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKELSHY 291
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL 487
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
23-289 |
9.27e-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: 52.75 E-value: 9.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 23 RAEVKRLSHELAETTrEKIQAAEYGLAVLEEkhqlklQFEELEVDYEAIRSEMEQLKEVSRAAlpcdprpapgpvgvvpg 102
Cdd:TIGR02168 676 RREIEELEEKIEELE-EKIAELEKALAELRK------ELEELEEELEQLRKELEELSRQISAL----------------- 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 103 traaKAFGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQN 182
Cdd:TIGR02168 732 ----RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 183 VEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQvsvLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEI 262
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ---IEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
250 260
....*....|....*....|....*..
gi 1034664654 263 SERQLEEALETLKTEREQKNSLRKELS 289
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRS 911
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
124-564 |
3.21e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 124 ESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDdiKEYKFREAR 203
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK--LEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 204 LLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIR-LKEISERQLEEALETLKTEREQKN 282
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEELQQRLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 283 SLRKELSHYMSINDSfytshLHVSLDGLKFSDDAAEPNNDAEALVNGFEHGGLAKLPLDNKTSTPKKEGLAPPSPSLVSD 362
Cdd:COG4717 210 ELEEELEEAQEELEE-----LEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 363 LLseLNISEIQKLKQQLMQMEREKAGLLATLQD-TQKQLEHTRGSLS-EQQEKVTRLTENLSALRRLQASKERQTALDNE 440
Cdd:COG4717 285 LL--ALLFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 441 KDRDSHED---GDYYEVDINGPEIL------ACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEkgRYEAEGQALTEK 511
Cdd:COG4717 363 LQLEELEQeiaALLAEAGVEDEEELraaleqAEEYQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEE 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1034664654 512 VSLLEKASRQDRELLARLEKELKKVsdvagETQGSLSVAQDELVTFSEELANL 564
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQL-----EEDGELAELLQELEELKAELREL 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
114-840 |
3.70e-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: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 114 TNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSE----NERLASVAQELKEINQNVEIQRGR 189
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEieelQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 190 LRDDIKEYKFREARLLQDYS----------ELEEENISLQKqvsvlrqnqvEFEGLKHEIKRLEEETEYLNSQLEDAirl 259
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESkldelaeelaELEEKLEELKE----------ELESLEAELEELEAELEELESRLEEL--- 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 260 keisERQLEEALETLKTEREQKNSLRKELShymsindsfytshlhvSLDGLKFSDDAAEPNNDAEalvngfehgglaklp 339
Cdd:TIGR02168 378 ----EEQLETLRSKVAQLELQIASLNNEIE----------------RLEARLERLEDRRERLQQE--------------- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 340 ldnktstpkkeglappspslVSDLLSELNISEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTE 419
Cdd:TIGR02168 423 --------------------IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 420 NLSALRRLQASKERQ------------TALDNEKDRDSHED--GDYYEVDingpeilaCKYHVAVAEAGELREQLKALRS 485
Cdd:TIGR02168 483 ELAQLQARLDSLERLqenlegfsegvkALLKNQSGLSGILGvlSELISVD--------EGYEAAIEAALGGRLQAVVVEN 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 486 THEAREAQhaeekgryEAEGQALTEKVSLLEKASRQDRELLARLEKELKKVSDVAGetqgslsvAQDELVTFSEE----L 561
Cdd:TIGR02168 555 LNAAKKAI--------AFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLG--------VAKDLVKFDPKlrkaL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 562 ANLYHHVCMCNNETPNRVMLDYYREGQG----GAGRTSPGGRTSPEARGRRSPILLPKGLLAPEAGRADGGTGDSS---- 633
Cdd:TIGR02168 619 SYLLGGVLVVDDLDNALELAKKLRPGYRivtlDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAelek 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 634 ------------PSPGSSLPSPLSDPRREPMNIYNLIAIIRDQIKHLQAAVDRT-----------TELSRQRIASQELGP 690
