|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
31-387 |
4.35e-101 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 308.77 E-value: 4.35e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 31 QEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKC 110
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 111 KAEHDQLLLNYAKKesdlngaqiklreyeaalnskdaalataLGDKKSLEGDLEDLKdqiaqleaslaaakKQLADETLL 190
Cdd:pfam00038 81 RLAAEDFRQKYEDE----------------------------LNLRTSAENDLVGLR--------------KDLDEATLA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 191 KVDLENRCQSLTEDLEFRKSMYEEEINETRRKH--ETRLVEVDSGRQIEyeykLAQALHEMREQHDAQVRLYKEELEQTY 268
Cdd:pfam00038 119 RVDLEAKIESLKEELAFLKKNHEEEVRELQAQVsdTQVNVEMDAARKLD----LTSALAEIRAQYEEIAAKNREEAEEWY 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 269 HAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLAKEKDNSRRMLTDKEREMAE 348
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQE 274
|
330 340 350
....*....|....*....|....*....|....*....
gi 5031877 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 5031877 439 TGNVCIEEIDVDG-----KFIRLKNTSEQDQPMGGWEMIRKIGDTsvsYKYTSRYVLKAGQTVTIWAANAGVTAS----P 509
Cdd:pfam00932 4 TGDVVISEVVYDGsggndEFIELYNTGSKAVDLSGWKLQDASGGT---YTFPNGTTLAPGQTVVVWTGSGTNSATagywG 80
|
90 100 110
....*....|....*....|....*....|....
gi 5031877 510 PTDLIWKNQNSWgtgedvkVILKNSQGEEVAQRS 543
Cdd:pfam00932 81 PSNAVWNNGGDA-------VALYDANGELVDSVG 107
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
12-349 |
3.00e-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: 82.80 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 12 GSRAGGPttplSPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEvrgreltglkalyetELADARR 91
Cdd:TIGR02168 659 GVITGGS----AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEE---------------ELEQLRK 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 92 ALDDTARERAKLQIELGKCKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIA 171
Cdd:TIGR02168 720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 172 QLEASLAAAKKQLADETLLKVDLENRCqsltEDLEFRKSMYEEEINETRRKHETRLVEV-----------DSGRQIEYEY 240
Cdd:TIGR02168 800 ALREALDELRAELTLLNEEAANLRERL----ESLERRIAATERRLEDLEEQIEELSEDIeslaaeieeleELIEELESEL 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 241 KLAQALHEMREQHDAQVRLYKEELEQTYH----AKLENARLSSEMNTStVNSAREELMESRMRIESLSSQLSNLQKESra 316
Cdd:TIGR02168 876 EALLNERASLEEALALLRSELEELSEELRelesKRSELRRELEELREK-LAQLELRLEGLEVRIDNLQERLSEEYSLT-- 952
|
330 340 350
....*....|....*....|....*....|...
gi 5031877 317 cLERIQELEDLLAKEKDNSRRMLTDKEREMAEI 349
Cdd:TIGR02168 953 -LEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
33-363 |
1.27e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 33 KEELRELndRLAVYIDKVRSLETENSALQLQVTEREEVRgRELTGLKALYETELADARRALDDTARERAKLQIELGKCKA 112
Cdd:TIGR02168 219 KAELREL--ELALLVLRLEELREELEELQEELKEAEEEL-EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 113 EhdqlllnYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKV 192
Cdd:TIGR02168 296 E-------ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 193 DLENRCQSLTEDLEFRKSmyeeeinetrrkhetrlvevdsgrqieyeyKLAQALHEMrEQHDAQVRLYKEELEQtyhAKL 272
Cdd:TIGR02168 369 ELESRLEELEEQLETLRS------------------------------KVAQLELQI-ASLNNEIERLEARLER---LED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 273 ENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKEsracLERIQELEDLLAKEKDNSRRMLTDKEREMAEIR-- 350
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE----LERLEEALEELREELEEAEQALDAAERELAQLQar 490
|
330
....*....|....
gi 5031877 351 -DQMQQQLNDYEQL 363
Cdd:TIGR02168 491 lDSLERLQENLEGF 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
70-389 |
4.39e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.23 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 70 VRGRELTGLKALY-ETELADARRALDDTARERAKLQIELGKCKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAA 148
Cdd:TIGR02168 662 TGGSAKTNSSILErRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 149 LATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKSMY---EEEINETRRK-HE 224
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelRAELTLLNEEaAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 225 TRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQtyhAKLENARLSSEmntstVNSAREELMESRMRIESLS 304
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE---LEELIEELESE-----LEALLNERASLEEALALLR 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 305 SQLSNLQKESRACLERIQELEDLLakekDNSRRMLTDKEREMAEIR---DQMQQQLN-DYEQLLDVKLALDMEISAYRKL 380
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRREL----EELREKLAQLELRLEGLEvriDNLQERLSeEYSLTLEEAEALENKIEDDEEE 969
|
....*....
gi 5031877 381 LEGEEERLK 389
Cdd:TIGR02168 970 ARRRLKRLE 978
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
31-280 |
5.39e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 31 QEKEELRELNDRLAVYIDKVRSLETENSALQLQVtEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKC 110
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLEL-EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 111 KAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLL 190
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 191 KVDLENRCQSLTEDLEFRKSMYEEEINETRRKHETRLVEVDSGRQI-EYEYKLAQALHEMREQHDAQVRLYKEELEQTYH 269
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAaEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250
....*....|.
