|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
31-387 |
9.20e-103 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 313.01 E-value: 9.20e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 31 QEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKF 110
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 111 KAEHDQLLLNYAKKesdlngaqiklreyeaalnskdaalataLGDKKSLESDLEDLKdqiaqleaslaaakKQLADETLL 190
Cdd:pfam00038 81 RLAAEDFRQKYEDE----------------------------LNLRTSAENDLVGLR--------------KDLDEATLA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 191 KVDLENRCQSLTEDLEFRKNMYEEEINETRRKH--ETRLVEVDSGRQIEyeykLAQALHEMREQHDAQVKLYKEELEQTY 268
Cdd:pfam00038 119 RVDLEAKIESLKEELAFLKKNHEEEVRELQAQVsdTQVNVEMDAARKLD----LTSALAEIRAQYEEIAAKNREEAEEWY 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 269 HAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLAKERDNSRRMLSDKEREMAE 348
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQE 274
|
330 340 350
....*....|....*....|....*....|....*....
gi 157074106 349 IRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEER 387
Cdd:pfam00038 275 TRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| LTD |
pfam00932 |
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ... |
439-543 |
2.35e-23 |
|
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.
Pssm-ID: 460003 [Multi-domain] Cd Length: 108 Bit Score: 94.80 E-value: 2.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 439 TGNVCIEEIDVDG-----KFIRLKNTSEQDQPMGGWEMIRKIGDTsvsYKYTSRYVLKAGQTVTIWAANAGVTAS----P 509
Cdd:pfam00932 4 TGDVVISEVVYDGsggndEFIELYNTGSKAVDLSGWKLQDASGGT---YTFPNGTTLAPGQTVVVWTGSGTNSATagywG 80
|
90 100 110
....*....|....*....|....*....|....
gi 157074106 510 PTDLIWKNQNSWgtgedvkVILKNSQGEEVAQRS 543
Cdd:pfam00932 81 PSNAVWNNGGDA-------VALYDANGELVDSVG 107
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10-349 |
1.03e-16 |
|
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: 83.95 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 10 RSGSRAGGPAtplsPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEvrgreltglkalyetELADA 89
Cdd:TIGR02168 657 PGGVITGGSA----KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEE---------------ELEQL 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 90 RRALDDTARERAKLQIELGKFKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLESDLEDLKDQ 169
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 170 IAQLEASLAAAKKQLADETLLKVDLENRCqsltEDLEFRKNMYEEEINETRRKHETRLVEVDS-GRQIEyeyKLAQALHE 248
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERL----ESLERRIAATERRLEDLEEQIEELSEDIESlAAEIE---ELEELIEE 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 249 MREQHDAQVKLYKEELEQTYHAKLENARLSSEMNTST---------VNSAREELMESRMRIESLSSQLSNLQK----ESR 315
Cdd:TIGR02168 871 LESELEALLNERASLEEALALLRSELEELSEELRELEskrselrreLEELREKLAQLELRLEGLEVRIDNLQErlseEYS 950
|
330 340 350
....*....|....*....|....*....|....
gi 157074106 316 ACLERIQELEDLLAKERDNSRRMLSDKEREMAEI 349
Cdd:TIGR02168 951 LTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
33-363 |
9.66e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 9.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 33 KEELRELndRLAVYIDKVRSLETENSALQLQVTEREEVRgRELTGLKALYETELADARRALDDTARERAKLQIELGKFKA 112
Cdd:TIGR02168 219 KAELREL--ELALLVLRLEELREELEELQEELKEAEEEL-EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 113 EhdqlllnYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLESDLEDLKDQIAQLEASLAAAKKQLADETLLKV 192
Cdd:TIGR02168 296 E-------ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 193 DLENRCQSLTEDLEFRKNmyeeeinetrrkhetrlvevdsgrqieyeyKLAQALHEMrEQHDAQVKLYKEELEQtyhAKL 272
Cdd:TIGR02168 369 ELESRLEELEEQLETLRS------------------------------KVAQLELQI-ASLNNEIERLEARLER---LED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 273 ENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKEsracLERIQELEDLLAKERDNSRRMLSDKEREMAEIR-- 350
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE----LERLEEALEELREELEEAEQALDAAERELAQLQar 490
|
330
....*....|....
gi 157074106 351 -DQMQQQLNDYEQL 363
Cdd:TIGR02168 491 lDSLERLQENLEGF 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
31-280 |
2.71e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 31 QEKEELRELNDRLAVYIDKVRSLETENSALQLQVtEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKF 110
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLEL-EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 111 KAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLESDLEDLKDQIAQLEASLAAAKKQLADETLL 190
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 191 KVDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQI-EYEYKLAQALHEMREQHDAQVKLYKEELEQTYH 269
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAaEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250
....*....|.
gi 157074106 270 AKLENARLSSE 280
Cdd:COG1196 482 LLEELAEAAAR 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
30-370 |
8.96e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 8.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 30 LQEKEELRELNdrlaVYIDKVRSLETENSALQLQVTEREEVRgRELTGLKALYETELADARRALDDTARERAKLQIELGK 109
Cdd:COG1196 218 LKEELKELEAE----LLLLKLRELEAELEELEAELEELEAEL-EELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 110 FKAEHDQLllnyakkESDLNGAQIKLREYEAALNSKDAALATALGDKKSLESDLEDLKDQIAQLEASLAAAKKQLADETL 189
Cdd:COG1196 293 LLAELARL-------EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 190 LKVDLEnrcQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVKLYKEELEQTYH 269
Cdd:COG1196 366 ALLEAE---AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 270 AKLEnarlssemntstvnsAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLAKERDNSRRMLSDKEREMAEI 349
Cdd:COG1196 443 ALEE---------------AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
330 340
....*....|....*....|.