Cdd:TIGR02168 699 alaelrkeleelEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLskelteleaeiEELEERLEEAEEELA 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 691 AVDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSkYENEKAMVTETMMKLRNELKALKEDAATF 770
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES-LERRIAATERRLEDLEEQIEELSEDIESL 857
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034664654 771 SSLRAMFATRCDEYITQLDE-------MQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLELLELDHEQTRRGRAKA 840
Cdd:TIGR02168 858 AAEIEELEELIEELESELEAllnerasLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
370-564 |
8.88e-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: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 370 SEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSALRRLQASKERQTALDNEKDRDSHEDG 449
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 450 dyyevdingpEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAEGQALTEKVSLLEKASRQDRELLARL 529
Cdd:COG1196 347 ----------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
170 180 190
....*....|....*....|....*....|....*
gi 1034664654 530 EKELKKVSDVAGETQGSLSVAQDELVTFSEELANL 564
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
117-442 |
8.95e-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: 49.67 E-value: 8.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 117 KKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNT-QSENERLASVAQELKEINQNVEIQRGRLRDDIK 195
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEiEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 196 EYKFREARLLQDYSELEEENISLQKQVSVLRQNQ-------VEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLE 268
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLErriaateRRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 269 EALETLKTEREQKNSLRKELshymsindsfytshlhvsldglkfsDDAAEPNNDAEALVNGFEHgglAKLPLDNKTSTpk 348
Cdd:TIGR02168 877 ALLNERASLEEALALLRSEL-------------------------EELSEELRELESKRSELRR---ELEELREKLAQ-- 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 349 keglappspslvsdllSELNISEIQKLKQQLMQMEREKAGLlaTLQDTQKQLEHTRGSLSEQQEKVTRLTE--------N 420
Cdd:TIGR02168 927 ----------------LELRLEGLEVRIDNLQERLSEEYSL--TLEEAEALENKIEDDEEEARRRLKRLENkikelgpvN 988
|
330 340
....*....|....*....|..
gi 1034664654 421 LSALRRLQASKERQTALDNEKD 442
Cdd:TIGR02168 989 LAAIEEYEELKERYDFLTAQKE 1010
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
136-288 |
2.66e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.79 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 136 SKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEEN 215
Cdd:pfam05483 464 TSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKE 543
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034664654 216 ISLQKQVSVLRQnqvEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKEL 288
Cdd:pfam05483 544 MNLRDELESVRE---EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEEL 613
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
127-291 |
4.62e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.38 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 127 EESLIQESASKEQYYVRKVLELQTELKQLRnvltntqsenerlaSVAQELKEINQNVEIQRGRLRDDIKEYKfreaRLLQ 206
Cdd:COG5022 938 NNIDLEEGPSIEYVKLPELNKLHEVESKLK--------------ETSEEYEDLLKKSTILVREGNKANSELK----NFKK 999
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 207 DYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQ--LEDAIRLKEISERQLEEALETLKTEREqkNSL 284
Cdd:COG5022 1000 ELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILkpLQKLKGLLLLENNQLQARYKALKLRRE--NSL 1077
|
....*..
gi 1034664654 285 RKELSHY 291
Cdd:COG5022 1078 LDDKQLY 1084
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
370-535 |
4.69e-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: 45.69 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 370 SEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSALR-RLQASKERQTALDNEKDRDSHED 448
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEaRIKKYEEQLGNVRNNKEYEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 449 gdyyEVDINGPEILACKYHV--AVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAEGQALTEKVSLLEKASrqdRELL 526
Cdd:COG1579 97 ----EIESLKRRISDLEDEIleLMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER---EELA 169
|
....*....