gi 5031877 270 AKLENARLSSE 280
Cdd:COG1196 482 LLEELAEAAAR 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
30-332 |
1.26e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 30 LQEKEELRELNdrlaVYIDKVRSLETENSALQLQVTEREEVRgRELTGLKALYETELADARRALDDTARERAKLQIELGK 109
Cdd:COG1196 218 LKEELKELEAE----LLLLKLRELEAELEELEAELEELEAEL-EELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 110 CKAEHDQLllnyakkESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETL 189
Cdd:COG1196 293 LLAELARL-------EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 190 LKVDLEnrcQSLTEDLEFRKSMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYH 269
Cdd:COG1196 366 ALLEAE---AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031877 270 AKLEnarlssemntstvnsAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLAKEK 332
Cdd:COG1196 443 ALEE---------------AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
95-388 |
1.31e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 95 DTARERAKLQIELGKCKAEHdqLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATalgdkksLEGDLEDLKDQIAQLE 174
Cdd:COG1196 210 EKAERYRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAE-------LEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 175 ASLAAAKKQLADetllkvdLENRCQSLTEDLEFRKsmyEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHD 254
Cdd:COG1196 281 LELEEAQAEEYE-------LLAELARLEQDIARLE---ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 255 AQVRLYKEELEQTyHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLAKEKDN 334
Cdd:COG1196 351 EELEEAEAELAEA-EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 5031877 335 SRRMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEERL 388
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
136-390 |
1.62e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 136 REYEAALNSKDAALAtaLGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLefrksmyeEE 215
Cdd:COG1196 216 RELKEELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--------EE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 216 INETRRKHETRLVEVDsgRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTyHAKLENARLSSEMNTSTVNSAREELME 295
Cdd:COG1196 286 AQAEEYELLAELARLE--QDIARLEERRRELEERLEELEEELAELEEELEEL-EEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 296 SRMRIESLSSQLSNLQKESRACLERIQELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEIS 375
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
250
....*....|....*
gi 5031877 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 |
1.94e-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: 57.39 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 80 ALYETELADARRALDDTARERAKLQIELGKCKAEHDQLLLNYAKKE--SDLngaQIKLREYEAALnskdaalatalgdkk 157
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryQAL---LKEKREYEGYE--------------- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 158 sLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFR----KSMYEEEINETRRKHETRLVEVDSG 233
Cdd:TIGR02169 228 -LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkiKDLGEEEQLRVKEKIGELEAEIASL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 234 RQIEYEYKL-AQALHEMREQHDAQVRLYKEELEQtYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQK 312
Cdd:TIGR02169 307 ERSIAEKEReLEDAEERLAKLEAEIDKLLAEIEE-LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 313 ESRACLERIQELEDLLAKEKDNSRRMLTDKER---EMAEIRDQMQQQLNDYEQLLDVKLALDMEISAyrklLEGEEERLK 389
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEELQRlseELADLNAAIAGIEAKINELEEEKEDKALEIKK----QEWKLEQLA 461
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
25-325 |
5.80e-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: 55.84 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 25 TRLSRLQ----EKEELRELNDRLAVY-----IDKVRSLETENSALQLQVTEREEvrgrELTGLKALYE---TELADARRA 92
Cdd:TIGR02169 198 QQLERLRrereKAERYQALLKEKREYegyelLKEKEALERQKEAIERQLASLEE----ELEKLTEEISeleKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 93 LDDTAR--------ERAKLQIELGKCKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAalatalgDKKSLEGDLE 164
Cdd:TIGR02169 274 LEELNKkikdlgeeEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA-------EIEELEREIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 165 DLKDQIAQLEASLAAAKKQLADetllkvdLENRCQSLTEDLE--FRKSM-YEEEINETRRKHEtrlvevDSGRQIEYEYK 241
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEELED-------LRAELEEVDKEFAetRDELKdYREKLEKLKREIN------ELKRELDRLQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 242 LAQALHEMREQHDAQVRLYKEELEQtYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERI 321
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINE-LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
....
gi 5031877 322 QELE 325
Cdd:TIGR02169 493 AEAE 496
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
70-376 |
7.31e-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: 55.46 E-value: 7.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 70 VRGRELTGLKALYETELADARRALDDTARERAKLQIELGKCKAEHDQLLlnyakkeSDLNGAQIKLREYEAALNSKDAAL 149
Cdd:TIGR02169 660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELS-------QELSDASRKIGEIEKEIEQLEQEE 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 150 ATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDL---EFRKSMYE-EEINETRRKHET 225
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsRIPEIQAElSKLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 226 RLVEVDsgrQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSS 305
Cdd:TIGR02169 813 RLREIE---QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 306 QLSNLQKESRACLERIQELEDLLAKEKDNSRRMLTDKE---REMAEIRDQMQQ------QLNDYEQLLDVKLALDMEISA 376
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEaleEELSEIEDPKGEdeeipeEELSLEDVQAELQRVEEEIRA 969
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
34-354 |
1.08e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 34 EELRELNDRLAVYIDKVRSLETENSALQLQVTEREEvrgrELTGLkalyETELADARRALDDTARERAKLQIELGKCKAE 113
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRRE----EIEEL----EEEIEELRERFGDAPVDLGNAEDFLEELREE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 114 HDQLLLNYAKKESDLNGAQIKLREYEAALNS----------KDAALATALGDKK----SLEGDLEDLKDQIAQLEASLAA 179
Cdd:PRK02224 421 RDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEDRerveELEAELEDLEEEVEEVEERLER 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 180 AKKQLADETLLKVDLENRcqsltEDLEFRKSMYEEEINETRRKhetrlvevdsgrqieyeyklAQALHEMREQHDAQVRl 259
Cdd:PRK02224 501 AEDLVEAEDRIERLEERR-----EDLEELIAERRETIEEKRER--------------------AEELRERAAELEAEAE- 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 260 YKEELEQTYHAKLENARLSsemnTSTVNSAREELMESRMRIESLSSQLSNLQkESRACLERIQELEDLLAKEKDNSRRML 339
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREE----VAELNSKLAELKERIESLERIRTLLAAIA-DAEDEIERLREKREALAELNDERRERL 629
|
330
....*....|....*
gi 5031877 340 TDKEREMAEIRDQMQ 354
Cdd:PRK02224 630 AEKRERKRELEAEFD 644
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
33-327 |
3.85e-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: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 33 KEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKAL------YETELADARRALDDTARERAKLQIE 106
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELeedlssLEQEIENVKSELKELEARIEELEED 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 107 LGKCKAEHDQLLLNYAKKESDLNGAQIK------------LREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLE 174
Cdd:TIGR02169 774 LHKLEEALNDLEARLSHSRIPEIQAELSkleeevsriearLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 175 ASLAAAKKQLAD------ETLLKV-DLENRCQSLTEDLEFRKSMYEE------EINETRRKHETRLVEVDSGRQIEyEYK 241
Cdd:TIGR02169 854 KEIENLNGKKEEleeeleELEAALrDLESRLGDLKKERDELEAQLRElerkieELEAQIEKKRKRLSELKAKLEAL-EEE 932
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 242 LAQALHEMRE-QHDAQVRLYKEELEQTYHAKLENARLSSEMNtstvNSAREELMESRMRIESLSSQLSNLQKESRACLER 320
Cdd:TIGR02169 933 LSEIEDPKGEdEEIPEEELSLEDVQAELQRVEEEIRALEPVN----MLAIQEYEEVLKRLDELKEKRAKLEEERKAILER 1008
|
....*..