gi 157074106 350 RDQMQQQLNDYEQLLDVKLAL 370
Cdd:COG1196 508 EGVKAALLLAGLRGLAGAVAV 528
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
119-388 |
7.37e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 7.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 119 LNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLESDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRC 198
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 199 QSLTEDLEFRKnmyEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVKLYKEELEQTyHAKLENARLS 278
Cdd:COG1196 298 ARLEQDIARLE---ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA-EEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 279 SEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLAKERDNSRRMLSDKEREMAEIRDQMQQQLN 358
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270
....*....|....*....|....*....|
gi 157074106 359 DYEQLLDVKLALDMEISAYRKLLEGEEERL 388
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELL 483
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
136-390 |
1.27e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 136 REYEAALNSKDAALAtaLGDKKSLESDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLefrknmyeEE 215
Cdd:COG1196 216 RELKEELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--------EE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 216 INETRRKHETRLVEVDsgRQIEYEYKLAQALHEMREQHDAQVKLYKEELEQTyHAKLENARLSSEMNTSTVNSAREELME 295
Cdd:COG1196 286 AQAEEYELLAELARLE--QDIARLEERRRELEERLEELEEELAELEEELEEL-EEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 296 SRMRIESLSSQLSNLQKESRACLERIQELEDLLAKERDNSRRMLSDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEIS 375
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
250
....*....|....*
gi 157074106 376 AYRKLLEGEEERLKL 390
Cdd:COG1196 443 ALEEAAEEEAELEEE 457
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
80-389 |
2.95e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 80 ALYETELADARRALDDTARERAKLQIELGKFKAEHDQLLLNYAKKES--DLngaQIKLREYEAALnskdaalatalgdkk 157
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqAL---LKEKREYEGYE--------------- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 158 sLESDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFR----KNMYEEEINETRRKHETRLVEVDSG 233
Cdd:TIGR02169 228 -LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkiKDLGEEEQLRVKEKIGELEAEIASL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 234 RQIEYEYKL-AQALHEMREQHDAQVKLYKEELEQtYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQK 312
Cdd:TIGR02169 307 ERSIAEKEReLEDAEERLAKLEAEIDKLLAEIEE-LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD 385
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157074106 313 ESRACLERIQELEDllakERDNSRRMLSDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEERLK 389
Cdd:TIGR02169 386 ELKDYREKLEKLKR----EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
10-327 |
3.33e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 10 RSGSRAGGPATPLSPTRLSRlQEKEELRELNDR-------LAVYIDKVRSLETENSALQ--LQVTERE----EVRGRELT 76
Cdd:TIGR02169 651 KSGAMTGGSRAPRGGILFSR-SEPAELQRLRERleglkreLSSLQSELRRIENRLDELSqeLSDASRKigeiEKEIEQLE 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 77 GLKALYETELADARRALDDTARERAKLQIELGKFKAEHDQLLLNYAKK-------ESDLNGAQIK--------------- 134
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLeealndlEARLSHSRIPeiqaelskleeevsr 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 135 ----LREYEAALNSKDAALATALGDKKSLESDLEDLKDQIAQLEASLAAAKKQLAD------ETLLKV-DLENRCQSLTE 203
Cdd:TIGR02169 810 iearLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEleeeleELEAALrDLESRLGDLKK 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 204 DLEFRKNMYEE------EINETRRKHETRLVEVDSGRQIEyEYKLAQALHEMRE-QHDAQVKLYKEELEQTYHAKLENAR 276
Cdd:TIGR02169 890 ERDELEAQLRElerkieELEAQIEKKRKRLSELKAKLEAL-EEELSEIEDPKGEdEEIPEEELSLEDVQAELQRVEEEIR 968
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 157074106 277 LSSEMNtstvNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDL 327
Cdd:TIGR02169 969 ALEPVN----MLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
25-325 |
4.89e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 4.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 25 TRLSRLQ----EKEELRELNDRLAVY-----IDKVRSLETENSALQLQVTEREEvrgrELTGLKALYE---TELADARRA 92
Cdd:TIGR02169 198 QQLERLRrereKAERYQALLKEKREYegyelLKEKEALERQKEAIERQLASLEE----ELEKLTEEISeleKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 93 LDDTAR--------ERAKLQIELGKFKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAalatalgDKKSLESDLE 164
Cdd:TIGR02169 274 LEELNKkikdlgeeEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA-------EIEELEREIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 165 DLKDQIAQLEASLAAAKKQLADetllkvdLENRCQSLTEDLE--FRKNM-YEEEINETRRKHEtrlvevDSGRQIEYEYK 241
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEELED-------LRAELEEVDKEFAetRDELKdYREKLEKLKREIN------ELKRELDRLQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 242 LAQALHEMREQHDAQVKLYKEELEQtYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERI 321
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINE-LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
....
gi 157074106 322 QELE 325
Cdd:TIGR02169 493 AEAE 496
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
34-354 |
4.90e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 34 EELRELNDRLAVYIDKVRSLETENSALQLQVTEREEvrgrELTGLkalyETELADARRALDDTARERAKLQIELGKFKAE 113
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRRE----EIEEL----EEEIEELRERFGDAPVDLGNAEDFLEELREE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 114 HDQLLLNYAKKESDLNGAQIKLREYEAALNS----------KDAALATALGDKK----SLESDLEDLKDQIAQLEASLAA 179
Cdd:PRK02224 421 RDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEDRerveELEAELEDLEEEVEEVEERLER 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 180 AKKQLADETLLKVDLENRcqsltEDLEFRKNMYEEEINETRRKhetrlvevdsgrqieyeyklAQALHEMREQHDAQVKl 259
Cdd:PRK02224 501 AEDLVEAEDRIERLEERR-----EDLEELIAERRETIEEKRER--------------------AEELRERAAELEAEAE- 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 260 YKEELEQTYHAKLENARLSsemnTSTVNSAREELMESRMRIESLSSQLSNLQkESRACLERIQELEDLLAKERDNSRRML 339
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREE----VAELNSKLAELKERIESLERIRTLLAAIA-DAEDEIERLREKREALAELNDERRERL 629
|
330
....*....|....*
gi 157074106 340 SDKEREMAEIRDQMQ 354
Cdd:PRK02224 630 AEKRERKRELEAEFD 644
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
147-379 |
2.61e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 147 AALATALGDKKSLESDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTE---DLEFRKNMYEEEINETRRKH 223
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 224 ETrlVEVDSGRQIEYEYKLAQALHEMREQHDAQVKLYKEELEQTYHakleNARLSSEMNTSTVNSArEELMESRMRIESL 303
Cdd:COG4942 93 AE--LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVR----RLQYLKYLAPARREQA-EELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157074106 304 SSQLSNLQKESRACLERIQELEDLLAKERDNSRRMLSDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRK 379
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
85-335 |
4.50e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 85 ELADARRALDDTARERAKLQIELGKFKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLESDLE 164
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 165 DLKDQIAQLEASLAAAKKQLADETLLKVDLENRcqsltedlEFRKNMYEEEINETRRKHETRLVEVDSgrqieyeyKLAQ 244
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLD--------AVRRLQYLKYLAPARREQAEELRADLA--------ELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 245 ALHEMREQHDAQVKLYKEELEQtyHAKLENARlssemntstvNSAREELMESRMRIESLSSQLSNLQKESRACLERIQEL 324
Cdd:COG4942 165 LRAELEAERAELEALLAELEEE--RAALEALK----------AERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
250
....*....|.