gi 1034664654 527 ARLEKELKK 535
Cdd:COG1579 170 AKIPPELLA 178
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
143-280 |
4.84e-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: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 143 RKVLELQTELKQLRNVLTNTQSENERLASVAQELKeinqnveiQRGRLRDDIKEYKFREarllQDYSELEEENISLQKQV 222
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQ--------ERREALQRLAEYSWDE----IDVASAEREIAELEAEL 677
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034664654 223 SVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQ 280
Cdd:COG4913 678 ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
5-291 |
7.28e-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: 46.60 E-value: 7.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 5 SEEEEYARLVMEAQPEWLRAEVKRLSHELaETTREKIQAAEYGLAVLE-EKHQLKLQFEELEVDYEAIRSEMEQLKevsr 83
Cdd:TIGR02169 204 RREREKAERYQALLKEKREYEGYELLKEK-EALERQKEAIERQLASLEeELEKLTEEISELEKRLEEIEQLLEELN---- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 84 aalpcdprpapgpvgvvpgtraakafgqahtnhKKVAADGESREESL---IQESASKEQYYVRKVLELQTELKQLRNVLT 160
Cdd:TIGR02169 279 ---------------------------------KKIKDLGEEEQLRVkekIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 161 NTQSENERLASVAQELKEinqNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEI- 239
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELER---EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIn 402
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034664654 240 -------------KRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKELSHY 291
Cdd:TIGR02169 403 elkreldrlqeelQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
371-538 |
1.12e-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: 45.53 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 371 EIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSALRR----LQASKERQTA---------- 436
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKeiaeLRAELEAQKEelaellraly 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 437 -----------LDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAEG 505
Cdd:COG4942 115 rlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190
....*....|....*....|....*....|...
gi 1034664654 506 QALTEKVSLLEKASRQDRELLARLEKELKKVSD 538
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
145-539 |
1.97e-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: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 145 VLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVsv 224
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI-- 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 225 lRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKELShymsindsfytshlh 304
Cdd:TIGR02168 750 -AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT--------------- 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 305 vsldglKFSDDAAEPNNDAEALVNgfehgglaklpldnktstpkkeglappspslvsdllselnisEIQKLKQQLMQMER 384
Cdd:TIGR02168 814 ------LLNEEAANLRERLESLER------------------------------------------RIAATERRLEDLEE 845
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 385 EKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSAL-RRLQASKERQTALDNEKDRDSHEDGDyyevdingpeila 463
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLeEALALLRSELEELSEELRELESKRSE------------- 912
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 464 ckyhvAVAEAGELREQLKALRSTHEAREAQHAEEKGR----YEAEGQALTEKVSLLEKASRQDRELLARLEKELKKVSDV 539
Cdd:TIGR02168 913 -----LRRELEELREKLAQLELRLEGLEVRIDNLQERlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPV 987
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
140-292 |
2.40e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 140 YYVRKVLeLQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGR------LRDDIKEYKFREARLLQDYSELEE 213
Cdd:PRK12704 22 YFVRKKI-AEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRnefekeLRERRNELQKLEKRLLQKEENLDR 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034664654 214 ENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDaiRLKEISERQLEEALETLKTEREQKnsLRKELSHYM 292
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ--ELERISGLTAEEAKEILLEKVEEE--ARHEAAVLI 175
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
148-326 |
6.52e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.35 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 148 LQTELKQLRNVLTNTQSENERLASVAQE-LKEINQNVEIQRGRLRDDIKEYkfreARLLQDYSELEEENISLQ---KQVS 223
Cdd:PLN02939 269 LDASLRELESKFIVAQEDVSKLSPLQYDcWWEKVENLQDLLDRATNQVEKA----ALVLDQNQDLRDKVDKLEaslKEAN 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 224 VLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREqknslRKELSHYMSINDSFYTSHL 303
Cdd:PLN02939 345 VSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESK-----KRSLEHPADDMPSEFWSRI 419
|
170 180
....*....|....*....|...
