|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
32-388 |
1.26e-100 |
|
Intermediate filament protein;
Pssm-ID: 425436 [Multi-domain] Cd Length: 313 Bit Score: 307.61 E-value: 1.26e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 32 QEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKF 111
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKDLETKISELRQKKGAEPSRLYSLYEREIRELRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 112 KAEHDQLLLNYAKKesdlsgaqiklreyeaalnskdaalataLGDKKSLEGDLEDLKdqiaqleaslsaakKQLADETLL 191
Cdd:pfam00038 81 RLAAEDFRQKYEDE----------------------------LNLRQSAEADIVGLR--------------KDLDEATLA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 192 KVDLENRCQSLTEDLEFRKNMYEEEINETRRKH--ETRLVEVDSGRQIEyeykLAQALHEMREQHDAQVRLYKEELEQTY 269
Cdd:pfam00038 119 RVDLEMKIESLKEELAFLKKNHEEEVRELQSQVsdTQVNVEMDAARKLD----LTSALAEIRAQYEEIAEKNREEAEEWY 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 270 HAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDMLAKERDNSRRMLSDREREMAE 349
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRSAKEEITELRRQIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQQ 274
|
330 340 350
....*....|....*....|....*....|....*....
gi 188219589 350 IRDQMQQQLSDYEQLLDVKLALDMEISAYRKLLEGEEER 388
Cdd:pfam00038 275 IRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| LTD |
pfam00932 |
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ... |
440-544 |
1.29e-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: 425951 [Multi-domain] Cd Length: 103 Bit Score: 95.56 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 440 TGNVCIEEIDVDG-----KFIRLKNTSEQDQPMGGWEMIRKIGDTsvsYKYTSRYVLKAGQTVTVWaANAGVTASPPTDL 514
Cdd:pfam00932 4 TGDVVISEVVYDGsggndEFIELYNTGDKAVDLSGWKLSDASGGT---FTFPNGTTLAPGQTVVVW-TGGGAGYWGPLNA 79
|
90 100 110
....*....|....*....|....*....|
gi 188219589 515 IWKNQNSWgtgedvkVILKNSQGEEVAQRS 544
Cdd:pfam00932 80 VWNNGGDA-------VALYDANGELVDSVG 102
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
24-350 |
1.60e-15 |
|
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: 80.10 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 24 SPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEvrgreltglkalyetELADARRALDDTARERAK 103
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEE---------------ELEQLRKELEELSRQISA 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 104 LQIELGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKK 183
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 184 QLADETLLKVDLENRCqsltEDLEFRKNMYEEEINETRRKHETRLVEV-----------DSGRQIEYEYKLAQALHEMRE 252
Cdd:TIGR02168 811 ELTLLNEEAANLRERL----ESLERRIAATERRLEDLEEQIEELSEDIeslaaeieeleELIEELESELEALLNERASLE 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 253 QHDAQVRLYKEELEQTYH----AKLENARLSSEMNTStVNSAREELMESRMRIESLSSQLSNLQKESracLERIQELEDM 328
Cdd:TIGR02168 887 EALALLRSELEELSEELRelesKRSELRRELEELREK-LAQLELRLEGLEVRIDNLQERLSEEYSLT---LEEAEALENK 962
|
330 340
....*....|....*....|..
gi 188219589 329 LAKERDNSRRMLSDREREMAEI 350
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
34-361 |
1.15e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 34 KEELRELndRLAVYIDKVRSLETENSALQLQVTEREEVRgRELTGLKALYETELADARRALDDTARERAKLQIELGKFKA 113
Cdd:TIGR02168 219 KAELREL--ELALLVLRLEELREELEELQEELKEAEEEL-EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 114 EhdqlllnYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLADETLLKV 193
Cdd:TIGR02168 296 E-------ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 194 DLENRCQSLTEDLEFRKNmyeeeinetrrkhetrlvevdsgrqieyeyKLAQALHEMrEQHDAQVRLYKEELEQtyhAKL 273
Cdd:TIGR02168 369 ELESRLEELEEQLETLRS------------------------------KVAQLELQI-ASLNNEIERLEARLER---LED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 274 ENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKEsracLERIQELEDMLAKERDNSRRMLSDREREMAEIR-- 351
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE----LERLEEALEELREELEEAEQALDAAERELAQLQar 490
|
330
....*....|....