gi 157074106 325 EDLLAKERDNS 335
Cdd:COG4942 233 EAEAAAAAERT 243
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
28-387 |
3.35e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 28 SRLQEKEELRELNDRLAVYIDKVRSLETENSalqlqvTEREEVRGReltglkalyeteLADARRALDDTARERAKLQIEL 107
Cdd:PRK02224 241 EVLEEHEERREELETLEAEIEDLRETIAETE------REREELAEE------------VRDLRERLEELEEERDDLLAEA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 108 GKFKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLESDLEDLKDQIAQLEASLAAAKKQLAD- 186
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDr 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 187 -----------ETLLK------VDLENrCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEYK-------- 241
Cdd:PRK02224 383 reeieeleeeiEELRErfgdapVDLGN-AEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpv 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 242 ----LAQALHEMREQHD------AQVKLYKEELEQTYH-----AKLENARLSSEMNTSTVNS----AREELMESRMRIES 302
Cdd:PRK02224 462 egspHVETIEEDRERVEeleaelEDLEEEVEEVEERLEraedlVEAEDRIERLEERREDLEEliaeRRETIEEKRERAEE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 303 LSSQLSNLQKESRACLERIQELEDllakERDNSRRMLSDKEREMAEIRDQMqQQLNDYEQLLDVKLALDMEISAYRKLLE 382
Cdd:PRK02224 542 LRERAAELEAEAEEKREAAAEAEE----EAEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKRE 616
|
....*
gi 157074106 383 GEEER 387
Cdd:PRK02224 617 ALAEL 621
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
84-367 |
3.74e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 84 TELADARRALDDtARERAKLqieLGKFKAEHDQlllnYAKKESDLNgaqiKLREYEAALNSKDAALATALgdkksLESDL 163
Cdd:COG4913 235 DDLERAHEALED-AREQIEL---LEPIRELAER----YAAARERLA----ELEYLRAALRLWFAQRRLEL-----LEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 164 EDLKDQIAQLEASLAAAKKQLADEtllkvdlenrcqsltedlefrknmyEEEINETRRKHETrlvevDSGRQIEyeyKLA 243
Cdd:COG4913 298 EELRAELARLEAELERLEARLDAL-------------------------REELDELEAQIRG-----NGGDRLE---QLE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 244 QALHEMREQHDAQvklykEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQE 323
Cdd:COG4913 345 REIERLERELEER-----ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 157074106 324 LEDLLAKERDNSRRMLSDKEREMAEIRDQMQQQLNDYEQ-------LLDVK 367
Cdd:COG4913 420 ELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAelpfvgeLIEVR 470
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
41-330 |
6.31e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 41 DRLAVYIDKVRSLETENSALQLQVTEREEVRgRELTGLKALYETeLADARRALDDTARerakLQIELGKFKAEHDQLLLN 120
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAEL-DALQERREALQR-LAEYSWDEIDVAS----AEREIAELEAELERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 121 yakkESDLNGAQIKLREYEAALNSKDAALATALGDKKSLESDLEDLKDQIAQLEASLAAAKKQLADETLLkvDLENRCQS 200
Cdd:COG4913 684 ----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--LLEERFAA 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 201 LTEDL---EFRKNMYEE--EINETRRKHETRLVEVDSGRQIEYEYKLAQ------ALHEMREQHDaqvKLYKEELEQtYH 269
Cdd:COG4913 758 ALGDAverELRENLEERidALRARLNRAEEELERAMRAFNREWPAETADldadleSLPEYLALLD---RLEEDGLPE-YE 833
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157074106 270 AKLENARLSSEmntstvnsareelmesrmrIESLSSQLSNLQKESRACLERIQELEDLLAK 330
Cdd:COG4913 834 ERFKELLNENS-------------------IEFVADLLSKLRRAIREIKERIDPLNDSLKR 875
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
83-229 |
6.61e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 83 ETELADARRALDDTARERAKLQIELGKFKAEHDQLLLNYAKKESDLNGAQIKLREYEAAL----NSKDAalatalgdkKS 158
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrNNKEY---------EA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157074106 159 LESDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVE 229
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
28-389 |
7.31e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 7.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 28 SRLQE-KEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYEtelaDARRALDDTARERAKLQIE 106
Cdd:PRK03918 338 ERLEElKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE----ELEKAKEEIEEEISKITAR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 107 LGKFKAEHDQLL-----LNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLESDLEDLKDQIAQLEASLAAAK 181
Cdd:PRK03918 414 IGELKKEIKELKkaieeLKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 182 KQLADETLLK--VDLENRCQSLT-EDLEFRKNMYEEEINETRR-KHETRLVEVDSGRQIEYEYKLAQALHEMREqhdaqv 257
Cdd:PRK03918 494 ELIKLKELAEqlKELEEKLKKYNlEELEKKAEEYEKLKEKLIKlKGEIKSLKKELEKLEELKKKLAELEKKLDE------ 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 258 klyKEELEQTYHAKLENARLSSEmntstvnsarEELMESRMRIESLSSQLSNLqKESRACLERIQELEDLLAKERDNSRR 337
Cdd:PRK03918 568 ---LEEELAELLKELEELGFESV----------EELEERLKELEPFYNEYLEL-KDAEKELEREEKELKKLEEELDKAFE 633
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 157074106 338 MLSDKEREMAEIRDQMQQQL-----NDYEQLLDVKLALDMEISAYRKLLEGEEERLK 389
Cdd:PRK03918 634 ELAETEKRLEELRKELEELEkkyseEEYEELREEYLELSRELAGLRAELEELEKRRE 690
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
57-286 |
8.65e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 57 NSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELG--KFKAEHDQLLLNYAKKESDLNGAQIK 134
Cdd:COG3206 155 NALAEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 135 LREYEAALNSKDAALATALGDKKSLESD--LEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKNMY 212
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 213 EEEINETRRKHETRLVEVDSgRQIEYEYKLAQA------LHEMREQHDAQVKLYkeeleQTYHAKLENARLSSEMNTSTV 286
Cdd:COG3206 315 LASLEAELEALQAREASLQA-QLAQLEARLAELpeleaeLRRLEREVEVARELY-----ESLLQRLEEARLAEALTVGNV 388