gi 1034664654 304 HVSLDGlkFSDDAAEPNNDAEAL 326
Cdd:PLN02939 420 LLLIDG--WLLEKKISNNDAKLL 440
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6-561 |
6.68e-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: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 6 EEEEYARLVMEAQPEWLRAEVKRLSHELAETTREKIQAAEyglavleEKHQLKLQFEELEVDYEAIRSEMEQLKEVSraa 85
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE-------RLANLERQLEELEAQLEELESKLDELAEEL--- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 86 lpcdprpapgpvgvvpgTRAAKAFGQAHTNHKKVAADGEsREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSE 165
Cdd:TIGR02168 340 -----------------AELEEKLEELKEELESLEAELE-ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 166 NERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARllqdySELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEE 245
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ-----AELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 246 TEYLNSQLEDAIRLKEISERQLE------EALETLKTEREQKNSLRKELSHYMSInDSFYTSHLHVSLDGLK---FSDDA 316
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQEnlegfsEGVKALLKNQSGLSGILGVLSELISV-DEGYEAAIEAALGGRLqavVVENL 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 317 AEPNNDAEALVNGfEHGGLAKLPLD---------NKTSTPKKEG-----------LAPPSPSLVSDLLSELNI------- 369
Cdd:TIGR02168 556 NAAKKAIAFLKQN-ELGRVTFLPLDsikgteiqgNDREILKNIEgflgvakdlvkFDPKLRKALSYLLGGVLVvddldna 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 370 ------------------------------------------SEIQKLKQQLMQMEREKAGLLATLQDTQKQLE----HT 403
Cdd:TIGR02168 635 lelakklrpgyrivtldgdlvrpggvitggsaktnssilerrREIEELEEKIEELEEKIAELEKALAELRKELEeleeEL 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 404 RGSLSEQQEKVTRLTENLSALRRLQASKERQTALDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKAL 483
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034664654 484 RSTHEAREAQHAEEKGRYEAEGQALTEKVSLLEKASRQDRELLARLEkELKKVSDVAGETQGSLSVAQDELVTFSEEL 561
Cdd:TIGR02168 795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE-DLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
125-288 |
7.14e-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: 43.52 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 125 SREESLIQESASKEQYYVRKVLELQTELKQLrnvLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARL 204
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQL---EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 205 LQdySELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSL 284
Cdd:TIGR02169 775 HK--LEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852
|
....
gi 1034664654 285 RKEL 288
Cdd:TIGR02169 853 EKEI 856
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
124-298 |
9.53e-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: 9.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 124 ESREESLIQESASKEQyyvrKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREAR 203
Cdd:TIGR02169 853 EKEIENLNGKKEELEE----ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 204 LLQDYSELEEENISLQKQVSvlrqNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISER---QLEEALETLKTER-- 278
Cdd:TIGR02169 929 LEEELSEIEDPKGEDEEIPE----EELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKrldELKEKRAKLEEERka 1004
|
170 180
....*....|....*....|....*..
gi 1034664654 279 -----EQKNSLRKE--LSHYMSINDSF 298
Cdd:TIGR02169 1005 ileriEEYEKKKREvfMEAFEAINENF 1031
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
15-274 |
1.20e-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: 42.74 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 15 MEAQPEWLRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEVSRAAlpcdprpap 94
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL--------- 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 95 gpvgvvpgTRAAKAFGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVL------------------------ELQT 150
Cdd:TIGR02168 802 --------REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEqieelsedieslaaeieeleelieELES 873
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 151 ELKQLRNVLTNTQSE----NERLASVAQELKEINQNV---EIQRGRLRDDIKEYKFREARLLQDYSEL-----EEENISL 218
Cdd:TIGR02168 874 ELEALLNERASLEEAlallRSELEELSEELRELESKRselRRELEELREKLAQLELRLEGLEVRIDNLqerlsEEYSLTL 953
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034664654 219 QKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAI-RLKEISERQ---------LEEALETL 274
Cdd:TIGR02168 954 EEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIeEYEELKERYdfltaqkedLTEAKETL 1019
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
370-564 |
1.27e-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: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 370 SEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSAL--------RRLQASKERQTALDNEK 441
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALeqelaaleAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 442 DRDSHEDGD-----YYEVDINGPEILackyhVAVAEAGELREQLKALRSTHEAREAQHAEekgrYEAEGQALTEKVSLLE 516
Cdd:COG4942 100 EAQKEELAEllralYRLGRQPPLALL-----LSPEDFLDAVRRLQYLKYLAPARREQAEE----LRADLAELAALRAELE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1034664654 517 KASRQDRELLARLEKELKKVSDVAGETQGSLSVAQDELVTFSEELANL 564
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
147-288 |
1.64e-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: 41.93 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 147 ELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLR 226