gi 5031877 321 IQELEDL 327
Cdd:TIGR02169 1009 IEEYEKK 1015
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
85-335 |
5.61e-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: 52.07 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 85 ELADARRALDDTARERAKLQIELGKCKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLE 164
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 165 DLKDQIAQLEASLAAAKKQLADETLLKVDLENRcqsltedlEFRKSMYEEEINETRRKHETRLVEVDSgrqieyeyKLAQ 244
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLD--------AVRRLQYLKYLAPARREQAEELRADLA--------ELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 245 ALHEMREQHDAQVRLYKEELEQtyHAKLENARlssemntstvNSAREELMESRMRIESLSSQLSNLQKESRACLERIQEL 324
Cdd:COG4942 165 LRAELEAERAELEALLAELEEE--RAALEALK----------AERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
250
....*....|.
gi 5031877 325 EDLLAKEKDNS 335
Cdd:COG4942 233 EAEAAAAAERT 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
147-379 |
6.40e-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: 51.69 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 147 AALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTE---DLEFRKSMYEEEINETRRKH 223
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 224 ETrlVEVDSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYHakleNARLSSEMNTSTVNSArEELMESRMRIESL 303
Cdd:COG4942 93 AE--LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVR----RLQYLKYLAPARREQA-EELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031877 304 SSQLSNLQKESRACLERIQELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRK 379
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
22-382 |
2.73e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 22 LSPTRLSRLQEKEELRELNDRLAV---YIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTAR 98
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEEleeRLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 99 ERAKLQIELGKCKAEHDQLLLNYAKKESDLNGAQIKLREYEAALnskDAALATALGDKKSLEGDLEDLKDQIAQLEASLA 178
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL---LLLIAAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 179 AAKKQLADETLLKVDLENRCQSLTEDLEFRKSMYEEEINETRRKHEtRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVR 258
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALG-LPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 259 LYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERI------QELEDLLAKEK 332
Cdd:COG4717 363 LQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeeeleEELEELEEELE 442
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 5031877 333 DNSRRmLTDKEREMAEIRDQMQQQLND---------YEQLLDVKLALDMEISAYRKLLE 382
Cdd:COG4717 443 ELEEE-LEELREELAELEAELEQLEEDgelaellqeLEELKAELRELAEEWAALKLALE 500
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
86-395 |
3.68e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 86 LADARRALDDTARERAKLQIELGKCKAEHDQL--LLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKksleGDL 163
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALqeRREALQRLAEYSWDEIDVASAEREIAELEAELERLDASS----DDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 164 EDLKDQIAQLEASLAAAKKQLAdetllkvDLENRCQSLTEDLefrksmyeEEINETRRKHETRLVEVDSGRQIEYEYKLA 243
Cdd:COG4913 688 AALEEQLEELEAELEELEEELD-------ELKGEIGRLEKEL--------EQAEEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 244 QALHEmreqhdaqvrLYKEELEQTYHAKLENARlssEMNTSTVNSAREELMESRMR--------IESLSSQLSNLQkESR 315
Cdd:COG4913 753 ERFAA----------ALGDAVERELRENLEERI---DALRARLNRAEEELERAMRAfnrewpaeTADLDADLESLP-EYL 818
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 316 ACLERIQElEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLND-YEQLLDVKLALdmeisayRKLLEGEEERLKLSPSP 394
Cdd:COG4913 819 ALLDRLEE-DGLPEYEERFKELLNENSIEFVADLLSKLRRAIREiKERIDPLNDSL-------KRIPFGPGRYLRLEARP 890
|
.