gi 188219589 352 ----DQMQQQLSDY 361
Cdd:TIGR02168 491 ldslERLQENLEGF 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
24-367 |
1.47e-10 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 64.35 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 24 SPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVtereevrgRELTGLKALYETELADARRALDDTARERAK 103
Cdd:COG1196 656 SRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNEL--------RSLEDLLEELRRQLEELERQLEELKRELAA 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 104 LQIELGKFKA-------EHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEA 176
Cdd:COG1196 728 LEEELEQLQSrleeleeELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAER 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 177 SLSAAKKQLADETLLKVDLENRCQSLTE---DLEFRKNMYEEEINET---RRKHETRLVEVDSGRQiEYEYKLAQALHEm 250
Cdd:COG1196 808 RLDALERELESLEQRRERLEQEIEELEEeieELEEKLDELEEELEELekeLEELKEELEELEAEKE-ELEDELKELEEE- 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 251 REQHDAQVRLYKEELEQtyhAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDMLA 330
Cdd:COG1196 886 KEELEEELRELESELAE---LKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLETELEREIERLEEEIEALG 962
|
330 340 350
....*....|....*....|....*....|....*..
gi 188219589 331 KERDNSRRMLSDREREMAEIRDQMQQQLSDYEQLLDV 367
Cdd:COG1196 963 PVNLRAIEEYEEVEERYEELKSQREDLEEAKEKLLEV 999
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
34-327 |
2.20e-09 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 60.50 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 34 KEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALyETELADARRALDDTARERAKLQIELGKFKA 113
Cdd:COG1196 750 EEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEEL-EEELEEAERRLDALERELESLEQRRERLEQ 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 114 EHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLAdetllkv 193
Cdd:COG1196 829 EIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELA------- 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 194 dlenRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQhdaqvrlyKEELEQtyhakl 273
Cdd:COG1196 902 ----ELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLETELEREIERLEEE--------IEALGP------ 963
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 188219589 274 enarlssemntstVNS-AREELMESRMRIESLSSQLSNLQKESRACLERIQELED 327
Cdd:COG1196 964 -------------VNLrAIEEYEEVEERYEELKSQREDLEEAKEKLLEVIEELDK 1005
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
71-387 |
1.67e-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: 57.77 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 71 VRGRELTGLKALYETELADARRALDDTARERAKLQIELGKFKAEHDQLLlnyakkeSDLSGAQIKLREYEAALNskdaal 150
Cdd:TIGR02169 660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELS-------QELSDASRKIGEIEKEIE------ 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 151 atalgdkkSLEGDLEDLKDQIAQLEASLSAAKKQLADETLLKVDLENRCQSLTEDLefrkNMYEEEINETRRKhetrlve 230
Cdd:TIGR02169 727 --------QLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL----HKLEEALNDLEAR------- 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 231 vDSGRQIEYEYKLAQALHEMREQHDAQV---------RLYKEELEQTYHAKLENARLSSEMNtstVNSAREELMESRMRI 301
Cdd:TIGR02169 788 -LSHSRIPEIQAELSKLEEEVSRIEARLreieqklnrLTLEKEYLEKEIQELQEQRIDLKEQ---IKSIEKEIENLNGKK 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 302 ESLSSQLSNLQKESRaclERIQELEDmLAKERDNSRRMLSDREREMAEIRDQMQQQLSDYEQLLDVKLALDMEISAYRKL 381
Cdd:TIGR02169 864 EELEEELEELEAALR---DLESRLGD-LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939
|
....*.
gi 188219589 382 LEGEEE 387
Cdd:TIGR02169 940 KGEDEE 945
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
96-389 |
1.75e-08 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 57.42 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 96 DTARERAKLQIELgkFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLE 175
Cdd:COG1196 210 EKAERYQELKAEL--RELELALLLAKLKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 176 ASLSAAKKQLADETLLKVDLENRCqsltEDLEFRKNMYEEEINETRRKHETR--LVEVDSGRQIEYEYKLAQaLHEMREQ 253
Cdd:COG1196 288 EELLELKEEIEELEGEISLLRERL----EELENELEELEERLEELKEKIEALkeELEERETLLEELEQLLAE-LEEAKEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 254 HDAQVRLYKEELEqtyhaklenarlssemntSTVNSAREELMESRMRIESLSSQLSNLQKEsraclerIQELEDmlakER 333
Cdd:COG1196 363 LEEKLSALLEELE------------------ELFEALREELAELEAELAEIRNELEELKRE-------IESLEE----RL 413
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 188219589 334 DNSRRMLSDREREMAEIRDQMQQQLSDYEQLLDVKLALDMEISAYRKLLEGEEERL 389
Cdd:COG1196 414 ERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELEREL 469
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
34-354 |
5.91e-08 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 55.88 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 34 KEELRELndRLAVYIDKVRSLETENSALQLQVTEREEvRGRELTGLKALYETELADARRALDDTARERAKLQIELGKFKA 113
Cdd:COG1196 219 KAELREL--ELALLLAKLKELRKELEELEEELSRLEE-ELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKE 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 114 EHDQLLLN-------YAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLA 186
Cdd:COG1196 296 EIEELEGEisllrerLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 187 DETLlkvdlenRCQSLTEDLEFRKNMYEEEINETRrkhetrlvevdsgRQIEYEYKLAQALHEMREQHDAQVRLYKEELE 266
Cdd:COG1196 376 ELFE-------ALREELAELEAELAEIRNELEELK-------------REIESLEERLERLSERLEDLKEELKELEAELE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 267 QTyHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDMlAKERDNSRRMLSDRERE 346
Cdd:COG1196 436 EL-QTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAE-QRASQGVRAVLEALESG 513
|
....*...