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
30-386 |
1.08e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.56 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 30 LQEKEELRELNDRLA------VYIDKVRSLETENSALQLQVTE-REEVRGRELTGLKalyeTELADARRALDDTARERAK 102
Cdd:pfam05483 421 LDEKKQFEKIAEELKgkeqelIFLLQAREKEIHDLEIQLTAIKtSEEHYLKEVEDLK----TELEKEKLKNIELTAHCDK 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 103 LQIELGKFKAEHDQLLLNYAKKESDLNGAQiklREYEAALNSKDAALATALGDKKSLESDLEDLKDQIAQLEASLAAAKK 182
Cdd:pfam05483 497 LLLENKELTQEASDMTLELKKHQEDIINCK---KQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEE 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 183 Q--------LADETLLKVdLENRCQSLTEDLEfRKNMYEEEINETRRKHETRlVEVDSGRQIEYEYKLAQALHEMreqhd 254
Cdd:pfam05483 574 NarsieyevLKKEKQMKI-LENKCNNLKKQIE-NKNKNIEELHQENKALKKK-GSAENKQLNAYEIKVNKLELEL----- 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 255 AQVKLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLAKERDN 334
Cdd:pfam05483 646 ASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDS 725
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 157074106 335 SRRMLSDKEREMAEIRDQMQQQLNDYE-QLLDVKLALDMEISAYRKLLEGEEE 386
Cdd:pfam05483 726 ELGLYKNKEQEQSSAKAALEIELSNIKaELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
120-205 |
1.25e-05 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 47.80 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 120 NYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLESDLEDLKDQIAQL-EASLAAAKKQLADETLLKVDLENRC 198
Cdd:TIGR04320 262 KLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTaQNNLATAQAALANAEARLAKAKEAL 341
|
....*..
gi 157074106 199 QSLTEDL 205
Cdd:TIGR04320 342 ANLNADL 348
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
28-225 |
1.27e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 28 SRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEvRGRELTGLKALYETELADARRALDDTARERAKLQIEL 107
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-RIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 108 GKFKAEHDQLLLNYAKKE-----------SDLNGAqIKLREYEAALNSKDAALATALGDKKsleSDLEDLKDQIAQLEAS 176
Cdd:COG4942 100 EAQKEELAELLRALYRLGrqpplalllspEDFLDA-VRRLQYLKYLAPARREQAEELRADL---AELAALRAELEAERAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 157074106 177 LAAAKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEEINETRRKHET 225
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
22-360 |
1.98e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 22 LSPTRLSRLQEKEELRELNDRLAV---YIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTAR 98
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEEleeRLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 99 ERAKLQIELGKFKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLESDLEDLKDQIAQLEASLA 178
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 179 AA-------KKQLADETLLKVDLENRCQSLTE--------DLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEYKLA 243
Cdd:COG4717 287 ALlflllarEKASLGKEAEELQALPALEELEEeeleellaALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 244 QALHEM-----------REQHDAQVKLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQK 312
Cdd:COG4717 367 ELEQEIaallaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEE 446
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 157074106 313 ESRACLERIQELEDLLAKERDNSRrmLSDKEREMAEIRDQMQQQLNDY 360
Cdd:COG4717 447 ELEELREELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEEW 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
34-221 |
3.02e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 34 EELRELNDRLAVYIDKVRSLETENSALQLQVTEREevrgreltglKALYETELADARRALDDTARERAKLQIELGKFKAE 113
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRR----------LELLEAELEELRAELARLEAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 114 HDQLLLNYAKK--------ESDLNGAQIKLREYEAALNSKDAALA----TALGDKKSLESDLEDLKDQIAQLEASLAAAK 181
Cdd:COG4913 325 LDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLAalglPLPASAEEFAALRAEAAALLEALEEELEALE 404
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 157074106 182 KQLADETLLKVDLENRCQSLTEDLEF---RKNMYEEEINETRR 221
Cdd:COG4913 405 EALAEAEAALRDLRRELRELEAEIASlerRKSNIPARLLALRD 447
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
163-388 |
4.00e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 163 LEDLKDQIAQLEASLAAAKKQLADetllkvdLENRCQSLTEdlefrknmyeeeinetRRKHETRLVEVDsgrqiEYEYKL 242
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEA-------LEAELDALQE----------------RREALQRLAEYS-----WDEIDV 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 243 AQALHEMREqhdaqvklykeeLEQtyhaKLENARLSSemntSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQ 322
Cdd:COG4913 664 ASAEREIAE------------LEA----ELERLDASS----DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELE 723
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157074106 323 ELEDLLAKERDNSRRMLSDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEERL 388
Cdd:COG4913 724 QAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
88-395 |
5.36e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 88 DARRALDDTARERAKLQIELGKFKAEHDQLllnyakkESDLNGAQIKLREYEAALNSKDAALatalgDKKSLESDLEDLK 167
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEAL-------EAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 168 DQIAQLEAS---LAAAKKQLADETLLKVDLENRCQSLTEDLEfRKNMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQ 244
Cdd:COG4913 675 AELERLDASsddLAALEEQLEELEAELEELEEELDELKGEIG-RLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 245 ALHEmreqhdaqvkLYKEELEQTYHAKLENARlssEMNTSTVNSAREELMESRMR--------IESLSSQLSNLQkESRA 316