gi 5031877 395 S 395
Cdd:COG4913 891 R 891
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
28-387 |
7.05e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 28 SRLQEKEELRELNDRLAVYIDKVRSLETENSalqlqvTEREEVRGReltglkalyeteLADARRALDDTARERAKLQIEL 107
Cdd:PRK02224 241 EVLEEHEERREELETLEAEIEDLRETIAETE------REREELAEE------------VRDLRERLEELEEERDDLLAEA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 108 GKCKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLAD- 186
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDr 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 187 -----------ETLLK------VDLENrCQSLTEDLEFRKSMYEEEINETRRKHETRLVEVDSGRQIEYEYK-------- 241
Cdd:PRK02224 383 reeieeleeeiEELRErfgdapVDLGN-AEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpv 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 242 ----LAQALHEMREQHD------AQVRLYKEELEQTYH-----AKLENARLSSEMNTSTVNS----AREELMESRMRIES 302
Cdd:PRK02224 462 egspHVETIEEDRERVEeleaelEDLEEEVEEVEERLEraedlVEAEDRIERLEERREDLEEliaeRRETIEEKRERAEE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 303 LSSQLSNLQKESRACLERIQELEDllakEKDNSRRMLTDKEREMAEIRDQMqQQLNDYEQLLDVKLALDMEISAYRKLLE 382
Cdd:PRK02224 542 LRERAAELEAEAEEKREAAAEAEE----EAEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKRE 616
|
....*
gi 5031877 383 GEEER 387
Cdd:PRK02224 617 ALAEL 621
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
28-225 |
1.01e-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: 48.22 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 28 SRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEvRGRELTGLKALYETELADARRALDDTARERAKLQIEL 107
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-RIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 108 GKCKAEHDQLLLNYAKKE-----------SDLNGAqIKLREYEAALNSKDAALATALGDKKSlegDLEDLKDQIAQLEAS 176
Cdd:COG4942 100 EAQKEELAELLRALYRLGrqpplalllspEDFLDA-VRRLQYLKYLAPARREQAEELRADLA---ELAALRAELEAERAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 5031877 177 LAAAKKQLADETLLKVDLENRCQSLTEDLEFRKSMYEEEINETRRKHET 225
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
34-221 |
1.50e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 34 EELRELNDRLAVYIDKVRSLETENSALQLQVTEREevrgreltglKALYETELADARRALDDTARERAKLQIELGKCKAE 113
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRR----------LELLEAELEELRAELARLEAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 114 HDQLLLNYAKK--------ESDLNGAQIKLREYEAALNSKDAALA----TALGDKKSLEGDLEDLKDQIAQLEASLAAAK 181
Cdd:COG4913 325 LDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLAalglPLPASAEEFAALRAEAAALLEALEEELEALE 404
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 5031877 182 KQLADETLLKVDLENRCQSLTEDLEF---RKSMYEEEINETRR 221
Cdd:COG4913 405 EALAEAEAALRDLRRELRELEAEIASlerRKSNIPARLLALRD 447
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
120-205 |
2.04e-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: 47.03 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 120 NYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQL-EASLAAAKKQLADETLLKVDLENRC 198
Cdd:TIGR04320 262 KLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTaQNNLATAQAALANAEARLAKAKEAL 341
|
....*..
gi 5031877 199 QSLTEDL 205
Cdd:TIGR04320 342 ANLNADL 348
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
28-389 |
2.88e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 28 SRLQE-KEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYEtelaDARRALDDTARERAKLQIE 106
Cdd:PRK03918 338 ERLEElKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE----ELEKAKEEIEEEISKITAR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 107 LGKCKAEHDQLL-----LNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAK 181
Cdd:PRK03918 414 IGELKKEIKELKkaieeLKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 182 KQLADETLLK--VDLENRCQSLT-EDLEFRKSMYEEEINETRR-KHETRLVEVDSGRQIEYEYKLAQALHEMREqhdaqv 257
Cdd:PRK03918 494 ELIKLKELAEqlKELEEKLKKYNlEELEKKAEEYEKLKEKLIKlKGEIKSLKKELEKLEELKKKLAELEKKLDE------ 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 258 rlyKEELEQTYHAKLENARLSSEmntstvnsarEELMESRMRIESLSSQLSNLqKESRACLERIQELEDLLAKEKDNSRR 337
Cdd:PRK03918 568 ---LEEELAELLKELEELGFESV----------EELEERLKELEPFYNEYLEL-KDAEKELEREEKELKKLEEELDKAFE 633
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 5031877 338 MLTDKEREMAEIRDQMQQQL-----NDYEQLLDVKLALDMEISAYRKLLEGEEERLK 389
Cdd:PRK03918 634 ELAETEKRLEELRKELEELEkkyseEEYEELREEYLELSRELAGLRAELEELEKRRE 690
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
83-229 |
3.59e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 83 ETELADARRALDDTARERAKLQIELGKCKAEHDQLLLNYAKKESDLNGAQIKLREYEAAL----NSKDAalatalgdkKS 158
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrNNKEY---------EA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031877 159 LEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKSMYEEEINETRRKHETRLVE 229
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
84-367 |
4.22e-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: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 84 TELADARRALDDtARERAKLqieLGKCKAEHDQlllnYAKKESDLNgaqiKLREYEAALNSKDAALATALgdkksLEGDL 163
Cdd:COG4913 235 DDLERAHEALED-AREQIEL---LEPIRELAER----YAAARERLA----ELEYLRAALRLWFAQRRLEL-----LEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 164 EDLKDQIAQLEASLAAAKKQLADEtllkvdlenrcqsltedlefrksmyEEEINETRRKHETrlvevDSGRQIEyeyKLA 243