gi 188219589 347 MAEIRDQM 354
Cdd:COG1196 514 LPGVYGPV 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
111-364 |
7.76e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 7.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 111 FKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLADETL 190
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 191 LKVDLENRCQSL---TEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEykLAQALHEMREQHDAQVRLYKEELEQ 267
Cdd:TIGR02168 317 QLEELEAQLEELeskLDELAEELAELEEKLEELKEELESLEAELEELEAELEE--LESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 268 TYHAKLENARLSSEMNTSTVNSAREelmesRMRIESLSSQLSNLQ-KESRACLERIQELEDMLAKERDNSRRMLSDRERE 346
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERL-----QQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250
....*....|....*...
gi 188219589 347 MAEIRDQMQQQLSDYEQL 364
Cdd:TIGR02168 470 LEEAEQALDAAERELAQL 487
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
81-390 |
7.95e-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: 55.46 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 81 ALYETELADARRALDDTARERAKLQIELGKFKAEHDQLLLNYAKKESDLSgAQIKLREYEAALnskdaalatalgdkksL 160
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQA-LLKEKREYEGYE----------------L 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 161 EGDLEDLKDQIAQLEASLSAAKKQLADETLLKVDLENRCQSLTEDLEFR----KNMYEEEINETRRKHETRLVEVDSGRQ 236
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkiKDLGEEEQLRVKEKIGELEAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 237 IEYEYKL-AQALHEMREQHDAQVRLYKEELEQtYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKES 315
Cdd:TIGR02169 309 SIAEKEReLEDAEERLAKLEAEIDKLLAEIEE-LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188219589 316 RACLERIQELEDMLAKERDNSRRMLSDRER---EMAEIRDQMQQQLSDYEQLLDVKLALDMEISAyrklLEGEEERLK 390
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRlseELADLNAAIAGIEAKINELEEEKEDKALEIKK----QEWKLEQLA 461
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
32-214 |
8.33e-08 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 55.49 E-value: 8.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 32 QEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKF 111
Cdd:COG1196 323 ERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEEL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 112 KAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLADETLL 191
Cdd:COG1196 403 KREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKE 482
|
170 180
....*....|....*....|...
gi 188219589 192 KVDLENRCQSLTEDLEFRKNMYE 214
Cdd:COG1196 483 LSSLEARLDRLEAEQRASQGVRA 505
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
26-326 |
1.92e-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: 54.30 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 26 TRLSRLQ----EKEELRELNDRLAVY-----IDKVRSLETENSALQLQVTEREEvrgrELTGLKALYE---TELADARRA 93
Cdd:TIGR02169 198 QQLERLRrereKAERYQALLKEKREYegyelLKEKEALERQKEAIERQLASLEE----ELEKLTEEISeleKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 94 LDDTAR--------ERAKLQIELGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAalatalgDKKSLEGDLE 165
Cdd:TIGR02169 274 LEELNKkikdlgeeEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA-------EIEELEREIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 166 DLKDQIAQLEASLSAAKKQLADetllkvdLENRCQSLTEDLE--FRKNM-YEEEINETRRKHEtrlvevDSGRQIEYEYK 242
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEELED-------LRAELEEVDKEFAetRDELKdYREKLEKLKREIN------ELKRELDRLQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 243 LAQALHEMREQHDAQVRLYKEELEQtYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERI 322
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINE-LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
....
