|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
19-354 |
1.84e-14 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 78.22 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 19 KLQSLSRRLDELEEATKNLQRAEDELLDLQDKviqaegsdsstLAEIEVLRQRVL--KIEGKDEEIKRAEDlchtmkekl 96
Cdd:COG1196 187 NLERLEDLLEELEKQLEKLERQAEKAERYQEL-----------KAELRELELALLlaKLKELRKELEELEE--------- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 97 eEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTE 176
Cdd:COG1196 247 -ELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 177 QSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHM---RNASTFLERNDLRIEDGISSTLSS 253
Cdd:COG1196 326 EELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFealREELAELEAELAEIRNELEELKRE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 254 KESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNR 333
Cdd:COG1196 406 IESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSS 485
|
330 340
....*....|....*....|.
gi 1720408942 334 NRSLASQLEEIKLQVRKQKEL 354
Cdd:COG1196 486 LEARLDRLEAEQRASQGVRAV 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
14-351 |
2.28e-13 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 74.75 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 14 RHLRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVL-KIEGKDEEIKRAEDLCHTM 92
Cdd:COG1196 691 KSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEeELEELQERLEELEEELESL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 93 KEKLEEEENLTRELKSEIERLQKRmvdLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRL 172
Cdd:COG1196 771 EEALAKLKEEIEELEEKRQALQEE---LEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDEL 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 173 DKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQnkkmnrdhmrnastfLERNDLRIEDGISSTLS 252
Cdd:COG1196 848 EEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRE---------------LESELAELKEEIEKLRE 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 253 SKESKRKgsldyLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFE-----SLEE--ELKKMRAKNNDLQD 325
Cdd:COG1196 913 RLEELEA-----KLERLEVELPELEEELEEEYEDTLETELEREIERLEEEIEALGpvnlrAIEEyeEVEERYEELKSQRE 987
|
330 340
....*....|....*....|....*.
gi 1720408942 326 NYLTELNRNRSLASQLEEIKLQVRKQ 351
Cdd:COG1196 988 DLEEAKEKLLEVIEELDKEKRERFKE 1013
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
104-379 |
3.45e-13 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 73.98 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 104 RELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSEL 183
Cdd:COG1196 667 RELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEEL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 184 EKLKS---LTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDLRiedgISSTLSSKESKRKG 260
Cdd:COG1196 747 EELEEeleELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERR----LDALERELESLEQR 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 261 SLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFE----SLEEELKKMRAKNNDLQdnyltelNRNRS 336
Cdd:COG1196 823 RERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEaekeELEDELKELEEEKEELE-------EELRE 895
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1720408942 337 LASQLEEIKLQVRKQKELGNgDIEGEDAFLLGRGRHERTKLKG 379
Cdd:COG1196 896 LESELAELKEEIEKLRERLE-ELEAKLERLEVELPELEEELEE 937
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
7-356 |
1.12e-12 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 72.44 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 7 YKDAASNRHLRFKLQSLSRRLDELEEatkNLQRAEDELLDLQDKVIQAEGsdsstlaEIEVLRQRVLKIEGKDEEIKRAE 86
Cdd:COG1196 656 SRNKRSSLAQKRELKELEEELAELEA---QLEKLEEELKSLKNELRSLED-------LLEELRRQLEELERQLEELKREL 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 87 dlchtmkekleeeenltRELKSEIERLQKRmvdLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELE 166
Cdd:COG1196 726 -----------------AALEEELEQLQSR---LEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELE 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 167 SSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKmnrdhmrnastflERNDLRIEdg 246
Cdd:COG1196 786 EKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEE-------------KLDELEEE-- 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 247 ISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIK----HFESLEEELKKMRAKNND 322
Cdd:COG1196 851 LEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEklreRLEELEAKLERLEVELPE 930
|
330 340 350
....*....|....*....|....*....|....
gi 1720408942 323 LQDNYLTELNRNRSLASQlEEIKLQVRKQKELGN 356
Cdd:COG1196 931 LEEELEEEYEDTLETELE-REIERLEEEIEALGP 963
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
104-353 |
2.65e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.25 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 104 RELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSEL 183
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 184 EKLKSLTLSFVNERKYLNEKEKEN---EKIIKELTQ---------KLEQNKKMNRDHMRNASTFLERNDLRIEdGISSTL 251
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIeelEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEIN-GIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 252 SSKESKrKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHF--ESLEEELKKMRAKNNDLQDNYLT 329
Cdd:PRK03918 331 KELEEK-EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLtpEKLEKELEELEKAKEEIEEEISK 409
|
250 260
....*....|....*....|....
gi 1720408942 330 ELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:PRK03918 410 ITARIGELKKEIKELKKAIEELKK 433
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
3-353 |
2.16e-11 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 68.25 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 3 ELTNYKDAASNRHLRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLrqrvlkIEGKDEEI 82
Cdd:COG0419 217 KLEEIQEEQEEEELEQEIEALEERLAELEEEKERLEELKARLLEIESLELEALKIREEELRELERL------LEELEEKI 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 83 KRAEDLchtmkekleeeENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKV 162
Cdd:COG0419 291 ERLEEL-----------EREIEELEEELEGLRALLEELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLL 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 163 KELESS-EDRLDKTEQSLVSELE--------------KLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRD 227
Cdd:COG0419 360 EERLKElEERLEELEKELEKALErlkqleeaiqelkeELAELSAALEEIQEELEELEKELEELERELEELEEEIKKLEEQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 228 HMRNASTFLERNDLRIEDGISSTLSSK--ESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKH 305
Cdd:COG0419 440 INQLESKELMIAELAGAGEKCPVCGQElpEEHEKELLELYELELEELEEELSREKEEAELREEIEELEKELRELEEELIE 519
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720408942 306 --------FESLEEELKKMRAKNNDLQDNYL-TELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:COG0419 520 lleleealKEELEEKLEKLENLLEELEELKEkLQLQQLKEELRQLEDRLQELKELLE 576
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
19-356 |
2.50e-11 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 67.86 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 19 KLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDS---------STLAEIEVLRQRVLKIEGKDEEIKRAEDLC 89
Cdd:COG0419 418 ELEELERELEELEEEIKKLEEQINQLESKELMIAELAGAGEkcpvcgqelPEEHEKELLELYELELEELEEELSREKEEA 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 90 HTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLslNEERNLTKKISSELEMLRVKVKELESSE 169
Cdd:COG0419 498 ELREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEE--LKEKLQLQQLKEELRQLEDRLQELKELL 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 170 DRLDKTEQSLvSELEKLksltlsfvnerkylNEKEKENEKIIKELTQKLEQ-NKKMNRDHMRNASTFLERNDLRIEDgIS 248
Cdd:COG0419 576 EELRLLRTRK-EELEEL--------------RERLKELKKKLKELEERLSQlEELLQSLELSEAENELEEAEEELES-EL 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 249 STLSSKESKRKGSLDYLKQVEN---ETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQD 325
Cdd:COG0419 640 EKLNLQAELEELLQAALEELEEkveELEAEIRRELQRIENEEQLEEKLEELEQLEEELEQLREELEELLKKLGEIEQLIE 719
|
330 340 350
....*....|....*....|....*....|.
gi 1720408942 326 NYLTELNRNRSLASQLEEIKLQVRKQKELGN 356
Cdd:COG0419 720 ELESRKAELEELKKELEKLEKALELLEELRE 750
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
28-360 |
3.08e-11 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 67.82 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 28 DELEEATKNLQRAEDELLDLQDKviqaegsdsstlaeIEVLRQRVLKIEgkdEEIKRAEDlchtmkekleeeenlTRELK 107
Cdd:COG1196 172 ERKEEAERKLERTEENLERLEDL--------------LEELEKQLEKLE---RQAEKAER---------------YQELK 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 108 SEIERLQKRMV--DLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELEK 185
Cdd:COG1196 220 AELRELELALLlaKLKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEE 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 186 LKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMnrdhmrnastFLERNDLRIE-----DGISSTLSSKESKRKG 260
Cdd:COG1196 300 LEGEISLLRERLEELENELEELEERLEELKEKIEALKEE----------LEERETLLEEleqllAELEEAKEELEEKLSA 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 261 SLDYLKQVENETRDK-SENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLAS 339
Cdd:COG1196 370 LLEELEELFEALREElAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELE 449
|
330 340
....*....|....*....|.
gi 1720408942 340 QLEEIKLQVRKQKELGNGDIE 360
Cdd:COG1196 450 ELEEQLEELRDRLKELERELA 470
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
28-345 |
1.34e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 28 DELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLCHTMKEKLEEEENLTRELK 107
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 108 SEIERLQKRMVDLEKLEE------ALSRSKNEcsqlclSLNEERNLTK---KISSELEMLRVKVKELESSEDRLDKTEQS 178
Cdd:PRK03918 273 KEIEELEEKVKELKELKEkaeeyiKLSEFYEE------YLDELREIEKrlsRLEEEINGIEERIKELEEKEERLEELKKK 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 179 LvSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDLRIEDGISStLSSKESKR 258
Cdd:PRK03918 347 L-KELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE-LKKEIKEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 259 KGSLDYLKQVENET----RDKSENEKnrnqeDNKVKDLNQEIEKLKTQIKHFESLEEELKKmRAKNNDLQDNYLTELNRN 334
Cdd:PRK03918 425 KKAIEELKKAKGKCpvcgRELTEEHR-----KELLEEYTAELKRIEKELKEIEEKERKLRK-ELRELEKVLKKESELIKL 498
|
330
....*....|.