Cdd:COG4913 754 RFAA----------ALGDAVERELRENLEERI---DALRARLNRAEEELERAMRAfnrewpaeTADLDADLESLP-EYLA 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 317 CLERIQElEDLLAKERDNSRRMLSDKEREMAEIRDQMQQQLND-YEQLLDVKLALdmeisayRKLLEGEEERLKLSPSPS 395
Cdd:COG4913 820 LLDRLEE-DGLPEYEERFKELLNENSIEFVADLLSKLRRAIREiKERIDPLNDSL-------KRIPFGPGRYLRLEARPR 891
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
171-383 |
1.26e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.29 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 171 AQLEASLAAAKKQ---LADETLLKVDLENrcqslTEDLEFRKNMYEEEINETRRKhetrlvevdsgrqieyeykLAQALH 247
Cdd:PRK11281 39 ADVQAQLDALNKQkllEAEDKLVQQDLEQ-----TLALLDKIDRQKEETEQLKQQ-------------------LAQAPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 248 EMREQHDAQVKLYKEELEQTY--HAKLENARLSSEMN--TSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQE 323
Cdd:PRK11281 95 KLRQAQAELEALKDDNDEETRetLSTLSLRQLESRLAqtLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQ 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 324 LEDLLAKERDNSRrmlsdkeremaEIRDQMQQQLNDYEQLLDVKLALDmeisayRKLLEG 383
Cdd:PRK11281 175 IRNLLKGGKVGGK-----------ALRPSQRVLLQAEQALLNAQNDLQ------RKSLEG 217
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
243-389 |
1.35e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 243 AQALHEMREQHDAQVKLYK----EELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACL 318
Cdd:COG1196 215 YRELKEELKELEAELLLLKlrelEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157074106 319 ERIQELEDLLAKERDNSRRMLSDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEERLK 389
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
28-367 |
2.14e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.12 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 28 SRLQEKeeLRELNDRLAVYIDKVRSLETENSALQlQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIEL 107
Cdd:pfam07888 34 NRLEEC--LQERAELLQAQEAANRQREKEKERYK-RDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 108 GKFKAEHDQLLLNYAKKESdlngaqiKLREYEAALnskdAALATALGDKkslESDLEDLKDQIAQLEASLaaaKKQLADE 187
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEA-------RIRELEEDI----KTLTQRVLER---ETELERMKERAKKAGAQR---KEEEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 188 TLLKVDL---ENRCQSLTEDLEFRKNMYEEEINETRRKHE-----TRLVEVDSGRQIEYEYKLAQ--ALHEMREQHDAQV 257
Cdd:pfam07888 174 KQLQAKLqqtEEELRSLSKEFQELRNSLAQRDTQVLQLQDtittlTQKLTTAHRKEAENEALLEElrSLQERLNASERKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 258 KLYKEELEQTY------HAKLENARLSSEMNTSTVNSAREELMESRM------------------RIESLSSQLsnLQKE 313
Cdd:pfam07888 254 EGLGEELSSMAaqrdrtQAELHQARLQAAQLTLQLADASLALREGRArwaqeretlqqsaeadkdRIEKLSAEL--QRLE 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 157074106 314 SRACLERIQ--ELEDLLAKERDNSRRMLSDKEREMAEIRDQMQQQLNDYEQLLDVK 367
Cdd:pfam07888 332 ERLQEERMEreKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK 387
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
159-381 |
2.51e-04 |
|
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: 44.06 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 159 LESDLEDLKDQIAQLEASLAAAKKQL----ADETLLKVDLEN---RCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVD 231
Cdd:pfam12128 609 AEEALQSAREKQAAAEEQLVQANGELekasREETFARTALKNarlDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLE 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 232 sGRQIEYEYKLAQALHEMREQ---HDAQVKLYKEELEQTYHAKLenARLSSEMNTSTVNSARE--ELMESRMR------- 299
Cdd:pfam12128 689 -AQLKQLDKKHQAWLEEQKEQkreARTEKQAYWQVVEGALDAQL--ALLKAAIAARRSGAKAElkALETWYKRdlaslgv 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 300 -----------IESLSSQLSNLQKESRACLERIQELEDLLAKERDNSRRMLSDKEREMAEIRDQMQQQLNDYEqlLDVKl 368
Cdd:pfam12128 766 dpdviaklkreIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTK--LRRA- 842
|
250
....*....|...
gi 157074106 369 ALDMEISAYRKLL 381
Cdd:pfam12128 843 KLEMERKASEKQQ 855
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
61-250 |
3.30e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 61 QLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELgkfkaEHDQLLLNYAKKESDLNGAQIKLREYEA 140
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 141 ALnskdAALATALGDKKSLESDLEDLKDQIAQLEASLAAAKKQLADETLLKVdlenrcqsltEDLEFRKNMYEEEINETR 220
Cdd:COG4717 154 RL----EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL----------EELQQRLAELEEELEEAQ 219
|
170 180 190
....*....|....*....|....*....|
gi 157074106 221 RKHETRLVEVDSGRQIEYEYKLAQALHEMR 250
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEAR 249
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
86-362 |
3.86e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.79 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 86 LADARRALDDTARERAKLQIELGKFKAEHDQLLLNYAKKESDLNGA-------------QIKLREYEAALNSKDAALATA 152
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAAsdhlnlvqtalrqQEKIERYQEDLEELTERLEEQ 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 153 LGDKKSLESDLEDLKDQIAQLEASLAAAKKQLAD-------------------ETLLKVdlENRCQ--SLTED------L 205
Cdd:COG3096 367 EEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADyqqaldvqqtraiqyqqavQALEKA--RALCGlpDLTPEnaedylA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 206 EFRKNmyEEEINETRRKHETRL-VEVDSGRQIEYEYKLAQALH---EMREQHDAQVKLYKEELEQTYHAklenarlssem 281
Cdd:COG3096 445 AFRAK--EQQATEEVLELEQKLsVADAARRQFEKAYELVCKIAgevERSQAWQTARELLRRYRSQQALA----------- 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 282 ntSTVNSAREELMESRMRIESLSS---QLSNLQKESRACLERIQELEDLLAkERDNSRRMLSDKEREMAEIRDQMQQQLN 358
Cdd:COG3096 512 --QRLQQLRAQLAELEQRLRQQQNaerLLEEFCQRIGQQLDAAEELEELLA-ELEAQLEELEEQAAEAVEQRSELRQQLE 588
|
....