gi 188219589 323 QELE 326
Cdd:TIGR02169 493 AEAE 496
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
34-328 |
3.00e-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: 53.53 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 34 KEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKAL------YETELADARRALDDTARERAKLQIE 107
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELeedlssLEQEIENVKSELKELEARIEELEED 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 108 LGKFKAEHDQLLLNYAKKESDLSGAQIK------------LREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLE 175
Cdd:TIGR02169 774 LHKLEEALNDLEARLSHSRIPEIQAELSkleeevsriearLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 176 ASLSAAKKQLAD------ETLLKV-DLENRCQSLTEDLEFRKNMYEE------EINETRRKHETRLVEVDSGRQIEyEYK 242
Cdd:TIGR02169 854 KEIENLNGKKEEleeeleELEAALrDLESRLGDLKKERDELEAQLRElerkieELEAQIEKKRKRLSELKAKLEAL-EEE 932
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 243 LAQALHEMRE-QHDAQVRLYKEELEQTYHAKLENARLSSEMNtstvNSAREELMESRMRIESLSSQLSNLQKESRACLER 321
Cdd:TIGR02169 933 LSEIEDPKGEdEEIPEEELSLEDVQAELQRVEEEIRALEPVN----MLAIQEYEEVLKRLDELKEKRAKLEEERKAILER 1008
|
....*..
gi 188219589 322 IQELEDM 328
Cdd:TIGR02169 1009 IEEYEKK 1015
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
29-377 |
2.34e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 29 SRLQEKEELRELNDRLAVYIDKVRSLETENSalqlqvTEREEVRGReltglkalyeteLADARRALDDTARERAKLQIEL 108
Cdd:PRK02224 241 EVLEEHEERREELETLEAEIEDLRETIAETE------REREELAEE------------VRDLRERLEELEEERDDLLAEA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 109 GKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLAD- 187
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDr 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 188 -----------ETLLK------VDLENrCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEM 250
Cdd:PRK02224 383 reeieeleeeiEELRErfgdapVDLGN-AEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPV 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 251 REQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSArEELMESRMRIESLSSQLSNLQKESRACLERIQELEDMLA 330
Cdd:PRK02224 462 EGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAE 540
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 188219589 331 KERDNSrrmlSDREREMAEIRDQMQQQLSDYEQLLDVKLALDMEISA 377
Cdd:PRK02224 541 ELRERA----AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
29-390 |
2.38e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 29 SRLQE-KEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYEtelaDARRALDDTARERAKLQIE 107
Cdd:PRK03918 338 ERLEElKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE----ELEKAKEEIEEEISKITAR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 108 LGKFKAEHDQLL-----LNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAK 182
Cdd:PRK03918 414 IGELKKEIKELKkaieeLKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 183 KQLADETLLK--VDLENRCQSLT-EDLEFRKNMYEEEINETRR-KHETRLVEVDSGRQIEYEYKLAQALHEMREqhdaqv 258
Cdd:PRK03918 494 ELIKLKELAEqlKELEEKLKKYNlEELEKKAEEYEKLKEKLIKlKGEIKSLKKELEKLEELKKKLAELEKKLDE------ 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 259 rlyKEELEQTYHAKLENARLSSEmntstvnsarEELMESRMRIESLSSQLSNLqKESRACLERIQELEDMLAKERDNSRR 338
Cdd:PRK03918 568 ---LEEELAELLKELEELGFESV----------EELEERLKELEPFYNEYLEL-KDAEKELEREEKELKKLEEELDKAFE 633
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 188219589 339 MLSDREREMAEIRDQMQQQLS-----DYEQLLDVKLALDMEISAYRKLLEGEEERLK 390
Cdd:PRK03918 634 ELAETEKRLEELRKELEELEKkyseeEYEELREEYLELSRELAGLRAELEELEKRRE 690
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
33-387 |
2.57e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.41 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 33 EKEELRELNDRLAVYIDKVRSLETENSALQLQVTE----REEVRG--RELTGLKALYETELADARRALDDT-------AR 99
Cdd:pfam05483 392 ELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfekiAEELKGkeQELIFLLQAREKEIHDLEIQLTAIktseehyLK 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 100 ERAKLQIELGKFK-------AEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIA 172
Cdd:pfam05483 472 EVEDLKTELEKEKlknieltAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELE 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 173 QLEASLsaakKQLADETLLKVD----------------------LENRCQSLTEDLEfRKNMYEEEINETRRKHETRlVE 230
Cdd:pfam05483 552 SVREEF----IQKGDEVKCKLDkseenarsieyevlkkekqmkiLENKCNNLKKQIE-NKNKNIEELHQENKALKKK-GS 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 231 VDSGRQIEYEYKLAQALHEMreqhdAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSN 310
Cdd:pfam05483 626 AENKQLNAYEIKVNKLELEL-----ASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQH 700
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188219589 311 LQKESRACLERIQELEDMLAKERDNSRRMLSDREREMAEIRDQMQQQLSDYE-QLLDVKLALDMEISAYRKLLEGEEE 387
Cdd:pfam05483 701 KIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKaELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