gi 1720408942 335 RSLASQLEEIK 345
Cdd:PRK03918 499 KELAEQLKELE 509
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
103-362 |
1.53e-10 |
|
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: 65.47 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 103 TRELKSEIERLQKRMVDLEKLEEAL----SRSKNECSQLCLSLNEERNLTKKISSELEML---RVKVKE-LESSEDRLDK 174
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLqselRRIENRLDELSQELSDASRKIGEIEKEIEQLeqeEEKLKErLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 175 TEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKkmnRDHMRNASTFLERNDLRIEDgISSTLSSK 254
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEI---QAELSKLEEEVSRIEARLRE-IEQKLNRL 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 255 ESKRKGSLDYLKQVENETRDKSENEKNRNQE----DNKVKDLNQEIEKLKTQIKHFES----LEEELKKMRAKNNDLQDN 326
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEienlNGKKEELEEELEELEAALRDLESrlgdLKKERDELEAQLRELERK 904
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1720408942 327 Y---LTELNRNRSLASQLEEiKLQVRKQ--KELGNGDIEGE 362
Cdd:TIGR02169 905 IeelEAQIEKKRKRLSELKA-KLEALEEelSEIEDPKGEDE 944
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
14-314 |
1.97e-10 |
|
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: 65.09 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 14 RHLRFKLQSLSRRLDELEEATKNLQ----RAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLC 89
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQselrRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 90 htmkekleeeENLTRELKSEIERLQKRmvdLEKLEEALSRSKNECSQLCLSLNEERnlTKKISSELEMLRVKVKELESSE 169
Cdd:TIGR02169 750 ----------EQEIENVKSELKELEAR---IEELEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 170 DRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEqnkKMNRDhmrnastfLERNDLRIEDgiss 249
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE---ELEEE--------LEELEAALRD---- 879
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720408942 250 tLSSKESKRKgsldylKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIkhfESLEEELK 314
Cdd:TIGR02169 880 -LESRLGDLK------KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL---EALEEELS 934
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
27-348 |
2.10e-10 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 65.12 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 27 LDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIegkDEEIKRAEdlchtmkekleeeenltrel 106
Cdd:COG1196 231 LAKLKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEEL---REELEELQ-------------------- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 107 kseiERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELEKL 186
Cdd:COG1196 288 ----EELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 187 KSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDLRIEDgISSTLSSKESKRKGSLDYLK 266
Cdd:COG1196 364 EEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLED-LKEELKELEAELEELQTELE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 267 QVENETrdkSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKL 346
Cdd:COG1196 443 ELNEEL---EELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGVYG 519
|
..
gi 1720408942 347 QV 348
Cdd:COG1196 520 PV 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
3-319 |
2.28e-10 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 64.74 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 3 ELTNYKDAASNRHLRFKLQSLSRRLDELEEATKNLQRAEDELL----DLQDKVIQAEGSDSSTLAEIEVLRQRVL----K 74
Cdd:COG1196 217 ELKAELRELELALLLAKLKELRKELEELEEELSRLEEELEELQeeleEAEKEIEELKSELEELREELEELQEELLelkeE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 75 IEGKDEEIKRAEDLCHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERnltkkiSSE 154
Cdd:COG1196 297 IEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKL------SAL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 155 LEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKmnrdhmrnast 234
Cdd:COG1196 371 LEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQT----------- 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 235 flERNDLRIEdgisstLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEdnkVKDLNQEIEKLKTQIKHFESLEEELK 314
Cdd:COG1196 440 --ELEELNEE------LEELEEQLEELRDRLKELERELAELQEELQRLEKE---LSSLEARLDRLEAEQRASQGVRAVLE 508
|
....*
gi 1720408942 315 KMRAK 319
Cdd:COG1196 509 ALESG 513
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-410 |
2.68e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 104 RELKSEIERLQKRM--VDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVS 181
Cdd:TIGR02168 216 KELKAELRELELALlvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 182 ELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQnkkmnrdhmrnastfLERNDLRIEDGISSTLSSKESkrkgs 261
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE---------------LAEELAELEEKLEELKEELES----- 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 262 ldyLKQVENETRDKSENEKNRNQE-DNKVKDLNQEIEKLKTQIkhfESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQ 340
Cdd:TIGR02168 356 ---LEAELEELEAELEELESRLEElEEQLETLRSKVAQLELQI---ASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 341 LEEIKLQvRKQKELGNGDIEGEDAfllgRGRHERTKLKGHGSEASVSKHTSRELSPQHKRERLRNREFAL 410
Cdd:TIGR02168 430 LEEAELK-ELQAELEELEEELEEL----QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
30-350 |
4.03e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 30 LEEATKNLQRAED---------ELLDLQDKV------IQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLCHTMKE 94
Cdd:TIGR02168 181 LERTRENLDRLEDilnelerqlKSLERQAEKaerykeLKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 95 KLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERnltKKISSELEMLRVKVKELESSEDRLDK 174
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL---ANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 175 TEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKmnrdhmRNASTFLERNDLRIEdgISSTLSSK 254
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS------KVAQLELQIASLNNE--IERLEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 255 ESKrKGSLDYLKQvENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRN 334
Cdd:TIGR02168 410 ERL-EDRRERLQQ-EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL 487
|
330
....*....|....*.
gi 1720408942 335 RSLASQLEEIKLQVRK 350
Cdd:TIGR02168 488 QARLDSLERLQENLEG 503
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
30-345 |
1.13e-09 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 62.47 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 30 LEEATKNLQRAEDELLDLQ--DKVIQAEGSDSSTL-AEIEVLRQRV-LKIEGKDEEIKRAED-LCHTMKEKLEEEENLTR 104
Cdd:COG0419 149 LKSKPKERKEILDELFGLEkyEKLSELLKEVIKEAkAKIEELEGQLsELLEDIEDLLEALEEeLKELKKLEEIQEEQEEE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 105 ELKSEIERLQKRMVDLEKLEEALSRSKNecsqlclslneerNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLvSELE 184
Cdd:COG0419 229 ELEQEIEALEERLAELEEEKERLEELKA-------------RLLEIESLELEALKIREEELRELERLLEELEEKI-ERLE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 185 KLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDhMRNASTFLERNDLRIEDGiSSTLSSKESKRKGSLDY 264
Cdd:COG0419 295 ELEREIEELEEELEGLRALLEELEELLEKLKSLEERLEKLEEK-LEKLESELEELAEEKNEL-AKLLEERLKELEERLEE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 265 L-KQVENETRDKSENEKNRNQEDNKVKDLNQEIEK----LKTQIKHFESLEEELKKMRAKNNDLQDnyltELNRNRSLAS 339
Cdd:COG0419 373 LeKELEKALERLKQLEEAIQELKEELAELSAALEEiqeeLEELEKELEELERELEELEEEIKKLEE----QINQLESKEL 448
|
....*.
gi 1720408942 340 QLEEIK 345
Cdd:COG0419 449 MIAELA 454
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
16-345 |
2.86e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 16 LRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGsDSSTLAEIEVLRQRV--LKIEGKDEEIKRAEDLCHTMK 93
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-RHELYEEAKAKKEELerLKKRLTGLTPEKLEKELEELE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 94 EKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSqLC---LSLNEERNLTKKISSELEMLRVKVKELESSED 170
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP-VCgreLTEEHRKELLEEYTAELKRIEKELKEIEEKER 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 171 RLDKTEQSLVSELEKLKSLTlsfvnerkylneKEKENEKIIKELTQKLeqnKKMNRDHMRNASTFLE--RNDLRIEDGIS 248
Cdd:PRK03918 477 KLRKELRELEKVLKKESELI------------KLKELAEQLKELEEKL---KKYNLEELEKKAEEYEklKEKLIKLKGEI 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 249 STLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNK-----VKDLNQEIE----------KLKTQIKHFESLEEEL 313
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfesVEELEERLKelepfyneylELKDAEKELEREEKEL 621
|
330 340 350
....*....|....*....|....*....|..
gi 1720408942 314 KKMRAKNNDLQDNYLTELNRNRSLASQLEEIK 345
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEELE 653
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
104-439 |
9.07e-09 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 59.73 E-value: 9.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 104 RELKSEIERLQKRMVDLEKLEEALSRSKNEcSQLCLSLNEERNLTkkissELEMLRVKVKELESSEDRLDKTEQSLVSEL 183
Cdd:COG1196 182 ERTEENLERLEDLLEELEKQLEKLERQAEK-AERYQELKAELREL-----ELALLLAKLKELRKELEELEEELSRLEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 184 EKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKK------MNRDHMRNASTFLERNDLRIEDGISSTLSSKESK 257
Cdd:COG1196 256 EELQEELEEAEKEIEELKSELEELREELEELQEELLELKEeieeleGEISLLRERLEELENELEELEERLEELKEKIEAL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 258 RKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKhfESLEEELKKMRAKNNDLQDNyLTELNRNRSL 337
Cdd:COG1196 336 KEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALR--EELAELEAELAEIRNELEEL-KREIESLEER 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 338 ASQLEEIKLQVRKQKELGNGDIEGEDAFLLGRGRHERTKLKGHGSEASVSKHTSRELSP-QHKRERLRNREFALSNEHYS 416
Cdd:COG1196 413 LERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAElQEELQRLEKELSSLEARLDR 492
|
330 340
....*....|....*....|...
gi 1720408942 417 LSSKQASSPVFTNKRAAKASNMG 439
Cdd:COG1196 493 LEAEQRASQGVRAVLEALESGLP 515
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
19-353 |
1.59e-08 |
|
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: 58.49 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 19 KLQSLSRRLDELEEATKNLQRaedELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKdeeIKRAEDLCHTMKEKLEE 98
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQR---ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQEKLNQQKDEQIKK 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 99 EENLTRELKSEIERLQKrmvDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSedrLDKTEQS 178
Cdd:TIGR04523 417 LQQEKELLEKEIERLKE---TIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN---LEQKQKE 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 179 LVSELEKLKSLTlsfvNERKYLNEKEKENEKIIKELTQKLEQnkkmnrdhmrnastfLERNDLRIEDGISST----LSSK 254
Cdd:TIGR04523 491 LKSKEKELKKLN----EEKKELEEKVKDLTKKISSLKEKIEK---------------LESEKKEKESKISDLedelNKDD 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 255 ESKRKGSLDYLKQVENETRDKSENE-----KNRNQEDNKVKDLNQEIEKLKTQI----KHFESLEEELKKMRAKNNDLQD 325
Cdd:TIGR04523 552 FELKKENLEKEIDEKNKEIEELKQTqkslkKKQEEKQELIDQKEKEKKDLIKEIeekeKKISSLEKELEKAKKENEKLSS 631
|
330 340
....*....|....*....|....*...
gi 1720408942 326 NYLTELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:TIGR04523 632 IIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-315 |
3.43e-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: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 7 YKDAASNRHLRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAe 86
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 87 dlchtmkekleeeenlTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQlclSLNEERNLTKKISSELEMLRVKVKELE 166
Cdd:TIGR02168 297 ----------------ISRLEQQKQILRERLANLERQLEELEAQLEELES---KLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 167 SSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDLRIEDG 246
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720408942 247 ISSTLsskESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKK 315
Cdd:TIGR02168 438 LQAEL---EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
16-334 |
4.36e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 16 LRFKLQSLSRRLDELEEATKNLQRAeDELLDLQDKVIQAEGSDSSTLAEIEVLRqrvlkiegKDEEIKRAEDLCHTMKEK 95
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKA-DEAKKAEEAKKADEAKKAEEAKKADEAK--------KAEEKKKADELKKAEELK 1558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 96 LEEEENLTRELKSEIERlqkRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSED----- 170
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEED---KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEekkkv 1635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 171 -RLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDLRI----ED 245
Cdd:PTZ00121 1636 eQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKkeaeEK 1715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 246 GISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFES--LEEELKKMRAKNNDL 323
Cdd:PTZ00121 1716 KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEavIEEELDEEDEKRRME 1795
|
330
....*....|.