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034664654 227 QnqvEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKEL 288
Cdd:TIGR04523 433 E---TIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
147-290 |
2.11e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.65 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 147 ELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLlqdySELEEEnISLQKQ----V 222
Cdd:pfam05557 115 ELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRI----KELEFE-IQSQEQdseiV 189
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034664654 223 SVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISErQLEEALETLKTEREQKNSLRKELSH 290
Cdd:pfam05557 190 KNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVE-DLKRKLEREEKYREEAATLELEKEK 256
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
143-288 |
2.23e-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: 40.68 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 143 RKVLELQTELKQLRNVLTNTQsenERLASVAQELKEINQNVEIQRGRLRDDikEYKFREARLLQDYSELEEENISLQKQV 222
Cdd:COG1579 31 AELAELEDELAALEARLEAAK---TELEDLEKEIKRLELEIEEVEARIKKY--EEQLGNVRNNKEYEALQKEIESLKRRI 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034664654 223 SVLRQNQVEFEglkHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKEL 288
Cdd:COG1579 106 SDLEDEILELM---ERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
132-441 |
2.99e-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: 41.58 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 132 QESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQ----------ELKEINQNVEIQRGRLRDDIKEYKFRE 201
Cdd:TIGR01612 1499 KDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKtkkdseiiikEIKDAHKKFILEAEKSEQKIKEIKKEK 1578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 202 ARLLQDYSELEEEN---ISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQL--------EDAIRLKEISERQLEEA 270
Cdd:TIGR01612 1579 FRIEDDAAKNDKSNkaaIDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKIssfsidsqDTELKENGDNLNSLQEF 1658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 271 LETLKTEREQKNSLRKELSHYMSINDSFytshlhvsldglkfsddaaepNNDAEALVNGFEHGGLAKLPLDNKTSTPKKE 350
Cdd:TIGR01612 1659 LESLKDQKKNIEDKKKELDELDSEIEKI---------------------EIDVDQHKKNYEIGIIEKIKEIAIANKEEIE 1717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 351 GLAPPSPSLVSDLLSELNI----------------SEIQKLKQQLMQMEREKAGLLATLqdtqkqlehTRGSLSEQQEKV 414
Cdd:TIGR01612 1718 SIKELIEPTIENLISSFNTndlegidpnekleeynTEIGDIYEEFIELYNIIAGCLETV---------SKEPITYDEIKN 1788
|
330 340
....*....|....*....|....*..
gi 1034664654 415 TRLTENLSALRRLQASKERQTALDNEK 441
Cdd:TIGR01612 1789 TRINAQNEFLKIIEIEKKSKSYLDDIE 1815
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
661-840 |
3.84e-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: 41.20 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 661 IRDQIKHLQAA--VDRTTELSRQRIASQElgpavdkDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANL 738
Cdd:TIGR02168 218 LKAELRELELAllVLRLEELREELEELQE-------ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 739 KSKYeNEKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLA 818
Cdd:TIGR02168 291 YALA-NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
170 180
....*....|....*....|..
gi 1034664654 819 LTQRLELLELDHEQTRRGRAKA 840
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQL 391
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
125-289 |
4.50e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 125 SREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARl 204
Cdd:TIGR02169 719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQ- 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 205 lQDYSELEEENISLQKQVSVLRQN------------------QVEFEGLKHEIKRLEEETEYLNSQLED---AIRLKEIS 263
Cdd:TIGR02169 798 -AELSKLEEEVSRIEARLREIEQKlnrltlekeylekeiqelQEQRIDLKEQIKSIEKEIENLNGKKEEleeELEELEAA 876
|
170 180
....*....|....*....|....*.
gi 1034664654 264 ERQLEEALETLKTEREQknsLRKELS 289
Cdd:TIGR02169 877 LRDLESRLGDLKKERDE---LEAQLR 899
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
124-535 |
5.48e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 124 ESREESLIQESASKEQyyVRKVLELQTELKQLRNVLtntQSENERLASVAQELKEInQNVEIQRGRLRDDIKEYKFREAR 203
Cdd:COG4717 108 EAELEELREELEKLEK--LLQLLPLYQELEALEAEL---AELPERLEELEERLEEL-RELEEELEELEAELAELQEELEE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 204 LLQDYSELEEENIS-----LQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLkter 278
Cdd:COG4717 182 LLEQLSLATEEELQdlaeeLEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAA---- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 279 eqknslrkeLSHYMSINDSFYTSHLHV-----------SLDGLKFSDDAAEPNNDAEALVNGFEHGGLAKLPLDnktSTP 347
Cdd:COG4717 258 ---------LLALLGLGGSLLSLILTIagvlflvlgllALLFLLLAREKASLGKEAEELQALPALEELEEEELE---ELL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 348 KKEGLAPP-SPSLVSDLLSElnISEIQKLKQQLMQMEREKAglLATLQDTQKQLEHTRGSLSEQQekvtrLTENLSALRR 426
Cdd:COG4717 326 AALGLPPDlSPEELLELLDR--IEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVEDEEE-----LRAALEQAEE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 427 LQASKERQTALdnEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQ--HAEEKGRYEAE 504
Cdd:COG4717 397 YQELKEELEEL--EEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEleQLEEDGELAEL 474
|
410 420 430
....*....|....*....|....*....|....*..