Cdd:COG4913 298 EELRAELARLEAELERLEARLDAL-------------------------REELDELEAQIRG-----NGGDRLE---QLE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 244 QALHEMREQHDAQvrlykEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQE 323
Cdd:COG4913 345 REIERLERELEER-----ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 5031877 324 LEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYEQ-------LLDVK 367
Cdd:COG4913 420 ELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAelpfvgeLIEVR 470
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
57-286 |
4.36e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 57 NSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELG--KCKAEHDQLLLNYAKKESDLNGAQIK 134
Cdd:COG3206 155 NALAEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 135 LREYEAALNSKDAALATALGDKKSLEGD--LEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKSMY 212
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 213 EEEINETRRKHETRLVEVDSgRQIEYEYKLAQA------LHEMREQHDAQVRLYkeeleQTYHAKLENARLSSEMNTSTV 286
Cdd:COG3206 315 LASLEAELEALQAREASLQA-QLAQLEARLAELpeleaeLRRLEREVEVARELY-----ESLLQRLEEARLAEALTVGNV 388
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
171-383 |
6.97e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 171 AQLEASLAAAKKQ---LADETLLKVDLENrcqslTEDLEFRKSMYEEEINETRRKhetrlvevdsgrqieyeykLAQALH 247
Cdd:PRK11281 39 ADVQAQLDALNKQkllEAEDKLVQQDLEQ-----TLALLDKIDRQKEETEQLKQQ-------------------LAQAPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 248 EMREQHDAQVRLYKEELEQTY--HAKLENARLSSEMN--TSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQE 323
Cdd:PRK11281 95 KLRQAQAELEALKDDNDEETRetLSTLSLRQLESRLAqtLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQ 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 324 LEDLLAKEKDNSRrmltdkeremaEIRDQMQQQLNDYEQLLDVKLALDmeisayRKLLEG 383
Cdd:PRK11281 175 IRNLLKGGKVGGK-----------ALRPSQRVLLQAEQALLNAQNDLQ------RKSLEG 217
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
243-389 |
7.03e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 7.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 243 AQALHEMREQHDAQVRLYK----EELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACL 318
Cdd:COG1196 215 YRELKEELKELEAELLLLKlrelEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031877 319 ERIQELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEERLK 389
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
46-386 |
2.37e-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: 44.33 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 46 YIDKVRSLETEnsalqlqvTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKCKAEHDQLLlnyaKKE 125
Cdd:pfam05483 469 YLKEVEDLKTE--------LEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERML----KQI 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 126 SDLNGAQIKLREYEAALnskdaalatalgdKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDL 205
Cdd:pfam05483 537 ENLEEKEMNLRDELESV-------------REEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 206 EfRKSMYEEEINETRRKHETRlVEVDSGRQIEYEYKLAQALHEMreqhdAQVRLYKEELEQTYHAKLENARLSSEMNTST 285
Cdd:pfam05483 604 E-NKNKNIEELHQENKALKKK-GSAENKQLNAYEIKVNKLELEL-----ASAKQKFEEIIDNYQKEIEDKKISEEKLLEE 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 286 VNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYE-QLL 364
Cdd:pfam05483 677 VEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKaELL 756
|
330 340
....*....|....*....|..
gi 5031877 365 DVKLALDMEISAYRKLLEGEEE 386
Cdd:pfam05483 757 SLKKQLEIEKEEKEKLKMEAKE 778
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
30-389 |
3.50e-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: 43.67 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 30 LQEKEELRELNDRLA-VYIDKVRSLETENSALQLQVTE-REEVRG--RELTGLKALYETELADARRALDD-TARERAKLQ 104
Cdd:pfam12128 386 EQNNRDIAGIKDKLAkIREARDRQLAVAEDDLQALESElREQLEAgkLEFNEEEYRLKSRLGELKLRLNQaTATPELLLQ 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 105 IE------------LGKCKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDL-EDLKDQIA 171
Cdd:pfam12128 466 LEnfderierareeQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLlHFLRKEAP 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 172 QLEASLAaakKQLADETLLKVDLenrcqslteDLEFRKSMYEEEINETRRKHETRLVEVDSGRQIEYEYK--LAQALHEM 249
Cdd:pfam12128 546 DWEQSIG---KVISPELLHRTDL---------DPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRerLDKAEEAL 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 250 REQHDAQVRLyKEELEQTyHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSN-LQKESRACLERIQELEDLL 328
Cdd:pfam12128 614 QSAREKQAAA-EEQLVQA-NGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKaLAERKDSANERLNSLEAQL 691
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031877 329 AKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLA-LDMEISAYRKLLEGEEERLK 389
Cdd:pfam12128 692 KQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLAlLKAAIAARRSGAKAELKALE 753
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
66-364 |
3.85e-04 |
|
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: 43.63 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 66 EREEVRGRELTGLKALYETELADARRALDDTARERAKLQIEL----GKCKAEHDQLL--------LNYAKK--ESDLNGA 131
Cdd:pfam01576 85 EEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKvtteAKIKKLEEDILlledqnskLSKERKllEERISEF 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 132 QIKLREYE------AALNSKDAALATALGD---------------KKSLEGDLEDLKDQIAQLEASLAAAKKQLA----- 185