gi 1720408942 324 QDNYLTELNRN 334
Cdd:PTZ00121 1796 VDKKIKDIFDN 1806
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
105-354 |
4.31e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.87 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 105 ELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELE 184
Cdd:TIGR04523 156 KLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 185 KLKS----LTLSFVNERKYLNEKEKENEKIIKELTQK---LEQNKKMNRDhmrnastfLERNDLRIEDGISSTlssKESK 257
Cdd:TIGR04523 236 KKQQeineKTTEISNTQTQLNQLKDEQNKIKKQLSEKqkeLEQNNKKIKE--------LEKQLNQLKSEISDL---NNQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 258 RKGSLDYLK-QVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKK-MRAKNNDLQ------DNYLT 329
Cdd:TIGR04523 305 EQDWNKELKsELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQReLEEKQNEIEklkkenQSYKQ 384
|
250 260
....*....|....*....|....*
gi 1720408942 330 ELNrnrSLASQLEEIKLQVRKQKEL 354
Cdd:TIGR04523 385 EIK---NLESQINDLESKIQNQEKL 406
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
61-353 |
5.17e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.82 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 61 TLAEIEVLRQRVLKIEGKDEEIKRAEDlchtmKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLS 140
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQEL-----KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 141 LNEERNLTKKI---SSELEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQK 217
Cdd:pfam02463 249 EQEEIESSKQEiekEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 218 LEQNKKMNRDHMRNASTFLERNDLRIEDGISSTLSS--KESKRKGSLDYLKQVENETRDKSENEKN-----RNQEDNKVK 290
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLqeKLEQLEEELLAKKKLESERLSSAAKLKEeelelKSEEEKEAQ 408
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720408942 291 DLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-325 |
5.35e-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: 53.91 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 3 ELTNYKDAAsnRHLRFKLQSLSRRLDELEE----ATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGK 78
Cdd:TIGR02168 706 ELEELEEEL--EQLRKELEELSRQISALRKdlarLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 79 ----DEEIKRAEDLCHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERnltKKISSE 154
Cdd:TIGR02168 784 ieelEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI---ESLAAE 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 155 LEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQnkkmnrdhmrnAST 234
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ-----------LEL 929
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 235 FLERNDLRIeDGISSTLSSKESKrkgSLDYLKQVENETRDKSENEKNRnqednkVKDLNQEIEKLK----TQIKHFESLE 310
Cdd:TIGR02168 930 RLEGLEVRI-DNLQERLSEEYSL---TLEEAEALENKIEDDEEEARRR------LKRLENKIKELGpvnlAAIEEYEELK 999
|
330
....*....|....*
gi 1720408942 311 EELKKMRAKNNDLQD 325
Cdd:TIGR02168 1000 ERYDFLTAQKEDLTE 1014
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
16-415 |
7.75e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.51 E-value: 7.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 16 LRFKLQSLSRRLDELEEATKNLQRAEDELLDL---QDKVIQAEgsdsstLAEIEVLRQRVLKIEGKDEEIKRAEDLCHTM 92
Cdd:TIGR00606 700 LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLapgRQSIIDLK------EKEIPELRNKLQKVNRDIQRLKNDIEEQETL 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 93 KEKLEEEENLTRELKSE---IERLQKRMVDLEKLEEALSrSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSE 169
Cdd:TIGR00606 774 LGTIMPEEESAKVCLTDvtiMERFQMELKDVERKIAQQA-AKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLI 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 170 DRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELtQKLEQNKKMNRDHMRNASTFLERNDLRIEDGISS 249
Cdd:TIGR00606 853 QDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV-QSLIREIKDAKEQDSPLETFLEKDQQEKEELISS 931
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 250 TLSSK----------ESKRKGSLDYLKQVENETRDKSENEKnrNQEDNKVKDLNQEIEKLKtqiKHFESLEEELKKMRaK 319
Cdd:TIGR00606 932 KETSNkkaqdkvndiKEKVKNIHGYMKDIENKIQDGKDDYL--KQKETELNTVNAQLEECE---KHQEKINEDMRLMR-Q 1005
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 320 NNDLQDNYLTELNRNRSLASQLEEIKlQVRKQKELGNGDIeGEDAFLLGRGRH----ERTKLKGHGSEASVSKHTSRELS 395
Cdd:TIGR00606 1006 DIDTQKIQERWLQDNLTLRKRENELK-EVEEELKQHLKEM-GQMQVLQMKQEHqkleENIDLIKRNHVLALGRQKGYEKE 1083
|
410 420
....*....|....*....|
gi 1720408942 396 PQHKRERLRNREFALSNEHY 415
Cdd:TIGR00606 1084 IKHFKKELREPQFRDAEEKY 1103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
80-353 |
8.17e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 8.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 80 EEIKRAEDLCHTMKEKLEeeenltrELKSEIERLQKRMVDLEKLEEALSRSKNECS-QLCLSLNEERNLTKKISSELEML 158
Cdd:TIGR02168 684 EKIEELEEKIAELEKALA-------ELRKELEELEEELEQLRKELEELSRQISALRkDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 159 RVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNerkyLNEKEKENEKIIKELTQKLeQNKKMNRDHMRNASTFLER 238
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ----LKEELKALREALDELRAEL-TLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 239 NDLRIEDGISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKtqiKHFESLEEELKKMRA 318
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR---SELEELSEELRELES 908
|
250 260 270
....*....|....*....|....*....|....*
gi 1720408942 319 KNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
64-322 |
8.47e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 8.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 64 EIEVLRQRVLKIEGKDEEIKRAEDlchTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNE---CSQLCLS 140
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEE---ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEakkAEELKKK 1710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 141 LNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQ 220
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 221 NKKMNRDhmRNASTFLERNDLRIEDGISSTL---SSKE---SKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQ 294
Cdd:PTZ00121 1791 KRRMEVD--KKIKDIFDNFANIIEGGKEGNLvinDSKEmedSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEA 1868
|
250 260
....*....|....*....|....*...
gi 1720408942 295 EIEKLKTQIKHFESLEEELKKMRAKNND 322
Cdd:PTZ00121 1869 DFNKEKDLKEDDEEEIEEADEIEKIDKD 1896
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
21-280 |
9.02e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 9.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 21 QSLSRRLDELEEATKNLQR-AEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVlkiEGKDEEIKRAEDLCHtmkEKLEEE 99
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKEREL---EDAEERLAKLEAEID---KLLAEI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 100 ENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSL 179
Cdd:TIGR02169 339 EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 180 VSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHmrNASTFLERNDLRIedgISSTLSSKESKRK 259
Cdd:TIGR02169 419 SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY--EQELYDLKEEYDR---VEKELSKLQRELA 493
|
250 260
....*....|....*....|.
gi 1720408942 260 GSLDYLKQVENETRDKSENEK 280
Cdd:TIGR02169 494 EAEAQARASEERVRGGRAVEE 514
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2-349 |
2.21e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 2 AELTNYKDAASNRhlRFKLQSLSRRLDELEEATKN----LQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRV----- 72
Cdd:PRK02224 370 SELEEAREAVEDR--REEIEELEEEIEELRERFGDapvdLGNAEDFLEELREERDELREREAELEATLRTARERVeeaea 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 73 LKIEGK---------DEEIKRAEDLCHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNE 143
Cdd:PRK02224 448 LLEAGKcpecgqpveGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAE 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 144 ERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKI------------- 210
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIrtllaaiadaede 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 211 IKELTQKLEQNKKMNRDHMRNASTFLERNDLRIEDGISSTLSSKESKRKGSLDYLKQVENETRDKSEneknrnQEDnkvk 290
Cdd:PRK02224 608 IERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELRE------ERD---- 677
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720408942 291 DLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYltelnrnrSLASQLEEIKLQVR 349
Cdd:PRK02224 678 DLQAEIGAVENELEELEELRERREALENRVEALEALY--------DEAEELESMYGDLR 728
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
19-323 |
2.24e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.90 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 19 KLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLCHTMKEKLEE 98
Cdd:pfam02463 723 LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEE 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 99 EENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCL-SLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQ 177
Cdd:pfam02463 803 LRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKeEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQ 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 178 SLVSELEK-----------LKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMnRDHMRNASTFLERNDLRIEDG 246
Cdd:pfam02463 883 KLKDELESkeekekeekkeLEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEEL-LLEEADEKEKEENNKEEEEER 961
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720408942 247 ISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKhfeslEEELKKMRAKNNDL 323
Cdd:pfam02463 962 NKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRL-----KEFLELFVSINKGW 1033
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
21-378 |
2.78e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 51.59 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 21 QSLSRRLDELEEATKNLQRAED-----------------ELLDLQDKVIQAEGSDSStlAEIEvlrQRVLKIEGK----- 78
Cdd:PRK10929 48 EALQSALNWLEERKGSLERAKQyqqvidnfpklsaelrqQLNNERDEPRSVPPNMST--DALE---QEILQVSSQlleks 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 79 ---DEEIKRAEDLCHTMKEKLEEEENLTRELkSEIERlqkRMVDLEKLEEALSRSKNecsqlcLSLNEERNLTKKISSEL 155
Cdd:PRK10929 123 rqaQQEQDRAREISDSLSQLPQQQTEARRQL-NEIER---RLQTLGTPNTPLAQAQL------TALQAESAALKALVDEL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 156 EM-----------LRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENekIIKELTQKLEQNkkm 224
Cdd:PRK10929 193 ELaqlsannrqelARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALESTELLAEQSGD--LPKSIVAQFKIN--- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 225 nrdhmRNASTFLERNDLRIEDgisstLSSKESKRKGSLDYLKQVENETRDKSE--------NEKNRNQ-----EDNKVKD 291
Cdd:PRK10929 268 -----RELSQALNQQAQRMDL-----IASQQRQAASQTLQVRQALNTLREQSQwlgvsnalGEALRAQvarlpEMPKPQQ 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 292 LNQEIEKLKTQIKHFESLEEELKKMRAKNNDlqDNYLTELNRNRSLASQLeeiklqvRKQKELGNGDIEGEDAFLLgrgr 371
Cdd:PRK10929 338 LDTEMAQLRVQRLRYEDLLNKQPQLRQIRQA--DGQPLTAEQNRILDAQL-------RTQRELLNSLLSGGDTLIL---- 404
|
....*..