gi 1034664654 505 GQALTEKVSLLEKASRQD------RELLARLEKELKK 535
Cdd:COG4717 475 LQELEELKAELRELAEEWaalklaLELLEEAREEYRE 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
377-564 |
5.68e-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: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 377 QQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTEnLSALRRLQASKERQTALDNEKDRdsHEDgdyyEVDI 456
Cdd:COG4913 241 HEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRL-WFAQRRLELLEAELEELRAELAR--LEA----ELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 457 NGPEILACKYHVAVAEA------GELREQLKALRSTHEAREAQHAEEKGRYEAEGQALTEKVSL----LEKASRQDRELL 526
Cdd:COG4913 314 LEARLDALREELDELEAqirgngGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAsaeeFAALRAEAAALL 393
|
170 180 190
....*....|....*....|....*....|....*...
gi 1034664654 527 ARLEKELKKVSDVAGETQGSLSVAQDELVTFSEELANL 564
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
22-277 |
6.82e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.05 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 22 LRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEvsraalpcdprpapgpvgvvp 101
Cdd:TIGR02169 707 LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA--------------------- 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 102 gtRAAKAFGQAHTNHKKVAADGESREESLIQESaskeqyyVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQ 181
Cdd:TIGR02169 766 --RIEELEEDLHKLEEALNDLEARLSHSRIPEI-------QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 182 NVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQnqvEFEGLKHEIKRLEEETEYLNS---QLEDAIR 258
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES---RLGDLKKERDELEAQLRELERkieELEAQIE 913
|
250
....*....|....*....
gi 1034664654 259 LKEISERQLEEALETLKTE 277
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEE 932
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
6-227 |
7.23e-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: 39.75 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 6 EEEEYARLVMEAQPEWLRAEVKRLSHELAETTReKIQAAEYGLAVLEEK-HQLKLQFEELEVDYEAIRSEMEQlkevsra 84
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALAR-RIRALEQELAALEAElAELEKEIAELRAELEAQKEELAE------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 85 alpcdprpapgpvgvvpgtRAAKAFGQAHTNHKKVAADGESreeslIQESASKEQYYVRKVLELQTELKQLRNVLTNTQS 164
Cdd:COG4942 109 -------------------LLRALYRLGRQPPLALLLSPED-----FLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034664654 165 ENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQ 227
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
125-288 |
7.29e-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: 39.75 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 125 SREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSE----NERLASVAQELKEINQNVEIQRGRLRDDIKE-YK- 198
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQElaalEAELAELEKEIAELRAELEAQKEELAELLRAlYRl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 199 ------------------FREARLLQDYSELEEENI-SLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRL 259
Cdd:COG4942 117 grqpplalllspedfldaVRRLQYLKYLAPARREQAeELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
|
170 180
....*....|....*....|....*....
gi 1034664654 260 KEISERQLEEALETLKTEREQKNSLRKEL 288
Cdd:COG4942 197 RQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
373-565 |
9.15e-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: 9.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 373 QKLKQQLMqmEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSALR-RLQASKERQTALDNEKDRDSHEdgdy 451
Cdd:COG1196 216 RELKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEaELEELRLELEELELELEEAQAE---- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664654 452 yevdingpeilackYHVAVAEAGELREQLKALrsthEAREAQHAEEKGRYEAEGQALTEKVSLLEKASRQDRELLARLEK 531
Cdd:COG1196 290 --------------EYELLAELARLEQDIARL----EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190
....*....|....*....|....*....|....
gi 1034664654 532 ELKKVSDVAGETQGSLSVAQDELVTFSEELANLY 565
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
|
| |