Cdd:pfam01576 165 TSNLAEEEekakslSKLKNKHEAMISDLEErlkkeekgrqelekaKRKLEGESTDLQEQIAELQAQIAELRAQLAkkeee 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 186 ---------DETL------------------LKVDLENRCQS----------LTEDLEFRKSMYEEEINET------RRK 222
Cdd:pfam01576 245 lqaalarleEETAqknnalkkireleaqiseLQEDLESERAArnkaekqrrdLGEELEALKTELEDTLDTTaaqqelRSK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 223 HETRLVEVDsgRQIEYEYKLAQA-LHEMREQHDAQVRLYKEELEQTYHAKL-----------ENARLSSEMntSTVNSAR 290
Cdd:pfam01576 325 REQEVTELK--KALEEETRSHEAqLQEMRQKHTQALEELTEQLEQAKRNKAnlekakqalesENAELQAEL--RTLQQAK 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 291 EELMESRMRIEslsSQLSNLQKESRACLERIQELEDLLAK---EKDNSRRMLTDKERE---MAEIRDQMQQQLNDYEQLL 364
Cdd:pfam01576 401 QDSEHKRKKLE---GQLQELQARLSESERQRAELAEKLSKlqsELESVSSLLNEAEGKnikLSKDVSSLESQLQDTQELL 477
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
61-250 |
6.29e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 61 QLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELgkckaEHDQLLLNYAKKESDLNGAQIKLREYEA 140
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 141 ALnskdAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVdlenrcqsltEDLEFRKSMYEEEINETR 220
Cdd:COG4717 154 RL----EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL----------EELQQRLAELEEELEEAQ 219
|
170 180 190
....*....|....*....|....*....|
gi 5031877 221 RKHETRLVEVDSGRQIEYEYKLAQALHEMR 250
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEAR 249
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
29-350 |
7.18e-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: 7.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 29 RLQEKEELRELNDRLavyidkvRSLETENSALQLQVTERE---EVRGRELTGLKALyeteLADARRALDDTARERAKLQI 105
Cdd:pfam15921 529 KLQELQHLKNEGDHL-------RNVQTECEALKLQMAEKDkviEILRQQIENMTQL----VGQHGRTAGAMQVEKAQLEK 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 106 ELGKCKAEHDQLLLNYAKKESdlngaqiKLREYEAA---LNSKDAALATALGDKKSLEGDLEDLKDQIA-QLEASLAAAK 181
Cdd:pfam15921 598 EINDRRLELQEFKILKDKKDA-------KIRELEARvsdLELEKVKLVNAGSERLRAVKDIKQERDQLLnEVKTSRNELN 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 182 KQLADETLLKVDLENRCQSL---TEDLEFRKSMYEEEINETRRKHETrlVEVDSGRQIEYEYKLAQALHEMREQHDA--- 255
Cdd:pfam15921 671 SLSEDYEVLKRNFRNKSEEMettTNKLKMQLKSAQSELEQTRNTLKS--MEGSDGHAMKVAMGMQKQITAKRGQIDAlqs 748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 256 QVRLYKEEL----EQTYHAKLENARLSSEMNT--STVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLA 329
Cdd:pfam15921 749 KIQFLEEAMtnanKEKHFLKEEKNKLSQELSTvaTEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQ 828
|
330 340
....*....|....*....|.
gi 5031877 330 KEKDNSRRMLTDKEREMAEIR 350
Cdd:pfam15921 829 RQEQESVRLKLQHTLDVKELQ 849
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
163-390 |
7.56e-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: 7.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 163 LEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKSMYEEEINETRRKHETRLVEVDSgrqieyeyKL 242
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADA--------AV 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 243 AQALHEMrEQHDAQVRLYKEELEQTYHAKLENArlssemntstvNSAREELMESRMRIESLSSQLSNLQKE-SRACLERI 321
Cdd:pfam12128 318 AKDRSEL-EALEDQHGAFLDADIETAAADQEQL-----------PSWQSELENLEERLKALTGKHQDVTAKyNRRRSKIK 385
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5031877 322 QELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLaLDMEISAYRKLLEGEEERLKL 390
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGK-LEFNEEEYRLKSRLGELKLRL 453
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
29-359 |
7.62e-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: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 29 RLQEKEELRElndRLAVYIDK-VRSLETENSALQLQVTEREEVRGRELTGLKALYET------ELaDARRALDDTARERA 101
Cdd:pfam15921 93 RLNESNELHE---KQKFYLRQsVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQlqntvhEL-EAAKCLKEDMLEDS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 102 KLQIE-LGKCKAEHDQLLLNYAKKESDLNGAQ-IKLREYEAALNSKDAALATALGDK-KSLEGDLEDLKDQIAQLEASLA 178
Cdd:pfam15921 169 NTQIEqLRKMMLSHEGVLQEIRSILVDFEEASgKKIYEHDSMSTMHFRSLGSAISKIlRELDTEISYLKGRIFPVEDQLE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 179 AAKKQLADET-LLKVDLENRCQSLTEDLEFRKSMYEEEINETRRKHETrlveVDSGRQIEYEYKLAQALHEMREQHD--- 254
Cdd:pfam15921 249 ALKSESQNKIeLLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANS----IQSQLEIIQEQARNQNSMYMRQLSDles 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 255 --AQVRLYKEELEQTYHAKLEnarlssEMNTSTVnSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLAKEK 332
Cdd:pfam15921 325 tvSQLRSELREAKRMYEDKIE------ELEKQLV-LANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEK 397
|
330 340
....*....|....*....|....*..
gi 5031877 333 DNSRRmLTDKEREMAEIRDQMQQQLND 359
Cdd:pfam15921 398 EQNKR-LWDRDTGNSITIDHLRRELDD 423
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
83-185 |
1.29e-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: 41.25 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 83 ETELADARRALDDTARERAKLQIELGKCKAEHDQLLLNYAKKESDLNGAQiklreyEAALNSKDAALATALGDKKSLEGD 162
Cdd:TIGR04320 260 QAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQ------AQALQTAQNNLATAQAALANAEAR 333
|
90 100
....*....|....*....|...