gi 1720408942 372 hERTKLK 378
Cdd:PRK10929 405 -ELTKLK 410
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
19-214 |
9.08e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 9.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 19 KLQSLSRRLDELEEATKNLQRAEDELLD-LQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLCHTMKEKLE 97
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELEEELAELLKeLEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELD 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 98 EEENLTRELKSEIERLQKRmvdLEKLEEALSRSKNEcsqlclslnEERNLTKKISSELEMLRVKVKELESSEDRLDKTeq 177
Cdd:PRK03918 630 KAFEELAETEKRLEELRKE---LEELEKKYSEEEYE---------ELREEYLELSRELAGLRAELEELEKRREEIKKT-- 695
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720408942 178 slvseLEKLKsltlsfvNERKYLNEKEKENEKIIKEL 214
Cdd:PRK03918 696 -----LEKLK-------EELEEREKAKKELEKLEKAL 720
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
14-319 |
1.29e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 14 RHLRFKLQSLSRRLDELEEATKNLQRAED-------ELLDLQDKVIQAEGSdsstlAEIEVLRQRVLKIEGKDEEIK-RA 85
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrELTEEHRKELLEEYT-----AELKRIEKELKEIEEKERKLRkEL 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 86 EDLCHTMKEKLEEEENLT-----RELKSE-----IERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKIS--- 152
Cdd:PRK03918 483 RELEKVLKKESELIKLKElaeqlKELEEKlkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAele 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 153 ----------------------SELEMLRVKVKELESSEDR---LDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKEN 207
Cdd:PRK03918 563 kkldeleeelaellkeleelgfESVEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRL 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 208 EKIIKELTqklEQNKKMNRDHMRNASTFLERndlriedgISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRnqedn 287
Cdd:PRK03918 643 EELRKELE---ELEKKYSEEEYEELREEYLE--------LSRELAGLRAELEELEKRREEIKKTLEKLKEELEER----- 706
|
330 340 350
....*....|....*....|....*....|..
gi 1720408942 288 kvKDLNQEIEKLKTQIKHFESLEEELKKMRAK 319
Cdd:PRK03918 707 --EKAKKELEKLEKALERVEELREKVKKYKAL 736
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
19-353 |
1.49e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.27 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 19 KLQSLSRRLDELEEATKNLQRAEDELLDLQDKV-IQAEGSDSSTLAEIEVLRQRVLKIE----GKDEEIKRAEDLCHTMK 93
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLLNQEKTELLVEQGRLqLQADRHQEHIRARDSLIQSLATRLEldgfERGPFSERQIKNFHTLV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 94 EKLEEEENLTrelkseIERLQKRMVDLEKL-EEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRL 172
Cdd:TIGR00606 400 IERQEDEAKT------AAQLCADLQSKERLkQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 173 DKTEQSLVSELEKL-----KSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQ--NKKMNRDHMRNASTFLERNDLRIED 245
Cdd:TIGR00606 474 LELDQELRKAERELskaekNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQlnHHTTTRTQMEMLTKDKMDKDEQIRK 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 246 gISSTLSSKESKRKGSLDYLKQVENETRDKSeneKNRNQEDNKVKDLNQEIEKLKTQIKHFeslEEELKKMRAKNNDLQD 325
Cdd:TIGR00606 554 -IKSRHSDELTSLLGYFPNKKQLEDWLHSKS---KEINQTRDRLAKLNKELASLEQNKNHI---NNELESKEEQLSSYED 626
|
330 340
....*....|....*....|....*...
gi 1720408942 326 NyLTELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:TIGR00606 627 K-LFDVCGSQDEESDLERLKEEIEKSSK 653
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
106-359 |
2.01e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 106 LKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELEK 185
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 186 LKSLTLSFVNERKYLNEKEKENEKI--IKELTQKLEQNKKM-NRDHMRNasTFLERNDLRIEDGISSTLSSKESKRKGSL 262
Cdd:PRK01156 251 KNRYESEIKTAESDLSMELEKNNYYkeLEERHMKIINDPVYkNRNYIND--YFKYKNDIENKKQILSNIDAEINKYHAII 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 263 DYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLE 342
Cdd:PRK01156 329 KKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIK 408
|
250
....*....|....*..
gi 1720408942 343 EIKLQVRKQKELGNGDI 359
Cdd:PRK01156 409 KELNEINVKLQDISSKV 425
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
109-342 |
2.10e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.39 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 109 EIERLqKRMVDLEKLEEALSRSkNECSQLCLSLNEERNLTKKISSELEmlRVKVKELESSEDRLDKTEQSLVSELEKLks 188
Cdd:PRK05771 32 HIEDL-KEELSNERLRKLRSLL-TKLSEALDKLRSYLPKLNPLREEKK--KVSVKSLEELIKDVEEELEKIEKEIKEL-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 189 ltlsfVNERKYLNEKEKENEKIIKELTQ--------KLEQNKKmnrdhmrNASTFLERNDLRIEDGISSTLSSK----ES 256
Cdd:PRK05771 106 -----EEEISELENEIKELEQEIERLEPwgnfdldlSLLLGFK-------YVSVFVGTVPEDKLEELKLESDVEnveyIS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 257 KRKGSLDYLKQVENETRDKSENE--KN--RNQEDNKVKDLNQEIEKLKTQI----KHFESLEEELKKMRAKNNDL---QD 325
Cdd:PRK05771 174 TDKGYVYVVVVVLKELSDEVEEElkKLgfERLELEEEGTPSELIREIKEELeeieKERESLLEELKELAKKYLEEllaLY 253
|
250
....*....|....*...
gi 1720408942 326 NYL-TELNRNRSLASQLE 342
Cdd:PRK05771 254 EYLeIELERAEALSKFLK 271
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
82-356 |
4.23e-05 |
|
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: 47.74 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 82 IKRAEDLCHTMKEKLEEEENLTRELKSEIE-RLQKRMvdLEKLEEALSRSKNecsqlclSLNEERNLTKKISSELEMLRV 160
Cdd:TIGR01612 502 MKDFKDIIDFMELYKPDEVPSKNIIGFDIDqNIKAKL--YKEIEAGLKESYE-------LAKNWKKLIHEIKKELEEENE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 161 KVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKekeNEKIIKELT-QKLEQNKKMNRDHMRNASTFLERN 239
Cdd:TIGR01612 573 DSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNISDK---NEYIKKAIDlKKIIENNNAYIDELAKISPYQVPE 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 240 DLRIEDGISSTLSSKESK-RKGSLDYLKqveNETRD-KSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFE--SLEEELKK 315
Cdd:TIGR01612 650 HLKNKDKIYSTIKSELSKiYEDDIDALY---NELSSiVKENAIDNTEDKAKLDDLKSKIDKEYDKIQNMEtaTVELHLSN 726
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1720408942 316 MRAKNNDLQDNyLTELNR------NRSLASQLEEIKlqvRKQKELGN 356
Cdd:TIGR01612 727 IENKKNELLDI-IVEIKKhihgeiNKDLNKILEDFK---NKEKELSN 769
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
62-349 |
4.76e-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: 47.37 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 62 LAEIEVLRQRVLKIEGKDEEIK---------RAEDLCHTMKEKLEEEENLT------RELKSEIERLQKRMVDLEKLEEA 126
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRqqlerlrreREKAERYQALLKEKREYEGYellkekEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 127 LSRSKNECSQLCLSLNEERN-LTKKIS--SELEMLRVKVK--ELESSEDRLDKTEQSLVSELEKL-KSLTLSFVNERKYL 200
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEeLNKKIKdlGEEEQLRVKEKigELEAEIASLERSIAEKERELEDAeERLAKLEAEIDKLL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 201 NEKEKENEKIikeLTQKLEQNKKMNRDHMRNASTFLERNDLRIEDGISSTLSSKESKRKGSLDYLKQVENE---TRDKSE 277
Cdd:TIGR02169 336 AEIEELEREI---EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINElkrELDRLQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 278 NEKNRNQEdnKVKDLNQEIEKLKTQIKHFES-----------LEEELKKMRAKNNDLQDNYL---TELN----RNRSLAS 339
Cdd:TIGR02169 413 EELQRLSE--ELADLNAAIAGIEAKINELEEekedkaleikkQEWKLEQLAADLSKYEQELYdlkEEYDrvekELSKLQR 490
|
330
....*....|
gi 1720408942 340 QLEEIKLQVR 349
Cdd:TIGR02169 491 ELAEAEAQAR 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
19-189 |
5.20e-05 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 47.40 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 19 KLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRvlKIEGKDEEIKRAEDLCHTMKEKLEE 98
Cdd:COG1196 345 LLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRN--ELEELKREIESLEERLERLSERLED 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 99 EENLTRELKSEIERLQKRMVD----LEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDK 174
Cdd:COG1196 423 LKEELKELEAELEELQTELEElneeLEELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQG 502
|
170
....*....|....*
gi 1720408942 175 TEQSLVSELEKLKSL 189
Cdd:COG1196 503 VRAVLEALESGLPGV 517
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
20-353 |
6.16e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 20 LQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLCHTMKEKLEEE 99
Cdd:PRK01156 175 IDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRY 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 100 ENLTRELKSEIERLQKRMVDLEKLEEALSRSKNecSQLCLSLNEER---NLTKKISSELEMLRVKVKELESSEDRLDKTE 176
Cdd:PRK01156 255 ESEIKTAESDLSMELEKNNYYKELEERHMKIIN--DPVYKNRNYINdyfKYKNDIENKKQILSNIDAEINKYHAIIKKLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 177 --QSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQ---KLEQNKKMNRDHMRNASTFLERNDL------RIED 245
Cdd:PRK01156 333 vlQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESlkkKIEEYSKNIERMSAFISEILKIQEIdpdaikKELN 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 246 GISSTL---SSKESKRKGSLDYLKQVENETRDKSE-------------------NEKNRNQEDNKVKDLNQEIEKLKTQI 303
Cdd:PRK01156 413 EINVKLqdiSSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcgttlgeekSNHIINHYNEKKSRLEEKIREIEIEV 492
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1720408942 304 KHFESLEEELKKMRAKNNDLQDN-YLTELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:PRK01156 493 KDIDEKIVDLKKRKEYLESEEINkSINEYNKIESARADLEDIKIKINELKD 543
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
197-353 |
7.42e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 46.68 E-value: 7.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 197 RKYLNEKEKENEKIIKELTQkLEQNKKMnrdhmrnaSTFLERNDLRIEDGISSTLSSKESKRKGSLDYLKQVENETrdKS 276
Cdd:COG0419 146 DAFLKSKPKERKEILDELFG-LEKYEKL--------SELLKEVIKEAKAKIEELEGQLSELLEDIEDLLEALEEEL--KE 214
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720408942 277 ENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:COG0419 215 LKKLEEIQEEQEEEELEQEIEALEERLAELEEEKERLEELKARLLEIESLELEALKIREEELRELERLLEELEEKIE 291
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
68-354 |
8.10e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 46.63 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 68 LRQRVLKIEGKDEEIKRAEDLchtmkekleeeenlTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNL 147
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSL--------------TAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERA 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 148 TKKISSELEMLRVKVkELESSEdrldktEQSLVSELEKLKSLTlsfvNERKYLNEKEKENEKIIKELTQKLEQNKKMNRD 227
Cdd:pfam15921 512 IEATNAEITKLRSRV-DLKLQE------LQHLKNEGDHLRNVQ----TECEALKLQMAEKDKVIEILRQQIENMTQLVGQ 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 228 HMRNASTFL--------ERNDLRIEDGISSTLSSKESKRKGSLDylKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKL 299
Cdd:pfam15921 581 HGRTAGAMQvekaqlekEINDRRLELQEFKILKDKKDAKIRELE--ARVSDLELEKVKLVNAGSERLRAVKDIKQERDQL 658
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720408942 300 KTQIKHFESleeELKKMRAKNNDLQDNYlteLNRNRSLASQLEEIKLQVRK-QKEL 354
Cdd:pfam15921 659 LNEVKTSRN---ELNSLSEDYEVLKRNF---RNKSEEMETTTNKLKMQLKSaQSEL 708
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
103-363 |
8.57e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.89 E-value: 8.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 103 TRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEER------NLTKKISSELEMLRV--KVKELESSEDRLDK 174
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKkaleyyQLKEKLELEEEYLLYldYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 175 TEQSLVSELEKLKSL------TLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDLRIEDGIS 248
Cdd:pfam02463 245 LLRDEQEEIESSKQEiekeeeKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 249 STLSSKESKRKGSLDYLKQVENETRDKSENE-KNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKmRAKNNDLQDNY 327
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEeEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL-KEEELELKSEE 403
|
250 260 270
....*....|....*....|....*....|....*.