32-389 |
4.16e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 46.68 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 32 QEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRE------LTGLKALYETELADARRALDDTARERAKLQ 105
Cdd:COG0419 414 ELEKELEELERELEELEEEIKKLEEQINQLESKELMIAELAGAGekcpvcGQELPEEHEKELLELYELELEELEEELSRE 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 106 IELGKFKAEHDQLL--LNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKK 183
Cdd:COG0419 494 KEEAELREEIEELEkeLRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEKLQLQQLKEELRQLEDRLQELKE 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 184 QLADETLL--KVDLENRCQSLTEDLEFRKNMYEE---EINETRRKHETRLVEVDSGRQIEyEYKLAQALHEMREQHDAQV 258
Cdd:COG0419 574 LLEELRLLrtRKEELEELRERLKELKKKLKELEErlsQLEELLQSLELSEAENELEEAEE-ELESELEKLNLQAELEELL 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 259 RLYKEELEQTYHAKLE--NARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKEsracLERIQELEDMLAKERDNS 336
Cdd:COG0419 653 QAALEELEEKVEELEAeiRRELQRIENEEQLEEKLEELEQLEEELEQLREELEELLKK----LGEIEQLIEELESRKAEL 728
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 188219589 337 RRMLSDREremaeirdQMQQQLSDYEQLLDVKLALDMEISAYRKLLEGEEERL 389
Cdd:COG0419 729 EELKKELE--------KLEKALELLEELREKLGKAGLRADILRNLLAQIEAEA 773
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
121-206 |
7.72e-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: 45.10 E-value: 7.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 121 NYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQL-EASLSAAKKQLADETLLKVDLENRC 199
Cdd:TIGR04320 262 KLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTaQNNLATAQAALANAEARLAKAKEAL 341
|
....*..
gi 188219589 200 QSLTEDL 206
Cdd:TIGR04320 342 ANLNADL 348
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
34-360 |
1.54e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 34 KEELRELNDRLAVYIDKVRSLETENSALQLQV----TEREEVRGRELTGLKALYE-TELADARRALDDTARERAK-LQIE 107
Cdd:PRK02224 285 RERLEELEEERDDLLAEAGLDDADAEAVEARReeleDRDEELRDRLEECRVAAQAhNEEAESLREDADDLEERAEeLREE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 108 LGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLAD 187
Cdd:PRK02224 365 AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 188 -ETLLK----------------VDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEM 250
Cdd:PRK02224 445 aEALLEagkcpecgqpvegsphVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEEL 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 251 REQHDAQVRLYKEELEQTYHAKLEnarLSSEMNTstvnsAREELMESRMRIESLSSQLSNLQKESRACLERIQELE---D 327
Cdd:PRK02224 525 IAERRETIEEKRERAEELRERAAE---LEAEAEE-----KREAAAEAEEEAEEAREEVAELNSKLAELKERIESLErirT 596
|
330 340 350
....*....|....*....|....*....|....*
gi 188219589 328 MLAKERDNSRRMLSDRER--EMAEIRDQMQQQLSD 360
Cdd:PRK02224 597 LLAAIADAEDEIERLREKreALAELNDERRERLAE 631
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
172-384 |
1.70e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 172 AQLEASLSAAKKQ---LADETLLKVDLENrcqslTEDLEFRKNMYEEEINETRRKhetrlvevdsgrqieyeykLAQALH 248
Cdd:PRK11281 39 ADVQAQLDALNKQkllEAEDKLVQQDLEQ-----TLALLDKIDRQKEETEQLKQQ-------------------LAQAPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 249 EMREQHDAQVRLYKEELEQTY--HAKLENARLSSEMN--TSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQE 324
Cdd:PRK11281 95 KLRQAQAELEALKDDNDEETRetLSTLSLRQLESRLAqtLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQ 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 325 LEDMLAKERDNSRRMLSDReremaeiRDQMQQQLSdyeqlldvklALDMEISAYRKLLEG 384
Cdd:PRK11281 175 IRNLLKGGKVGGKALRPSQ-------RVLLQAEQA----------LLNAQNDLQRKSLEG 217
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
3-339 |
1.81e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 44.71 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 3 TATPVQQQRAGSRASAPATPLSPTRLSRLQEKEELRELNDRLavyidkvRSLETENSALQLQVTERE---EVRGRELTGL 79
Cdd:pfam15921 502 TASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHL-------RNVQTECEALKLQMAEKDkviEILRQQIENM 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 80 KALyeteLADARRALDDTARERAKLQIELGKFKAEHDQLLLNYAKKESdlsgaqiKLREYEAA---LNSKDAALATALGD 156
Cdd:pfam15921 575 TQL----VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDA-------KIRELEARvsdLELEKVKLVNAGSE 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 157 KKSLEGDLEDLKDQIA-QLEASLSAAKKQLADETLLKVDLENRCQSL---TEDLEFRKNMYEEEINETRRKHETrlVEVD 232
Cdd:pfam15921 644 RLRAVKDIKQERDQLLnEVKTSRNELNSLSEDYEVLKRNFRNKSEEMettTNKLKMQLKSAQSELEQTRNTLKS--MEGS 721
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 233 SGRQIEYEYKLAQALHEMREQHDA---QVRLYKEEL----EQTYHAKLENARLSSEMNT--STVNSAREELMESRMRIES 303
Cdd:pfam15921 722 DGHAMKVAMGMQKQITAKRGQIDAlqsKIQFLEEAMtnanKEKHFLKEEKNKLSQELSTvaTEKNKMAGELEVLRSQERR 801
|
330 340 350
....*....|....*....|....*....|....*.