gi 5031877 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 |
1.50e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 242 LAQALHEMREQHDAqvrlykEELEQTYHAKLENARLSSEMntstvnsaREELMESRMRIESLSSQLSNLQKESRACLERI 321
Cdd:COG2433 378 IEEALEELIEKELP------EEEPEAEREKEHEERELTEE--------EEEIRRLEEQVERLEAEVEELEAELEEKDERI 443
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031877 322 QELEDLLAKEKDNSRRmltdKEREMAEIRdqmqqqlndyeqlldvklALDMEISAYRKLLEGEEERLK 389
Cdd:COG2433 444 ERLERELSEARSEERR----EIRKDREIS------------------RLDREIERLERELEEERERIE 489
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
28-367 |
1.50e-03 |
|
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: 41.42 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 28 SRLQEKeeLRELNDRLAVYIDKVRSLETENSALQlQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIEL 107
Cdd:pfam07888 34 NRLEEC--LQERAELLQAQEAANRQREKEKERYK-RDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 108 GKCKAEHDQLLLNYAKKESdlngaqiKLREYEAALnskdAALATALGDKkslEGDLEDLKDQIAQLEASLaaaKKQLADE 187
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEA-------RIRELEEDI----KTLTQRVLER---ETELERMKERAKKAGAQR---KEEEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 188 TLLKVDL---ENRCQSLTEDLEFRKSMYEEEINETRRKHE-----TRLVEVDSGRQIEYEYKLAQ--ALHEMREQHDAQV 257
Cdd:pfam07888 174 KQLQAKLqqtEEELRSLSKEFQELRNSLAQRDTQVLQLQDtittlTQKLTTAHRKEAENEALLEElrSLQERLNASERKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 258 RLYKEELEQTY------HAKLENARLSSEMNTSTVNSAREELMESRM------------------RIESLSSQLsnLQKE 313
Cdd:pfam07888 254 EGLGEELSSMAaqrdrtQAELHQARLQAAQLTLQLADASLALREGRArwaqeretlqqsaeadkdRIEKLSAEL--QRLE 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 5031877 314 SRACLERIQ--ELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYEQLLDVK 367
Cdd:pfam07888 332 ERLQEERMEreKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK 387
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
234-398 |
1.53e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 234 RQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYH--AKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQ 311
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLReiNEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 312 KESRACLERIQELEDLLaKEKDNSRRMLTDKEREMAEIRDQMQQQL---NDYEQLLDVKLALDMEISAYRKLLEGEEERL 388
Cdd:PRK03918 252 GSKRKLEEKIRELEERI-EELKKEIEELEEKVKELKELKEKAEEYIklsEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170
....*....|
gi 5031877 389 KLSPSPSSRV 398
Cdd:PRK03918 331 KELEEKEERL 340
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
66-362 |
2.24e-03 |
|
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: 41.09 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 66 EREEVRGRELTGLKALYET--ELADARRALDDTARERAKLQIELGKCKAEHD------QLLLN---YAKK----ESDLNG 130
Cdd:COG3096 279 ERRELSERALELRRELFGArrQLAEEQYRLVEMARELEELSARESDLEQDYQaasdhlNLVQTalrQQEKieryQEDLEE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 131 AQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIA-----------------QLEASLAAAKKQLADETLLKVD 193
Cdd:COG3096 359 LTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqqaldvqqtraiqyqQAVQALEKARALCGLPDLTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 194 LENRCQSLTEDlefrksmyEEEINETRRKHETRL-VEVDSGRQIEYEYKLAQAL--HEMREQ-HDAQVRLYKEELEQTYH 269
Cdd:COG3096 439 AEDYLAAFRAK--------EQQATEEVLELEQKLsVADAARRQFEKAYELVCKIagEVERSQaWQTARELLRRYRSQQAL 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 270 AklenarlssemntSTVNSAREELMESRMRIESLSS---QLSNLQKESRACLERIQELEDLLAkEKDNSRRMLTDKEREM 346
Cdd:COG3096 511 A-------------QRLQQLRAQLAELEQRLRQQQNaerLLEEFCQRIGQQLDAAEELEELLA-ELEAQLEELEEQAAEA 576
|
330
....*....|....*.
gi 5031877 347 AEIRDQMQQQLNDYEQ 362
Cdd:COG3096 577 VEQRSELRQQLEQLRA 592
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
29-330 |
2.36e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 29 RLQEKE-ELRELNDRLAVYIDKVRSLETENSAL--QLQVTEREEVRGRELTGLKALYET--ELADARRALDDTARERAKL 103
Cdd:COG4913 611 KLAALEaELAELEEELAEAEERLEALEAELDALqeRREALQRLAEYSWDEIDVASAEREiaELEAELERLDASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 104 QIELGKCKAEHDQLllnyakkESDLNGAQIKLREYEAALnskdaalatalgdkKSLEGDLEDLKDQIAQLEASLAAAKKQ 183
Cdd:COG4913 691 EEQLEELEAELEEL-------EEELDELKGEIGRLEKEL--------------EQAEEELDELQDRLEAAEDLARLELRA 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 184 LADETLLKVDLENRCQSLTEDLEFRKsmyeEEINETRRKHETRLVEVDSGRQIEYEYKLAQ------ALHEMREQHDaqv 257
Cdd:COG4913 750 LLEERFAAALGDAVERELRENLEERI----DALRARLNRAEEELERAMRAFNREWPAETADldadleSLPEYLALLD--- 822
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031877 258 RLYKEELEQtYHAKLENARLSSEmntstvnsareelmesrmrIESLSSQLSNLQKESRACLERIQELEDLLAK 330
Cdd:COG4913 823 RLEEDGLPE-YEERFKELLNENS-------------------IEFVADLLSKLRRAIREIKERIDPLNDSLKR 875
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
28-387 |
2.58e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 28 SRLQEKEElRELNDRLAvyidkvrSLETENSALQLQVTEREEVRGREltglkalyetelADARRALDDTARERAKLQIEL 107
Cdd:PRK02224 194 AQIEEKEE-KDLHERLN-------GLESELAELDEEIERYEEQREQA------------RETRDEADEVLEEHEERREEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 108 GKCKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADE 187
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEC 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 188 TLLKVDLENRCQSLTE---DLEFR-------KSMYEEEINETR---RKHETRLVEVDSG-RQIEYEYKLAQALHEMREQH 253
Cdd:PRK02224 334 RVAAQAHNEEAESLREdadDLEERaeelreeAAELESELEEAReavEDRREEIEELEEEiEELRERFGDAPVDLGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 254 DAQVRLYKEEL---EQTYHAKLENARLSSEMNTSTVNSAR--------------EELMESRMRIESLSSQLSNLQKESRA 316
Cdd:PRK02224 414 LEELREERDELrerEAELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEE 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 317 CLERIQELEDL---------LAKEKDNSRRMLTDKEREMAEIRDQMqQQLNDYEQLLDVKlALDMEISAYRKLLEGEEER 387
Cdd:PRK02224 494 VEERLERAEDLveaedrierLEERREDLEELIAERRETIEEKRERA-EELRERAAELEAE-AEEKREAAAEAEEEAEEAR 571
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
155-252 |
2.76e-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: 40.81 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 155 DKKSLEGDL-------EDLKDQIAQLEASLAAAKKQLADETLLKVDLEN--RCQSLT-EDLEFRKSMYEEEINETRRKHE 224
Cdd:pfam05911 696 EKENLEVELasctenlESTKSQLQESEQLIAELRSELASLKESNSLAETqlKCMAESyEDLETRLTELEAELNELRQKFE 775
|
90 100
....*....|....*....|....*...