gi 1720408942 328 LTELNRNRSLASQLEEIkLQVRKQKELGNGDIEGED 363
Cdd:pfam02463 404 EKEAQLLLELARQLEDL-LKEEKKEELEILEEEEES 438
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
27-332 |
1.31e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 46.36 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 27 LDELEEATKNLQRAEDELLDLQDKVIQAEGSDSST--LAEIEVLRQRvlkIEGKDEEIKRAEDLCHTMkekleeeenltr 104
Cdd:PTZ00440 690 IKNLKKELQNLLSLKENIIKKQLNNIEQDISNSLNqyTIKYNDLKSS---IEEYKEEEEKLEVYKHQI------------ 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 105 elkseIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVK----ELESSEDRLDKTEQSLV 180
Cdd:PTZ00440 755 -----INRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKKnnqdLLNSYNILIQKLEAHTE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 181 SELEKLKSLTLSFVNERKYLNEKEKENE-----KIIKELTQKLEQ-NKKMNRDHMRNASTFLERNDLRIedgISSTLSSK 254
Cdd:PTZ00440 830 KNDEELKQLLQKFPTEDENLNLKELEKEfnennQIVDNIIKDIENmNKNINIIKTLNIAINRSNSNKQL---VEHLLNNK 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 255 ESKRKGSLDYLKQVENET----RDKSENEKNRNQEDNKV-KDLNQE-IEKLKTQIkhfESLEEELKKMRAKNNDLQDNYL 328
Cdd:PTZ00440 907 IDLKNKLEQHMKIINTDNiiqkNEKLNLLNNLNKEKEKIeKQLSDTkINNLKMQI---EKTLEYYDKSKENINGNDGTHL 983
|
....
gi 1720408942 329 TELN 332
Cdd:PTZ00440 984 EKLD 987
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
16-353 |
1.41e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 45.86 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 16 LRFKLQSLSRRLDELEEATKNLQRAEDELLD-LQDKVIQAEGS---------DSSTlaEIEVLRQRVLKIEGKDEEIKR- 84
Cdd:pfam15921 115 LQTKLQEMQMERDAMADIRRRESQSQEDLRNqLQNTVHELEAAkclkedmlnDSNT--QIEQLRKMMLSHEGVLQEIRSi 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 85 -------------AEDLCHTM--KEKLEEEENLTRELKSEIERLQKRMVDLEKLEEAL-SRSKNECSQLclsLNEERNLT 148
Cdd:pfam15921 193 lvdfeeasgkkiyEHDSMSTIhfRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALkSESQNKIELL---LQQHQDRI 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 149 KKISSELEmlrVKVKELESSEDRLDKTEQSLVSELEKLKSLTLsfvNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDH 228
Cdd:pfam15921 270 EQLISEHE---VEITGLTEKASSARSQANSIQSQLEIIQEQAR---NQNSMYMRQLSDLESTVSQLRSELREAKRMYEDK 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 229 MRNastfLERNDLRIEDGISSTLSSKE--SKRKGSLDYLKQVENETRDKSENEKNRNQEDNK------------------ 288
Cdd:pfam15921 344 IEE----LEKQLVLANSELTEARTERDqfSQESGNLDDQLQKLLADLHKREKELSLEKEQNKrlwdrdtgnsitidhlrr 419
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720408942 289 -VKDLNQEIEKLKTQIKHFES-----LEEELKKMRAKNNDLQdnyltelnRNRSLASQLEEIKLQVRKQKE 353
Cdd:pfam15921 420 eLDDRNMEVQRLEALLKAMKSecqgqMERQMAAIQGKNESLE--------KVSSLTAQLESTKEMLRKVVE 482
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
79-345 |
1.94e-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: 45.44 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 79 DEEIKRAEDLCHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEeALSRSKNECSQLCLSLNEERNLT--KKISSELE 156
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQ-ALLKEKREYEGYELLKEKEALERqkEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 157 MLRvkvKELESSEDRLDKTEQSLVSELEKLKSLT--LSFVNERKYLNEKEKenekiIKELTQKLEQNKKMNRDHMRNAST 234
Cdd:TIGR02169 248 SLE---EELEKLTEEISELEKRLEEIEQLLEELNkkIKDLGEEEQLRVKEK-----IGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 235 fLERNDLRIEDGISSTLSSKESKRKGSLDYLKQVENETrdkSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELK 314
Cdd:TIGR02169 320 -AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT---EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
250 260 270
....*....|....*....|....*....|.
gi 1720408942 315 KMRAKNNDLQDNYLTELNRNRSLASQLEEIK 345
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLN 426
|
|
| YloA |
COG1293 |
Predicted component of the ribosome quality control (RQC) complex, YloA/Tae2 family, contains ... |
109-353 |
2.20e-04 |
|
Predicted component of the ribosome quality control (RQC) complex, YloA/Tae2 family, contains fibronectin-binding (FbpA) and DUF814 domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 224212 [Multi-domain] Cd Length: 564 Bit Score: 45.08 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 109 EIERLQKRMVDLEKL--EEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELEKL 186
Cdd:COG1293 187 DIVRLLARFLGLGGLlaEELLSRAGLDKKVPAKDLFEEEIKKVREALEELLNPLKPNYYYKDEKYLDVVPLKAYADLEKL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 187 KSLTLSFVNER----KYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDL------RIEDGISS-TLSSKE 255
Cdd:COG1293 267 FNEALDEKFERdkikQLASELEKKLEKELKKLENKLEKQEDELEELEKAAEELRQKGELlyanlqLIEEGLKSvRLADFY 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 256 SKRKGSLDylkqvENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDnylTELNRNR 335
Cdd:COG1293 347 GNEEIKIE-----LDKSKTPSENAQRYFKKYKKLKGAKVNLDRQLSELKEAIAYYESAKTALEKAEGKKA---IEEIREE 418
|
250
....*....|....*...
gi 1720408942 336 SLASQLEEIKLQVRKQKE 353
Cdd:COG1293 419 LIEEGLLKSKKKKRKKKE 436
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
16-366 |
2.71e-04 |
|
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: 45.10 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 16 LRFKLQSLSRRLDELE-EATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGK----DEEIKRAEDLCH 90
Cdd:pfam05483 213 MHFKLKEDHEKIQHLEeEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKtklqDENLKELIEKKD 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 91 TMkekleeeenlTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLC-------LSLNEERNLTKKISSEL-------- 155
Cdd:pfam05483 293 HL----------TKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTeekeaqmEELNKAKAAHSFVVTEFeattcsle 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 156 EMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTlsfvnerKYLNEKEKENEKIIKELTQK---LEQNKKMNRdhmrna 232
Cdd:pfam05483 363 ELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMT-------KFKNNKEVELEELKKILAEDeklLDEKKQFEK------ 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 233 stflerndlriedgISSTLSSKESKRKGSLdylkqvenETRDKseneknrnqednKVKDLNQEIEKLKTQIKHF----ES 308
Cdd:pfam05483 430 --------------IAEELKGKEQELIFLL--------QAREK------------EIHDLEIQLTAIKTSEEHYlkevED 475
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720408942 309 LEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKELGNGDIEGEDAFL 366
Cdd:pfam05483 476 LKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERML 533
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
121-353 |
3.09e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 121 EKLEEALSRSKNECSQLCLSL-NEERNLTKKISsELEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKY 199
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELkNLDKNLNKDEE-KINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 200 LNEKEKENEKIIKELTQKLEQNKKmnrdhmrNASTFLerNDLRIEDGISSTLSSKES---KRKGSL-DYLKQVENETRDK 275
Cdd:TIGR04523 115 DKEQKNKLEVELNKLEKQKKENKK-------NIDKFL--TEIKKKEKELEKLNNKYNdlkKQKEELeNELNLLEKEKLNI 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720408942 276 SENEKNRNQEDNKvkdLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:TIGR04523 186 QKNIDKIKNKLLK---LELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD 260
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
29-360 |
3.51e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 29 ELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLR-QRVLKIEGKDEEIKRAEDLCHTMKEKLEEEENLTRELK 107
Cdd:PRK01156 410 ELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNgQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIE 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 108 SEIERLQKRMVDLEKLEEALSRSKNEcsqlclSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVS-ELEKL 186
Cdd:PRK01156 490 IEVKDIDEKIVDLKKRKEYLESEEIN------KSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlKLEDL 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 187 KSLTLSFVNERKYLNEKEKENEKiikelTQKLEQNKKMNRdhmrnastfLERNDLRIEDGISSTLSSKESkrkgsldYLK 266
Cdd:PRK01156 564 DSKRTSWLNALAVISLIDIETNR-----SRSNEIKKQLND---------LESRLQEIEIGFPDDKSYIDK-------SIR 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 267 QVENETRDkSENEKNRNQEDNKVKD-LNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNY------LTELNRNRSLAS 339
Cdd:PRK01156 623 EIENEANN-LNNKYNEIQENKILIEkLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLkksrkaLDDAKANRARLE 701
|
330 340
....*....|....*....|.