gi 188219589 304 LSSQLSNLQKESRACLERIQELEDMLAKERDNSRRM 339
Cdd:pfam15921 802 LKEKVANMEVALDKASLQFAECQDIIQRQEQESVRL 837
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
116-390 |
4.38e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 43.21 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 116 DQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLADETLLKVDL 195
Cdd:COG0419 203 DLLEALEEELKELKKLEEIQEEQEEEELEQEIEALEERLAELEEEKERLEELKARLLEIESLELEALKIREEELRELERL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 196 ENRCQSLTEDLEFRKNMYEEEINEtrrkhetrlvevdsgrqieyEYKLAQALHEMREQHDAQVRLykEELEQTYHAKLEN 275
Cdd:COG0419 283 LEELEEKIERLEELEREIEELEEE--------------------LEGLRALLEELEELLEKLKSL--EERLEKLEEKLEK 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 276 ARLSSEMNTSTVNSAREELmesRMRIESLSSQLSNLQKESRACLERIQELEDMLAKERdNSRRMLSDREREMAEIRDQMQ 355
Cdd:COG0419 341 LESELEELAEEKNELAKLL---EERLKELEERLEELEKELEKALERLKQLEEAIQELK-EELAELSAALEEIQEELEELE 416
|
250 260 270
....*....|....*....|....*....|....*
gi 188219589 356 QQLSDYEQLLDVKLALDMEISAYRKLLEGEEERLK 390
Cdd:COG0419 417 KELEELERELEELEEEIKKLEEQINQLESKELMIA 451
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
164-391 |
4.47e-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: 43.29 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 164 LEDLKDQIAQLEASLSAAKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSgrqieyeyKL 243
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADA--------AV 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 244 AQALHEMrEQHDAQVRLYKEELEQTYHAKLENA-RLSSEMNtsTVNSAREELMESRMRIESLSSQLSnlQKESRACLERI 322
Cdd:pfam12128 318 AKDRSEL-EALEDQHGAFLDADIETAAADQEQLpSWQSELE--NLEERLKALTGKHQDVTAKYNRRR--SKIKEQNNRDI 392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 188219589 323 QELEDMLAKERDnsrrmlsDREREMAEIRDQMQQQLSDYEQLLDVKLaLDMEISAYRKLLEGEEERLKL 391
Cdd:pfam12128 393 AGIKDKLAKIRE-------ARDRQLAVAEDDLQALESELREQLEAGK-LEFNEEEYRLKSRLGELKLRL 453
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
160-382 |
5.04e-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: 43.29 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 160 LEGDLEDLKDQIAQLEASLSAAKKQL----ADETLLKVDLEN---RCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVD 232
Cdd:pfam12128 609 AEEALQSAREKQAAAEEQLVQANGELekasREETFARTALKNarlDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLE 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 233 sGRQIEYEYKLAQALHEMREQ---HDAQVRLYKEELEQTYHAKLenARLSSEMNTSTVNSARE--ELMESRMR------- 300
Cdd:pfam12128 689 -AQLKQLDKKHQAWLEEQKEQkreARTEKQAYWQVVEGALDAQL--ALLKAAIAARRSGAKAElkALETWYKRdlaslgv 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 301 -----------IESLSSQLSNLQKESRACLERIQELEDMLAKERDNSRRMLSDREREMAEIRDQMQQQLSDYEqlLDVKl 369
Cdd:pfam12128 766 dpdviaklkreIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTK--LRRA- 842
|
250
....*....|...