gi 5031877 225 TRLVEVDSGRQIeYEYKLAqALHEMREQ 252
Cdd:pfam05911 776 ALEVELEEEKNC-HEELEA-KCLELQEQ 801
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
33-386 |
4.07e-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: 40.16 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 33 KEELRELNDRLAVYIDKVRSLETENSALQLQVT-------EREEVRGRELTGLKALYETELADARRALDDTARERAKLQI 105
Cdd:pfam01576 698 KTQLEELEDELQATEDAKLRLEVNMQALKAQFErdlqardEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 106 ELGKCKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLA 185
Cdd:pfam01576 778 DLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARR 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 186 DETLLKVDLENRCQSLTEDlefrKSMYEEEinetRRKHETRLVevdsgrQIEYEYKLAQALHEMREQHDAQVRLYKEELe 265
Cdd:pfam01576 858 QAQQERDELADEIASGASG----KSALQDE----KRRLEARIA------QLEEELEEEQSNTELLNDRLRKSTLQVEQL- 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 266 qtyhakleNARLSSEMNTSTVN-SAREEL----MESRMRIESLSSQLSNLQKESRACLE-RIQELEDLL---AKEKDNSR 336
Cdd:pfam01576 923 --------TTELAAERSTSQKSeSARQQLerqnKELKAKLQEMEGTVKSKFKSSIAALEaKIAQLEEQLeqeSRERQAAN 994
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 5031877 337 RMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEE 386
Cdd:pfam01576 995 KLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEE 1044
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
139-375 |
4.14e-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: 40.16 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 139 EAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETllkvDLENRCQSLTEDLEFRKSMYEEEINE 218
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAET----ELCAEAEEMRARLAARKQELEEILHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 219 TrrkhETRLVEvdsgrqieyEYKLAQALHEMREQHDAQVRLYKEELEQTyhaklENARLSSEMNTSTVNSAREELMEsrm 298
Cdd:pfam01576 80 L----ESRLEE---------EEERSQQLQNEKKKMQQHIQDLEEQLDEE-----EAARQKLQLEKVTTEAKIKKLEE--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 299 RIESLSSQLSNLQKESRACLERIQELEDLLAKEKDNSR---RMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEIS 375
Cdd:pfam01576 139 DILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKslsKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGEST 218
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
167-386 |
4.87e-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: 39.72 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 167 KDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKSMYEEEINETRRKheTRLVEVDSGRQIEYEYKLAQAl 246
Cdd:pfam05557 26 KRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLK--KKYLEALNKKLNEKESQLADA- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 247 hemreqHDAQVRLYKEELEqtYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLE---RIQE 323
Cdd:pfam05557 103 ------REVISCLKNELSE--LRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqRIKE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031877 324 LEDLLAKEKDNSRRMLTDKER--EMAEIRDQMQQQLNDYEQL---LDVKLALDMEISAYRKLLEGEEE 386
Cdd:pfam05557 175 LEFEIQSQEQDSEIVKNSKSElaRIPELEKELERLREHNKHLnenIENKLLLKEEVEDLKRKLEREEK 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
122-186 |
5.25e-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: 5.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5031877 122 AKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLAD 186
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
103-329 |
5.48e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 103 LQIELGKCKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKK 182
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 183 QLADETLLKvdlenrcqsLTEDLEFRKSMYEEEINETRRKHETRLvevdsgRQIEYEYKLAQALHEMREQHDAQVRLYKE 262
Cdd:COG4717 124 LLQLLPLYQ---------ELEALEAELAELPERLEELEERLEELR------ELEEELEELEAELAELQEELEELLEQLSL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5031877 263 ELEQTyhakLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRAC--LERIQELEDLLA 329
Cdd:COG4717 189 ATEEE----LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAalEERLKEARLLLL 253
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
148-336 |
5.97e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 148 ALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADetllkvdLENRCQSLTEDLEFRksmyeeEINETRRKHETRL 227
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE-------LREELEKLEKLLQLL------PLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 228 vevdsgrqIEYEYKLAQALHEMREQHDAQVRLY--KEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSS 305
Cdd:COG4717 142 --------AELPERLEELEERLEELRELEEELEelEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEE 213
|
170 180 190
....*....|....*....|....*....|.
gi 5031877 306 QLSNLQKESRACLERIQELEDLLAKEKDNSR 336
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
106-381 |
7.65e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 106 ELGKCKAEHDQLLLNYAKKESDLNGAQIKLREYEA---ALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKK 182
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEElkeEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 183 Q---------LADETLLKVDLENRCQSLTEDLEFRKSMYEEEINETRRKHETRLVEVDSGRQIEYEYK-LAQALHEMREQ 252
Cdd:PRK03918 281 KvkelkelkeKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKeLEKRLEELEER 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031877 253 HDA--QVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQEledllAK 330
Cdd:PRK03918 361 HELyeEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK-----AK 435
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031877 331 EK-DNSRRMLTDKER---------EMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLL 381
Cdd:PRK03918 436 GKcPVCGRELTEEHRkelleeytaELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI 496
|
|
| |