gi 1720408942 340 QLEEIKLQVRKQKELGNGDIE 360
Cdd:PRK01156 702 STIEILRTRINELSDRINDIN 722
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
15-347 |
7.58e-04 |
|
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: 43.56 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 15 HLRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKViqaeGSDSSTLAEIEVLRQRVLKIEGKDEEI--------KRAE 86
Cdd:pfam05483 378 QLKIITMELQKKSSELEEMTKFKNNKEVELEELKKIL----AEDEKLLDEKKQFEKIAEELKGKEQELifllqareKEIH 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 87 DL---CHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSK----NECSQLCLSL-NEERNLTKKISSELEML 158
Cdd:pfam05483 454 DLeiqLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENkeltQEASDMTLELkKHQEDIINCKKQEERML 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 159 rvkvKELESsedrLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLER 238
Cdd:pfam05483 534 ----KQIEN----LEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEN 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 239 NDLRIEDgisstlsskeskrkgsldyLKQVENETRDKSENE-KNRNQEDNKVKDLNQEIEKLKTQikhFESLEEELKKMR 317
Cdd:pfam05483 606 KNKNIEE-------------------LHQENKALKKKGSAEnKQLNAYEIKVNKLELELASAKQK---FEEIIDNYQKEI 663
|
330 340 350
....*....|....*....|....*....|
gi 1720408942 318 AKNNDLQDNYLTELNRNRSLASqlEEIKLQ 347
Cdd:pfam05483 664 EDKKISEEKLLEEVEKAKAIAD--EAVKLQ 691
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
4-226 |
7.99e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 225288 [Multi-domain] Cd Length: 652 Bit Score: 43.15 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 4 LTNYKDAASNRHLRFKLQSLSRRLDELEEATKNLQR-AEDELLDLQDKVIQAEGSDSSTLAEieVLRQRVLKIEGKDEEI 82
Cdd:COG2433 331 LRTLKISVSDDHERDALAAAYKAYLAYKPKLEKVERkLPELGIWKDVERIKALVIRGYPLAE--ALSKVKEEERPREKEG 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 83 KRAEDlchtmKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRsknecsqlclslneernltkkissELEMLRVKV 162
Cdd:COG2433 409 TEEEE-----RREITVYEKRIKKLEETVERLEEENSELKRELEELKR------------------------EIEKLESEL 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720408942 163 KEL---ESSEDRLDKTEQSLVSELEKLksltlsfvnERKYLNEKEKenekiIKELTQKLEQNKKMNR 226
Cdd:COG2433 460 ERFrreVRDKVRKDREIRARDRRIERL---------EKELEEKKKR-----VEELERKLAELRKMRK 512
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
3-223 |
8.16e-04 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 43.55 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 3 ELTNYKDAASNRHLRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEgkdEEI 82
Cdd:COG1196 803 EEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELE---DEL 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 83 KRAEDLCHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALsrsKNECSQLCLSLNEERNLTkkISSELEMlrvKV 162
Cdd:COG1196 880 KELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERL---EVELPELEEELEEEYEDT--LETELER---EI 951
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720408942 163 KELESSEDRLDKTEQSLVSELEKLKsltlsfvNERKYLNEKEKENEKI---IKELTQKLEQNKK 223
Cdd:COG1196 952 ERLEEEIEALGPVNLRAIEEYEEVE-------ERYEELKSQREDLEEAkekLLEVIEELDKEKR 1008
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
73-374 |
8.24e-04 |
|
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: 43.50 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 73 LKIEGKDEEIKRAEDLCHTMKEKLEEEENlTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQL-CLSLNEERNLTKKI 151
Cdd:TIGR01612 1226 LFLEKIDEEKKKSEHMIKAMEAYIEDLDE-IKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHhIISKKHDENISDIR 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 152 SSELEMLRVKVKEleSSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKEN--EKII---KELTQKLEQNKKMNR 226
Cdd:TIGR01612 1305 EKSLKIIEDFSEE--SDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNILKLNkiKKIIdevKEYTKEIEENNKNIK 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 227 DHMRNASTFLE--RNDLRIED---GISSTLSSKE-----SKRKGSLDYL--KQVENETRDKSENEKNRN----------- 283
Cdd:TIGR01612 1383 DELDKSEKLIKkiKDDINLEEcksKIESTLDDKDideciKKIKELKNHIlsEESNIDTYFKNADENNENvlllfkniema 1462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 284 ----------QEDNKVKDLNQEIEKLKTQIKHFESLEEEL---KKMRAKNNDLQDNYLTELNR--NRSLASQLEEIKLQV 348
Cdd:TIGR01612 1463 dnksqhilkiKKDNATNDHDFNINELKEHIDKSKGCKDEAdknAKAIEKNKELFEQYKKDVTEllNKYSALAIKNKFAKT 1542
|
330 340
....*....|....*....|....*..
gi 1720408942 349 RKQKELGNGDI-EGEDAFLLGRGRHER 374
Cdd:TIGR01612 1543 KKDSEIIIKEIkDAHKKFILEAEKSEQ 1569
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
154-354 |
9.72e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 43.21 E-value: 9.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 154 ELEMLRVKVKELESS-EDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNA 232
Cdd:COG0419 168 KYEKLSELLKEVIKEaKAKIEELEGQLSELLEDIEDLLEALEEELKELKKLEEIQEEQEEEELEQEIEALEERLAELEEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 233 STFLERNDLRIEDGISStlsskeskrkgsldylkqvenetrdKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEE 312
Cdd:COG0419 248 KERLEELKARLLEIESL-------------------------ELEALKIREEELRELERLLEELEEKIERLEELEREIEE 302
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1720408942 313 LKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKEL 354
Cdd:COG0419 303 LEEELEGLRALLEELEELLEKLKSLEERLEKLEEKLEKLESE 344
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
14-347 |
1.03e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.14 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 14 RHLRFKLQSLSRRLDELEEATKNL---QRAEDELLDLQDKVIQAEGSDSSTLAEievLRQRVLKIEGKDEEIKRAEDLCH 90
Cdd:COG5022 758 RYLRRRYLQALKRIKKIQVIQHGFrlrRLVDYELKWRLFIKLQPLLSLLGSRKE---YRSYLACIIKLQKTIKREKKLRE 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 91 TMKEKLEEEENLTRELKSEIERLQKRMVDLEKlEEALSRSKNEcsqlclSLNEERNLT--KKISSELEMLRVKVKELESS 168
Cdd:COG5022 835 TEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKK-ETIYLQSAQR------VELAERQLQelKIDVKSISSLKLVNLELESE 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 169 EDRLDKTEQSlvSELEKLKSLTLSFVNERKYLNEKEKENEKIIKeltqkLEQNKKMNRDHMRNAS---TFLERNDLRIED 245
Cdd:COG5022 908 IIELKKSLSS--DLIENLEFKTELIARLKKLLNNIDLEEGPSIE-----YVKLPELNKLHEVESKlkeTSEEYEDLLKKS 980
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 246 GIS-STLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRA---KNN 321
Cdd:COG5022 981 TILvREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLKGLlllENN 1060
|
330 340
....*....|....*....|....*.
gi 1720408942 322 DLQDNYLTELNRNRSLASQLEEIKLQ 347
Cdd:COG5022 1061 QLQARYKALKLRRENSLLDDKQLYQL 1086
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
81-413 |
1.08e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.28 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 81 EIKRAEDLCHTMKE---KLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEM 157
Cdd:PTZ00440 496 YQEKVDELLQIINSikeKNNIVNNNFKNIEDYYITIEGLKNEIEGLIELIKYYLQSIETLIKDEKLKRSMKNDIKNKIKY 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 158 LR---VKVKELESSEDRLDKTEQslvsELEKLKSLTLSfvNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMrnaST 234
Cdd:PTZ00440 576 IEenvDHIKDIISLNDEIDNIIQ----QIEELINEALF--NKEKFINEKNDLQEKVKYILNKFYKGDLQELLDEL---SH 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 235 FLERNdlriedgisstlsSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNkvkdlNQEIEKLKTQIKHFESLEEELK 314
Cdd:PTZ00440 647 FLDDH-------------KYLYHEAKSKEDLQTLLNTSKNEYEKLEFMKSDNI-----DNIIKNLKKELQNLLSLKENII 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 315 KMRAKN--NDLQDNYLTELNRNRSLASQLEEIKLQVRKQKELGNGDIEGEDAFLLGRGRHERTKLKGHGSEASVSKHtsr 392
Cdd:PTZ00440 709 KKQLNNieQDISNSLNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQY--- 785
|
330 340
....*....|....*....|.
gi 1720408942 393 elspqhkRERLRNREFALSNE 413
Cdd:PTZ00440 786 -------KDTILNKENKISND 799
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
25-364 |
1.19e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 25 RRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAE-----------IEVLRQRVLKiegKDEEIKRAEDLCHTMK 93
Cdd:PTZ00121 1134 RKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEdakkaeaarkaEEVRKAEELR---KAEDARKAEAARKAEE 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 94 EKLEEEENLTRELK--SEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRvKVKELESSEDR 171
Cdd:PTZ00121 1211 ERKAEEARKAEDAKkaEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR-KADELKKAEEK 1289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 172 LDKTEQSLVSELEKLKSLtlsfvnerkylnEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDLRIEDGISSTL 251
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEA------------KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 252 SSKESKRKGSLDYLKQveNETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKM-RAKNNDLQDNYLTE 330
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKK--EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAdEAKKKAEEKKKADE 1435
|
330 340 350
....*....|....*....|....*....|....