gi 188219589 370 ALDMEISAYRKLL 382
Cdd:pfam12128 843 KLEMERKASEKQQ 855
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
32-390 |
6.22e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 42.83 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 32 QEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREevrgRELTGLKALYETELADARRALDDTARERAKLQIELGKF 111
Cdd:COG0419 326 SLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERL----KELEERLEELEKELEKALERLKQLEEAIQELKEELAEL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 112 KAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEgdledlkdQIAQLEASLSAAKKQLADETLL 191
Cdd:COG0419 402 SAALEEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKELMIA--------ELAGAGEKCPVCGQELPEEHEK 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 192 KVDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEyKLAQALHEMREQHDA---QVRLYKEELEQT 268
Cdd:COG0419 474 ELLELYELELEELEEELSREKEEAELREEIEELEKELRELEEELIELLE-LEEALKEELEEKLEKlenLLEELEELKEKL 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 269 YHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSqLSNLQKESRACLERIQELedMLAKERDNSRRMLSDREREMA 348
Cdd:COG0419 553 QLQQLKEELRQLEDRLQELKELLEELRLLRTRKEELEE-LRERLKELKKKLKELEER--LSQLEELLQSLELSEAENELE 629
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 188219589 349 EIRdqmqQQLSDYEQLLDVKLALDMEISAYRKLLEGEEERLK 390
Cdd:COG0419 630 EAE----EELESELEKLNLQAELEELLQAALEELEEKVEELE 667
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
33-331 |
9.95e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 9.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 33 EKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEvrgrELTGLKALYEtELADARRALDDTaRERAKLQIELGKFK 112
Cdd:PRK03918 229 EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE----RIEELKKEIE-ELEEKVKELKEL-KEKAEEYIKLSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 113 AEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLK------DQIAQLEASLSAAKKQLA 186
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEerhelyEEAKAKKEELERLKKRLT 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 187 DETLLKVDLEnrcqslTEDLEFRKNMYEEEINE-TRRKHETRLVEVDSGRQIEyEYKLAQAL-----HEMREQHdaqvrl 260
Cdd:PRK03918 383 GLTPEKLEKE------LEELEKAKEEIEEEISKiTARIGELKKEIKELKKAIE-ELKKAKGKcpvcgRELTEEH------ 449
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 188219589 261 yKEELEQTYHAKLENarLSSEMntSTVNSAREELMESRMRIESLSSQLSNLQKEsRACLERIQELEDMLAK 331
Cdd:PRK03918 450 -RKELLEEYTAELKR--IEKEL--KEIEEKERKLRKELRELEKVLKKESELIKL-KELAEQLKELEEKLKK 514
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
78-346 |
1.29e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 41.25 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 78 GLKALYETELADARRaLDDTARERAKLQIELGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDK 157
Cdd:COG4942 25 AVLAAAFSAAADDKQ-LKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 158 KSLEGDLEDLKDQIAQLeasLSAAKKQLADETLLKVDLENRCQSltedlEFRKNMYEEEINETRRKHETRLVEVDSGRQi 237
Cdd:COG4942 104 NALEVQEREQRRRLAEQ---LAALQRSGRNPPPALLVSPEDAQR-----SVRLAIYYGALNPARAERIDALKATLKQLA- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 238 eyeyKLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTstvnsareELMESRMRIESLSSQLSNLQKE-SR 316
Cdd:COG4942 175 ----AVRAEIAAEQAELTTLLSEQRAQQAKLAQLLEERKKTLAQLNS--------ELSADQKKLEELRANESRLKNEiAS 242
|
250 260 270
....*....|....*....|....*....|
gi 188219589 317 ACLERIQELEDMLAKERDNSRRMLSDRERE 346
Cdd:COG4942 243 AEAAAAKAREAAAAAEAAAARARAAEAKRT 272
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
235-399 |
1.68e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 235 RQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYH--AKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQ 312
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLReiNEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 313 KESRACLERIQELEDMLAKERDNSRRmLSDREREMAEIRDQMQQQL---SDYEQLLDVKLALDMEISAYRKLLEGEEERL 389