gi 157074106 359 DYEQ 362
Cdd:COG3096 589 QLRA 592
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
103-267 |
5.77e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.41 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 103 LQIELGKFKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGdkksLESDLEDLKDQIAQLEASLAAAKK 182
Cdd:pfam00529 49 FQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDG----ATAQLRAAQAAVKAAQAQLAQAQI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 183 QLAD-ETLLKVDLENRCQSLTEDLEFRKNmyEEEINETRRKHETRLVEVDSGRQieyeyKLAQALHEMREQHDAQVKLYK 261
Cdd:pfam00529 125 DLARrRVLAPIGGISRESLVTAGALVAQA--QANLLATVAQLDQIYVQITQSAA-----ENQAEVRSELSGAQLQIAEAE 197
|
....*.
gi 157074106 262 EELEQT 267
Cdd:pfam00529 198 AELKLA 203
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
29-338 |
6.82e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 29 RLQEKEELRELNDRLavyidkvRSLETENSALQLQVTERE---EVRGRELTGLKALyeteLADARRALDDTARERAKLQI 105
Cdd:pfam15921 529 KLQELQHLKNEGDHL-------RNVQTECEALKLQMAEKDkviEILRQQIENMTQL----VGQHGRTAGAMQVEKAQLEK 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 106 ELGKFKAEHDQLLLNYAKKESdlngaqiKLREYEAA---LNSKDAALATALGDKKSLESDLEDLKDQIA-QLEASLAAAK 181
Cdd:pfam15921 598 EINDRRLELQEFKILKDKKDA-------KIRELEARvsdLELEKVKLVNAGSERLRAVKDIKQERDQLLnEVKTSRNELN 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 182 KQLADETLLKVDLENRCQSL---TEDLEFRKNMYEEEINETRRKHETrlVEVDSGRQIEYEYKLAQALHEMREQHDA--- 255
Cdd:pfam15921 671 SLSEDYEVLKRNFRNKSEEMettTNKLKMQLKSAQSELEQTRNTLKS--MEGSDGHAMKVAMGMQKQITAKRGQIDAlqs 748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 256 QVKLYKEEL----EQTYHAKLENARLSSEMNT--STVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLA 329
Cdd:pfam15921 749 KIQFLEEAMtnanKEKHFLKEEKNKLSQELSTvaTEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQ 828
|
....*....
gi 157074106 330 KERDNSRRM 338
Cdd:pfam15921 829 RQEQESVRL 837
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
163-390 |
7.88e-04 |
|
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: 42.52 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 163 LEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSgrqieyeyKL 242
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADA--------AV 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 243 AQALHEMrEQHDAQVKLYKEELEQTYHAKLENA-RLSSEMNtsTVNSAREELMESRMRIESLSSQLSnlQKESRACLERI 321
Cdd:pfam12128 318 AKDRSEL-EALEDQHGAFLDADIETAAADQEQLpSWQSELE--NLEERLKALTGKHQDVTAKYNRRR--SKIKEQNNRDI 392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157074106 322 QELEDLLAKERDnsrrmlsDKEREMAEIRDQMQQQLNDYEQLLDVKLaLDMEISAYRKLLEGEEERLKL 390
Cdd:pfam12128 393 AGIKDKLAKIRE-------ARDRQLAVAEDDLQALESELREQLEAGK-LEFNEEEYRLKSRLGELKLRL 453
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
83-185 |
9.33e-04 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 41.64 E-value: 9.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 83 ETELADARRALDDTARERAKLQIELGKFKAEHDQLLLNYAKKESDLNGAQiklreyEAALNSKDAALATALGDKKSLESD 162
Cdd:TIGR04320 260 QAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQ------AQALQTAQNNLATAQAALANAEAR 333
|
90 100
....*....|....*....|...