gi 1720408942 331 LNRNRSLASQLEEIKLQVRKQKELGNGDIEGEDA 364
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
27-345 |
1.29e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.53 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 27 LDELEEATK--NLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLrqrvLKIEGKD-EEIKRAEDLchtmkekleeeenlT 103
Cdd:pfam06160 69 LFEAEELNDkyRFKKAKKALDEIEELLDDIEEDIKQILEELDEL----LESEEKNrEEVEELKDK--------------Y 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 104 RELKSEIerLQKRM---VDLEKLEEALSRSKNECSQLcLSLNEE------RNLTKKISSELEMLRVKVKELEsseDRLDK 174
Cdd:pfam06160 131 RELRKTL--LANRFsygPAIDELEKQLAEIEEEFSQF-EELTESgdyleaREVLEKLEEETDALEELMEDIP---PLYEE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 175 TEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEkiIKELTQKLEQNKKM-NRDHMRNASTFLERNDLRIeDGISSTL-- 251
Cdd:pfam06160 205 LKTELPDQLEELKEGYREMEEEGYALEHLNVDKE--IQQLEEQLEENLALlENLELDEAEEALEEIEERI-DQLYDLLek 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 252 --SSK---ESKRKGSLDYLKQVENETRD-KSENE---KN---RNQEDNKVKDLNQEIEKLKTQikhFESLEEELKKMRAK 319
Cdd:pfam06160 282 evDAKkyvEKNLPEIEDYLEHAEEQNKElKEELErvqQSytlNENELERVRGLEKQLEELEKR---YDEIVERLEEKEVA 358
|
330 340
....*....|....*....|....*.
gi 1720408942 320 NNDLQDNYLTELNRNRSLASQLEEIK 345
Cdd:pfam06160 359 YSELQEELEEILEQLEEIEEEQEEFK 384
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
108-220 |
1.36e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 108 SEIERLQKRMVDLEKLE------EALSRSKNECSQLCLSLNEERNLTKKISSELEmLRVKVKE--LESSEDRLDKTEQSL 179
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEaeaikkEALLEAKEEIHKLRNEFEKELRERRNELQKLE-KRLLQKEenLDRKLELLEKREEEL 112
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1720408942 180 VSELEKLKsltlsfvNERKYLNEKEKENEKIIKELTQKLEQ 220
Cdd:PRK12704 113 EKKEKELE-------QKQQELEKKEEELEELIEEQLQELER 146
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
28-349 |
1.47e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 28 DELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLchtmkekleeeENLTRELK 107
Cdd:TIGR00606 577 DWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDE-----------ESDLERLK 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 108 SEIERLQKRMVDL-------EKLEEALSRSKNECSQLC----LSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTE 176
Cdd:TIGR00606 646 EEIEKSSKQRAMLagatavySQFITQLTDENQSCCPVCqrvfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRR 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 177 QSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHM-RNASTFLERNDLRIEDGISSTLSSKE 255
Cdd:TIGR00606 726 DEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMpEEESAKVCLTDVTIMERFQMELKDVE 805
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 256 SKRKGSLDYLKQVENEtRDKSENEKNRNQEDNKVKDLNQEIEKLKtqiKHFESLEEELKKMRAKNNDLQDNYL---TELN 332
Cdd:TIGR00606 806 RKIAQQAAKLQGSDLD-RTVQQVNQEKQEKQHELDTVVSKIELNR---KLIQDQQEQIQHLKSKTNELKSEKLqigTNLQ 881
|
330
....*....|....*..
gi 1720408942 333 RNRSLASQLEEIKLQVR 349
Cdd:TIGR00606 882 RRQQFEEQLVELSTEVQ 898
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
25-315 |
1.61e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 25 RRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIE--GKDEEIKRAEDLCHTMKEKLEEEENL 102
Cdd:PTZ00121 1230 KKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADelKKAEEKKKADEAKKAEEKKKADEAKK 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 103 TRELKSEIERLQKRMVDLEKLEEALSRSKNEcsqlclslNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSE 182
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEE--------AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 183 LEKLKSLTLSFVNERKylnEKEKENEKIIKELTQKLEQNKKMnrDHMRNASTFLERND---LRIEDGISSTLSSKESKRK 259
Cdd:PTZ00121 1382 AAKKKAEEKKKADEAK---KKAEEDKKKADELKKAAAAKKKA--DEAKKKAEEKKKADeakKKAEEAKKADEAKKKAEEA 1456
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720408942 260 GSLDYLKQVENETRdKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKK 315
Cdd:PTZ00121 1457 KKAEEAKKKAEEAK-KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
21-361 |
1.77e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 42.40 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 21 QSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRV---------LKIEGkdEEIKRAEDLCHT 91
Cdd:pfam15921 475 EMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVdlklqelqhLKNEG--DHLRNVQTECEA 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 92 MKEKLEEEENLTRELKSEIERLQK------RMVDLEKLEEAlsRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKEL 165
Cdd:pfam15921 553 LKLQMAEKDKVIEILRQQIENMTQlvgqhgRTAGAMQVEKA--QLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 166 ESSEDRLDKTEQSLVSELEKLKSLTLSFVNE----RKYLNEKEKENEKIIKELTQKLEQNKKMN---RDHMRNASTFLE- 237
Cdd:pfam15921 631 ELEKVKLVNAGSERLRAVKDIKQERDQLLNEvktsRNELNSLSEDYEVLKRNFRNKSEEMETTTnklKMQLKSAQSELEq 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 238 -RNDLRIEDG-------ISSTLSSKESKRKGSLDYLKQ--------VENETRDKSENEKNRNQEDNKVKDLNQEIEKLKT 301
Cdd:pfam15921 711 tRNTLKSMEGsdghamkVAMGMQKQITAKRGQIDALQSkiqfleeaMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAG 790
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 302 QIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKELGNGDIEG 361
Cdd:pfam15921 791 ELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQG 850
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
16-353 |
2.02e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 16 LRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTL-------AEIEVLRQRVLKIEGKDEEIKRAEDL 88
Cdd:TIGR00606 191 LRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSReivksyeNELDPLKNRLKEIEHNLSKIMKLDNE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 89 CHTMKEKLEEEENLTRELKSEIERL----QKRMVDLEKLEEALSRSKNE----CSQLCLSLNEERNLTKKISSELEmlrV 160
Cdd:TIGR00606 271 IKALKSRKKQMEKDNSELELKMEKVfqgtDEQLNDLYHNHQRTVREKERelvdCQRELEKLNKERRLLNQEKTELL---V 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 161 KVKELESSEDRLDktEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMrnastflernd 240
Cdd:TIGR00606 348 EQGRLQLQADRHQ--EHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLC----------- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 241 lriedgisSTLSSKESKRKGSLDYLKQVENETRDKSENEKNR-NQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAK 319
Cdd:TIGR00606 415 --------ADLQSKERLKQEQADEIRDEKKGLGRTIELKKEIlEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERE 486
|
330 340 350
....*....|....*....|....*....|....
gi 1720408942 320 NNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKE 353
Cdd:TIGR00606 487 LSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKL 520
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
19-354 |
2.53e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 19 KLQSLSRRLDELEEATKNLQRAEDELLDlqdkviQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLCHTMKEKLEE 98
Cdd:TIGR00606 406 EAKTAAQLCADLQSKERLKQEQADEIRD------EKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 99 EENLTREL-----KSEIERLQKRMVDLEKLEEALSRSKNECSQLclslNEERNLTKKISSELEML-RVKVKELESSEDRL 172
Cdd:TIGR00606 480 LRKAERELskaekNSLTETLKKEVKSLQNEKADLDRKLRKLDQE----MEQLNHHTTTRTQMEMLtKDKMDKDEQIRKIK 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 173 DKTEQSLVSELEKL---KSLTLSFVNERKYLNEKEKENEKIIKELtQKLEQNKkmnrDHMRNASTFLERNDLRIEDGISS 249
Cdd:TIGR00606 556 SRHSDELTSLLGYFpnkKQLEDWLHSKSKEINQTRDRLAKLNKEL-ASLEQNK----NHINNELESKEEQLSSYEDKLFD 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 250 TLSSKESKRK-------------------GSLDYLKQVENETRDKSENEKNRNQEDNKVK-DLNQEIEKLKTQIKHF--- 306
Cdd:TIGR00606 631 VCGSQDEESDlerlkeeieksskqramlaGATAVYSQFITQLTDENQSCCPVCQRVFQTEaELQEFISDLQSKLRLApdk 710
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720408942 307 -ESLEEELKK-------------MRAKNNDLQDNYLTEL-NRNRSLASQLEEIKLQVRKQKEL 354
Cdd:TIGR00606 711 lKSTESELKKkekrrdemlglapGRQSIIDLKEKEIPELrNKLQKVNRDIQRLKNDIEEQETL 773
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
28-423 |
3.20e-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: 41.75 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 28 DELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKR----------------------- 84
Cdd:pfam12128 471 ERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELqlfpqagtllhflrkeapdweqs 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 85 ------AEDLCHTMKEKLEEEENLTRELKSEIERLQKRMVDLEK---LEEALsrsKNECSQLCLSLNEERNLTKKISSEL 155
Cdd:pfam12128 551 igkvisPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEwaaSEEEL---RERLDKAEEALQSAREKQAAAEEQL 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 156 EMLRVKVKELESSEDRldkTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTF 235
Cdd:pfam12128 628 VQANGELEKASREETF---ARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEE 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 236 LERNDLRIEDGISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKvKDLN------QEIEKLKTQIKHFESL 309
Cdd:pfam12128 705 QKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYK-RDLAslgvdpDVIAKLKREIRTLERK 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 310 EEELKKMRAKNNDLQDNYL-TELNRNRSLASQLEEIKLQVRkqkelgngDIEGEdaflLGRGRHE-RTKLKGHGSEASVS 387
Cdd:pfam12128 784 IERIAVRRQEVLRYFDWYQeTWLQRRPRLATQLSNIERAIS--------ELQQQ----LARLIADtKLRRAKLEMERKAS 851
|
410 420 430
....*....|....*....|....*....|....*.