gi 157074106 163 LEDLKDQIAQLEASLAAAKKQLA 185
Cdd:TIGR04320 334 LAKAKEALANLNADLAKKQAALD 356
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
242-389 |
1.05e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 242 LAQALHEMREQHDAqvklykEELEQTYHAKLENARLSSEMntstvnsaREELMESRMRIESLSSQLSNLQKESRACLERI 321
Cdd:COG2433 378 IEEALEELIEKELP------EEEPEAEREKEHEERELTEE--------EEEIRRLEEQVERLEAEVEELEAELEEKDERI 443
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157074106 322 QELEDLLAKERDNSRRmlsdKEREMAEIRdqmqqqlndyeqlldvklALDMEISAYRKLLEGEEERLK 389
Cdd:COG2433 444 ERLERELSEARSEERR----EIRKDREIS------------------RLDREIERLERELEEERERIE 489
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
234-398 |
1.42e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 234 RQIEYEYKLAQALHEMREQHDAQVKLYKEELEQTYH--AKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQ 311
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLReiNEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 312 KESRACLERIQELEDLLAKERDNSRRmLSDKEREMAEIRDQMQQQL---NDYEQLLDVKLALDMEISAYRKLLEGEEERL 388
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKAEEYIklsEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170
....*....|
gi 157074106 389 KLSPSPSSRV 398
Cdd:PRK03918 331 KELEEKEERL 340
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
33-386 |
1.56e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 33 KEELRELNDRLAVYIDKVRSLETENSALQLQVT-------EREEVRGRELTGLKALYETELADARRALDDTARERAKLQI 105
Cdd:pfam01576 698 KTQLEELEDELQATEDAKLRLEVNMQALKAQFErdlqardEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 106 ELGKFKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLESDLEDLKDQIAQLEASLAAAKKQLA 185
Cdd:pfam01576 778 DLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARR 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 186 DETLLKVDLENRCQSLTEDlefrKNMYEEEinetRRKHETRLVevdsgrQIEYEYKLAQALHEMREQHDAQVKLYKEELe 265
Cdd:pfam01576 858 QAQQERDELADEIASGASG----KSALQDE----KRRLEARIA------QLEEELEEEQSNTELLNDRLRKSTLQVEQL- 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 266 qtyhakleNARLSSEMNTSTVN-SAREEL----MESRMRIESLSSQLSNLQKESRACLE-RIQELEDLL---AKERDNSR 336
Cdd:pfam01576 923 --------TTELAAERSTSQKSeSARQQLerqnKELKAKLQEMEGTVKSKFKSSIAALEaKIAQLEEQLeqeSRERQAAN 994
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 157074106 337 RMLSDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEE 386
Cdd:pfam01576 995 KLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEE 1044
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
28-387 |
1.98e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 28 SRLQEKEElRELNDRLAvyidkvrSLETENSALQLQVTEREEVRGREltglkalyetelADARRALDDTARERAKLQIEL 107
Cdd:PRK02224 194 AQIEEKEE-KDLHERLN-------GLESELAELDEEIERYEEQREQA------------RETRDEADEVLEEHEERREEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 108 GKFKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLESDLEDLKDQIAQLEASLAAAKKQLADE 187
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEC 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 188 TLLKVDLENRCQSLTE---DLEFRKNMYEEEINETRRKHETRLVEVDSGR-QIEyeyKLAQALHEMREQ-HDAQVKL--- 259
Cdd:PRK02224 334 RVAAQAHNEEAESLREdadDLEERAEELREEAAELESELEEAREAVEDRReEIE---ELEEEIEELRERfGDAPVDLgna 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 260 --YKEELEQTyHAKLENARLSSEMNTSTVNSAREE-------------------------LMESRMRIESLSSQLSNLQK 312
Cdd:PRK02224 411 edFLEELREE-RDELREREAELEATLRTARERVEEaealleagkcpecgqpvegsphvetIEEDRERVEELEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 313 ESRACLERIQELEDL---------LAKERDNSRRMLSDKEREMAEIRDQMqQQLNDYEQLLDVKlALDMEISAYRKLLEG 383
Cdd:PRK02224 490 EVEEVEERLERAEDLveaedrierLEERREDLEELIAERRETIEEKRERA-EELRERAAELEAE-AEEKREAAAEAEEEA 567
|
....
gi 157074106 384 EEER 387
Cdd:PRK02224 568 EEAR 571
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
139-375 |
2.70e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 139 EAALNSKDAALATALGDKKSLESDLEDLKDQIAQLEASLAAAKKQLADETllkvDLENRCQSLTEDLEFRKNMYEEEINE 218
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAET----ELCAEAEEMRARLAARKQELEEILHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 219 TrrkhETRLVEvdsgrqieyEYKLAQALHEMREQHDAQVKLYKEELEQTyhaklENARLSSEMNTSTVNSAREELMEsrm 298
Cdd:pfam01576 80 L----ESRLEE---------EEERSQQLQNEKKKMQQHIQDLEEQLDEE-----EAARQKLQLEKVTTEAKIKKLEE--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 299 RIESLSSQLSNLQKESRACLERIQELEDLLAKERDNSRRMLSDK---EREMAEIRDQMQQQLNDYEQLLDVKLALDMEIS 375
Cdd:pfam01576 139 DILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKnkhEAMISDLEERLKKEEKGRQELEKAKRKLEGEST 218
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
20-351 |
2.91e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 20 TPLSPTRLSRLQEKEELR--ELNDRLAVYIDKVRSLETENSALQLQVTEREEVR------GRELT-----GLKALYETEL 86
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAkeEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcGRELTeehrkELLEEYTAEL 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 87 ADARRALDDTARERAKLQIELGKFKAE--HDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATAL--------GDK 156
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVlkKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLkekliklkGEI 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 157 KSLESDLE---DLKDQIAQLEASLAAAKKQLADetlLKVDLENRCQSLTEDLEfrknmyeEEINETRRKHETRLVEVDSG 233
Cdd:PRK03918 542 KSLKKELEkleELKKKLAELEKKLDELEEELAE---LLKELEELGFESVEELE-------ERLKELEPFYNEYLELKDAE 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 234 RQIEYEYKLAQALHEMREQHDAQVKLYKEELEqtyhaklenaRLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKE 313
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLE----------ELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAE 681
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 157074106 314 SRACLERIQELEDLLAK------ERDNSRRMLSDKEREMAEIRD 351
Cdd:PRK03918 682 LEELEKRREEIKKTLEKlkeeleEREKAKKELEKLEKALERVEE 725
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
66-364 |
3.04e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 66 EREEVRGRELTGLKALYETELADARRALDDTARERAKLQIEL----GKFKAEHDQLL--------LNYAKK--ESDLNGA 131
Cdd:pfam01576 85 EEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKvtteAKIKKLEEDILlledqnskLSKERKllEERISEF 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 132 QIKLREYE------AALNSKDAALATALGD---------------KKSLESDLEDLKDQIAQLEASLAAAKKQLA----- 185
Cdd:pfam01576 165 TSNLAEEEekakslSKLKNKHEAMISDLEErlkkeekgrqelekaKRKLEGESTDLQEQIAELQAQIAELRAQLAkkeee 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 186 ---------DETL------------------LKVDLENRCQS----------LTEDLEFRKNMYEEEINET------RRK 222
Cdd:pfam01576 245 lqaalarleEETAqknnalkkireleaqiseLQEDLESERAArnkaekqrrdLGEELEALKTELEDTLDTTaaqqelRSK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 223 HETRLVEVDsgRQIEYEYKLAQA-LHEMREQHDAQVKLYKEELEQTYHAKL-----------ENARLSSEMntSTVNSAR 290