gi 1720408942 388 KHTSRELSPQHKRERLRNREFALSNEHYSLSSKQAS 423
Cdd:pfam12128 852 EKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGS 887
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
28-245 |
3.80e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organisation and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 425563 [Multi-domain] Cd Length: 235 Bit Score: 40.01 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 28 DELEEATKNLQRAEDELLDLQDKVIQAEgsdsstlAEIEVLRQRVLKIEgkdEEIKRAEDLCHTMKEKLEEEENLTrelk 107
Cdd:pfam00261 8 EELDEAEERLKEAMKKLEEAEKRAEKAE-------AEVAALNRRIQLLE---EELERTEERLAEALEKLEEAEKAA---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 108 SEIERLQKrmvdleKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVK----ELESSEDRLDKTEqSLVSEL 183
Cdd:pfam00261 74 DESERGRK------VLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVvvegDLERAEERAELAE-SKIVEL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 184 EK--------LKSLTLSfvnERKYlNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTfLERNDLRIED 245
Cdd:pfam00261 147 EEelkvvgnnLKSLEAS---EEKA-SEREDKYEEQIRFLTEKLKEAETRAEFAERSVQK-LEKEVDRLED 211
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
29-325 |
3.80e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 41.30 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 29 ELEEATKNLQRAEDELLDLQDKvIQAEgsdSSTLAEIEVLRQRvlkIEGKDEEIkraEDLCHTMKEKLEEEENLTRELKS 108
Cdd:pfam01576 27 ELKELEKKHQQLCEEKNILAEQ-LQAE---TELFAEAEEMRAR---LAARKQEL---EEILHELEARLEEEEERSQQLQN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 109 EIERLQKRMVDLE-KLEE------ALSRSKNECSQLCLSLNEERNLTKKISSELEmlrvkvKELESSEDRLDKTEQSLVS 181
Cdd:pfam01576 97 EKKKMQQHIQDLEeQLEEeeaarqKLQLEKVTTEAKIKKMEEDILLLEDQNNKLQ------KERKLLEERISEFTSNLAE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 182 ELEKLKSltlsfvnerkyLNEKEKENEKIIKELTQKLEQNKKMnRDHMRNASTFLERNDLRIEDGIS----------STL 251
Cdd:pfam01576 171 EEEKSKS-----------LNKLKNKHEAMISDLEDRLKKEEKG-RQELEKAKRKLEGESSDLQEQIAelqaqiaelrAQL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720408942 252 SSKESKRKGSLDylkQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQ----IKHFESLEEELKKMRAKNNDLQD 325
Cdd:pfam01576 239 AKKEEELQAALA---RLEEETAQKNAALKKLRELEAQLSELQEDLESERAArakaEKQRRDLGEELEALKTELEDTLD 313
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
22-223 |
4.00e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 224259 [Multi-domain] Cd Length: 294 Bit Score: 40.43 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 22 SLSRRLDELEEATKNLQRAEDELLDLQDKVIQaegsDSSTLAEievlrqrvlKIEGKDEEIKRAEDLCHTMKEKLEEEEN 101
Cdd:COG1340 3 AMLDKLDELELKRKQLKEEIEELKEKRDELRK----EASELAE---------KRDELNAKVRELREKAQELREERDEINE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 102 LTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQ---------------------LCLSLNEERNLTKKISSELEMLRV 160
Cdd:COG1340 70 EVQELKEKRDEINAKLQELRKEYRELKEKRNEFNLggrsikslereierlekkqqtSVLTPEEERELVQKIKELRKELED 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720408942 161 KVKELESSEDRldkteQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKK 223
Cdd:COG1340 150 AKKALEENEKL-----KELKAEIDELKKKAREIHEKIQELANEAQEYHEEMIKLFEEADELRK 207
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
104-377 |
4.64e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 434900 [Multi-domain] Cd Length: 384 Bit Score: 40.43 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 104 RELKSEIERLQKRMVDLEKlEEALSRSKN-ECSQLCLSLNEER---------------NLTKKISS---ELEMLRVKVKE 164
Cdd:pfam15742 16 QQLRQDLQRLQILCTSAER-ELRYEREKNlDLKQHNSLLQEENikikaelkqaqqkllDSTKMCSSltaEWEHCQQKIRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 165 LESSEDRLDKTEQSLVS---ELEKLKS-----------------------LTLSFVNERKYLNEKEKENEKIIKELTQKL 218
Cdd:pfam15742 95 LELEVLKQAQSIKSQNSlqeKLAQEKSkvadaekkilelqqklehahkvcLTETCILEKKQLEEEIKEAQENEAKLKQQY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 219 --EQNKKMNRDHMRNASTFLERNDLRIEDGISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEI 296
Cdd:pfam15742 175 qeEQQKRKLLDQNVNELQQQVRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQELSEKLSSLQQEK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 297 EKLKTQIKHF-ESLEEELK-----------KMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKELGNGDIEGEDA 364
Cdd:pfam15742 255 EALQEELQQVlKQLDVHVRkynekhhhhkaKLRRAKDRLVHEVEQRDERIKQLENEIRILRQQIEKEKAFQKQVTAENDT 334
|
330
....*....|...
gi 1720408942 365 FLLgrgrhERTKL 377
Cdd:pfam15742 335 LLL-----EKRKL 342
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
262-346 |
4.66e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.39 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 262 LDYLKQVENETRDKSENEKNRNQEdnKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNrnrSLASQL 341
Cdd:smart00787 188 LRQLKQLEDELEDCDPTELDRAKE--KLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIA---EAEKKL 262
|
....*
gi 1720408942 342 EEIKL 346
Cdd:smart00787 263 EQCRG 267
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
37-380 |
4.93e-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: 428520 [Multi-domain] Cd Length: 660 Bit Score: 40.87 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 37 LQRAEDELLDLQDKVIQAEGSDSSTLAEIEvlRQRVLKIEGKDEEIKRAEDLCHTMKEKLEEEENLTRELKSEIERLQKR 116
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELE--RKASALARQLERESDRNQELQKRIRLLEKREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 117 MvdleKLEEALSRSKNECSQLCLSLNE-ERNLTKKIS--------SELEmLRVKVKELESSEDRLDKTEQSLvSELEKLK 187
Cdd:pfam05557 82 K----KNLEALNKKLNEKESQLADAREvISCLKNELSelrrqiqrQELE-LSSTNSELEELQERLDLQKAKA-QEAEQLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 188 SLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNAStfLERNDLRIEDGISSTLSSKESKrkgslDYLKQ 267
Cdd:pfam05557 156 QNLEAQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIPE--LERELERLREHNKHLNENIENK-----LLLKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 268 VENETRDKSENEKNRNQEdnkVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQ 347
Cdd:pfam05557 229 EVEDLKRKLEREEGYREE---LATLELEKEKLEQELKSWEKLAQDTGLNLRSPEDLSRRIEQLQQREITLKEENSSLTSS 305
|
330 340 350
....*....|....*....|....*....|...
gi 1720408942 348 VRkQKELGNGDIEGEDAFLLGRGRHERTKLKGH 380
Cdd:pfam05557 306 AR-QLEKAQRELEQELAQYLKNIEDLNKKLKRH 337
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
197-353 |
5.12e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 197 RKYLNEKEKENEKIIKELTQKLEQNKKmnrDHMRNASTflERNDLRIEdgisstlSSKESKRKgsLDYLKQVENETRDKS 276
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKK---EALLEAKE--EIHKLRNE-------FEKELRER--RNELQKLEKRLLQKE 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720408942 277 ENEKNRNQednkvkDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASqlEEIKLQVRKQKE 353
Cdd:PRK12704 96 ENLDRKLE------LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTA--EEAKEILLEKVE 164
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal domain of peptidoglycan hydrolase CwlO [Function unknown]; |
28-217 |
5.85e-03 |
|
Uncharacterized N-terminal domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 226400 [Multi-domain] Cd Length: 265 Bit Score: 39.70 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 28 DELEEATKNLQRAEDELLDLQDKViqaegsdSSTLAEIEVLRQRVLKIEgkdEEIKraedlchtmkekleeeenltrELK 107
Cdd:COG3883 38 SKLSELQKEKKNIQNEIESLDNQI-------EEIQSKIDELQKEIDQSK---AEIK---------------------KLQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 108 SEIERLQKRMVDLEKLEEALSRS--KNECSQLCL-------SLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQS 178
Cdd:COG3883 87 KEIAELKENIVERQELLKKRARAmqVNGTATSYIdvilnskSFSDLISRVTAISVIVDADKKILEQQKEDKKSLEEKQAA 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 1720408942 179 LVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQK 217
Cdd:COG3883 167 LEDKLETLVALQNELETQLNSLNSQKAEKNALIAALAAK 205
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
15-354 |
7.32e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 15 HLRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSD-------------SSTLAEIEVLRQRVL-----KIE 76
Cdd:TIGR00618 390 TLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQelqqryaelcaaaITCTAQCEKLEKIHLqesaqSLK 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 77 GKDEEIKRAEDLCHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTK---KISS 153
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETseeDVYH 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 154 ELEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSL---TLSFVNERKYLNEKEKENEKIIKELTQKL------EQNKKM 224
Cdd:TIGR00618 550 QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDipnLQNITVRLQDLTEKLSEAEDMLACEQHALlrklqpEQDLQD 629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 225 NRDHMRNAS-------TFLERNDL-----RIEDGISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDL 292
Cdd:TIGR00618 630 VRLHLQQCSqelalklTALHALQLtltqeRVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLREL 709
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720408942 293 NQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKEL 354
Cdd:TIGR00618 710 ETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVT 771
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
11-223 |
7.80e-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: 40.44 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 11 ASNRHLRFKLQSLSRRLDELEEATKNLQRAEDElLDLQDKVIQAEGSDS-----STLAEIEVLRQRVLKIEGKDEEIKRA 85
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRID-LKEQIKSIEKEIENLngkkeELEEELEELEAALRDLESRLGDLKKE 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 86 EDlchTMKEKLEEEENLTRELKSEIERLQKRMVDL-EKLEEALSRSKnecsqlclSLNEERNLTKKISSELEMLRVKVKE 164
Cdd:TIGR02169 891 RD---ELEAQLRELERKIEELEAQIEKKRKRLSELkAKLEALEEELS--------EIEDPKGEDEEIPEEELSLEDVQAE 959
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720408942 165 LESSEDRLDKTEQSLVSELEKLKSlTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKK 223
Cdd:TIGR02169 960 LQRVEEEIRALEPVNMLAIQEYEE-VLKRLDELKEKRAKLEEERKAILERIEEYEKKKR 1017
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
8-188 |
9.40e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 40.25 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 8 KDAASNRHLRFKLQSLSRRLDELEEATKNLQRAEDELLDL---QDKVIQAEgsdsstlaEIEVLRQRVlkiegkdeeikr 84
Cdd:COG3096 503 REGPDQRHLAEQVQPLRMRLSELEQRLRQQQSAERLLADFckrQGKNLDAE--------ELEALHQEL------------ 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408942 85 aEDLCHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKE 164
Cdd:COG3096 563 -EALIESLSDSVSNAREQRMALRQEQEQLQSRIQSLMQRAPVWLAAQNALEQLSEQSGEEFTDSQDVTEYMQQLLERERE 641
|
170 180
....*....|....*....|....
gi 1720408942 165 LESSEDRLDKTEQSLVSELEKLKS 188
Cdd:COG3096 642 ATVERDELGARKNALDEEIERLSQ 665
|
|
|