Cdd:pfam01576 325 REQEVTELK--KALEEETRSHEAqLQEMRQKHTQALEELTEQLEQAKRNKAnlekakqalesENAELQAEL--RTLQQAK 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 291 EELMESRMRIEslsSQLSNLQKESRACLERIQELEDLLAK---ERDNSRRMLSDKERE---MAEIRDQMQQQLNDYEQLL 364
Cdd:pfam01576 401 QDSEHKRKKLE---GQLQELQARLSESERQRAELAEKLSKlqsELESVSSLLNEAEGKnikLSKDVSSLESQLQDTQELL 477
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
103-329 |
3.06e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 103 LQIELGKFKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLESDLEDLKDQIAQLEASLAAAKK 182
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 183 QLADETLLKvdlenrcqsLTEDLEFRKNMYEEEINETRRKHETRLvevdsgRQIEYEYKLAQALHEMREQHDAQVKLYKE 262
Cdd:COG4717 124 LLQLLPLYQ---------ELEALEAELAELPERLEELEERLEELR------ELEEELEELEAELAELQEELEELLEQLSL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157074106 263 ELEQTyhakLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRAC--LERIQELEDLLA 329
Cdd:COG4717 189 ATEEE----LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAalEERLKEARLLLL 253
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
158-386 |
3.11e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.49 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 158 SLESDLEDLKDQIAQ-----------LEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEEINETRRKheTR 226
Cdd:pfam05557 6 ESKARLSQLQNEKKQmelehkrarieLEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLK--KK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 227 LVEVDSGRQIEYEYKLAQAlhemreqHDAQVKLYKEELEqtYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQ 306
Cdd:pfam05557 84 YLEALNKKLNEKESQLADA-------REVISCLKNELSE--LRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 307 LSNLQKESRACLE---RIQELEDLLAKERDNSRRMLSDKER--EMAEIRDQMQQQLNDYEQL---LDVKLALDMEISAYR 378
Cdd:pfam05557 155 RQNLEKQQSSLAEaeqRIKELEFEIQSQEQDSEIVKNSKSElaRIPELEKELERLREHNKHLnenIENKLLLKEEVEDLK 234
|
....*...
gi 157074106 379 KLLEGEEE 386
Cdd:pfam05557 235 RKLEREEK 242
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
123-247 |
3.35e-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: 40.00 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 123 KKESDLNGAQIKLREYEAALNSKDAALATALGDKKSL-ESDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSL 201
Cdd:smart00787 165 KELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCdPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDL 244
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 157074106 202 TEDlefrKNMYEEEINETRRKHET-RLVEVDSGRQIEYEYKLAQALH 247
Cdd:smart00787 245 TNK----KSELNTEIAEAEKKLEQcRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
34-389 |
3.49e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 34 EELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALyETELADARRALDDTARERAKLQIELGKFKAE 113
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKK-EKELEKLNNKYNDLKKQKEELENELNLLEKE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 114 hdqlllnYAKKESDLNgaqiKLREYEAALNSKDAALATALGDKKSLESDLEDLKDQIAQLEASLAAAKKQLADETLLKVD 193
Cdd:TIGR04523 182 -------KLNIQKNID----KIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 194 LENRCQSLTEDLEFRKNMYEEEINETrrkhetrlvevdsgrqieyeyklaqalhemrEQHDAQVKLYKEELeQTYHAKLE 273
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQLSEKQKEL-------------------------------EQNNKKIKELEKQL-NQLKSEIS 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 274 NarLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELE-DLLAKERDNS--RRMLSDKEREMAEIR 350
Cdd:TIGR04523 299 D--LNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKkELTNSESENSekQRELEEKQNEIEKLK 376
|
330 340 350
....*....|....*....|....*....|....*....
gi 157074106 351 DQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEERLK 389
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK 415
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
122-186 |
5.88e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 5.88e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157074106 122 AKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLESDLEDLKDQIAQLEASLAAAKKQLAD 186
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
154-252 |
6.22e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 39.66 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 154 GDKKSLESDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLEN--RCQSLT-EDLEFRKNMYEEEINETRRKHETRLVEV 230
Cdd:pfam05911 702 VELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETqlKCMAESyEDLETRLTELEAELNELRQKFEALEVEL 781
|
90 100
....*....|....*....|..
gi 157074106 231 DSGRQIeYEYKLAqALHEMREQ 252
Cdd:pfam05911 782 EEEKNC-HEELEA-KCLELQEQ 801
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
120-186 |
8.98e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 38.55 E-value: 8.98e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157074106 120 NYAKKESDLNGAQIKLR-----EYEAALNSKDAALATALGDKKSLESDLEDLKDQIAQLEASLAAAKKQLAD 186
Cdd:TIGR04320 236 SYIADGNKFDKTPIPNPpnslaALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELAN 307
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
160-385 |
9.51e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 38.79 E-value: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 160 ESDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYE 239
Cdd:COG5185 235 LKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 240 YKLAQALHEmrEQHDAQVKLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRmRIESLSSQLSNLQKESRACLE 319
Cdd:COG5185 315 EEQLAAAEA--EQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEV-ELSKSSEELDSFKDTIESTKE 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 320 RIQELEDLLAKERDNSRRMLSDK----EREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEE 385
Cdd:COG5185 392 SLDEIPQNQRGYAQEILATLEDTlkaaDRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEES 461
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
134-364 |
9.87e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 38.95 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 134 KLREYEAALNSKDAALATALGDKKSLESDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENR--CQSLTEDlEFRKNM 211
Cdd:pfam15921 343 KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtGNSITID-HLRREL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 212 YEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHD---AQVKLYKEELEQTYHaKLENARLSSEMNTSTVNS 288
Cdd:pfam15921 422 DDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSsltAQLESTKEMLRKVVE-ELTAKKMTLESSERTVSD 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157074106 289 AREELMESRMRIESLSSQLSNLQkeSRACLeRIQELEDlLAKERDNSRRMLSDKER---EMAE---IRDQMQQQLNDYEQ 362
Cdd:pfam15921 501 LTASLQEKERAIEATNAEITKLR--SRVDL-KLQELQH-LKNEGDHLRNVQTECEAlklQMAEkdkVIEILRQQIENMTQ 576
|
..
gi 157074106 363 LL 364
Cdd:pfam15921 577 LV 578
|
|
| |