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKAEEYIklsEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170
....*....|
gi 188219589 390 KLSPSPSSRV 399
Cdd:PRK03918 331 KELEEKEERL 340
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
29-368 |
1.74e-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: 429718 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 29 SRLQEKeeLRELNDRLAVYIDKVRSLETENSALQlQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIEL 108
Cdd:pfam07888 34 NRLEEC--LQERAELLQAQEAANRQREKEKERYK-RDREQWERQRRELESRVAELKEELRQSREKVEELEEKYKELSRSG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 109 GKFKAEHDQLLLNYAKKESdlsgaqiKLREYEAALnskdAALATALGDKkslEGDLEDLKDQIAQLEASLsaaKKQLADE 188
Cdd:pfam07888 111 EELAEEKDALLAQRAESEA-------RIRELEEDI----KTLTQRVLER---ETELERMKERVKKAGAQR---KEEEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 189 TLLKVDL---ENRCQSLTEDLEFRKNMYEEEINETRRKHE-----TRLVEVDSGRQIEYEYKLAQ--ALHEMREQHDAQV 258
Cdd:pfam07888 174 KQLQAKLqqtEEELRSLSKEFQELRNSLAQRDTQVLQLQDtittlTQKLTTAHRKEAENEALLEElrSLQERLNASERKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 259 RLYKEELEQTY------HAKLENARLSSEMNTSTVNSAREELMESRM------------------RIESLSSQLsnLQKE 314
Cdd:pfam07888 254 EGLGEELSSMAaqrdrtQAELHQARLQAAQLTLQLADASLALREGRArwaqeretlqqsaeadkdRIEKLSAEL--QRLE 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 188219589 315 SRACLERIQ--ELEDMLAKERDNSRRMLSDREREMAEIRDQMQQQLSDYEQLLDVK 368
Cdd:pfam07888 332 ERLQEERMEreKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK 387
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
157-390 |
1.92e-03 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 41.24 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 157 KKSLEGDLEDLKDQIAQLE--ASLSAAKKQLaDETLLKVDLENRCQSLtEDLEFRKNMYEEEINETRRKHETRLVEVDSg 234
Cdd:COG1196 195 LEELEKQLEKLERQAEKAEryQELKAELREL-ELALLLAKLKELRKEL-EELEEELSRLEEELEELQEELEEAEKEIEE- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 235 rqieyeykLAQALHEMREQ-HDAQVRLYKEELE-QTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQ 312
Cdd:COG1196 272 --------LKSELEELREElEELQEELLELKEEiEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERE 343
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188219589 313 KESRACLERIQELEDMLAKERDNSRRMLSDREREMAEIRDQMQQQLSDYEQLLDVKLALDMEISAYRKLLEGEEERLK 390
Cdd:COG1196 344 TLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLE 421
|
|
| COG4913 |
COG4913 |
Uncharacterized protein, contains a C-terminal ATPase domain [Function unknown]; |
89-364 |
2.28e-03 |
|
Uncharacterized protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 227250 [Multi-domain] Cd Length: 1104 Bit Score: 41.16 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 89 DARRALDDTARER------AKLQIELGKFKAEHDQLLLnYAKKESDLSGAQIKLREYEAALNsKDAALATALGDKKSLEG 162
Cdd:COG4913 597 DDRRKLGDRSTYRlgstndAKVETLRETVKAMLSREDF-YMIKIMRQQGEYIKLQEQANALA-HIQALNFASIDLPSAQR 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 163 DLEDLKDQIAQLEASLSA---AKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEY 239
Cdd:COG4913 675 QIAELQARLERLTHTQSDiaiAKAALDAAQTRQKVLERQYQQEVTECAGLKKDLKRAAMLSRKVHSIAKQGMTGALQALG 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 240 EyklAQALHEMREQHDAQVRLYKEELEQTYHAKL--ENARL-----------SSEMNTSTVNSA---------------- 290
Cdd:COG4913 755 A---AHFPQVAPEQHDDIVDIERIEHRRQLQKRIdaVNARLrrlreeiigrmSDAKKEDTAALSevgaelddipeylarl 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 291 ----REELME---------SRMRIESLSSQLSNLQKESRACLERIQELEDMLAKERDNSRRMLSDREREMAEIRDQMQQQ 357
Cdd:COG4913 832 qtltEDALPEflarfqellNRSSDDGVTQLLSHLDHERALIEERIEAINDSLRRVDFNSGRYLHIDIAKQPVPHDSMRTF 911
|
....*..
gi 188219589 358 LSDYEQL 364
Cdd:COG4913 912 QQALRAL 918
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
167-390 |
2.57e-03 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 40.85 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 167 LKDQIAQLEASLSAAKKQLADETLLKVDLENRCQSLTEdlEFRKNMYEEEINETRRKHEtrlvevdsGRQIEYEYKLAQA 246
Cdd:COG1196 170 YKERKEEAERKLERTEENLERLEDLLEELEKQLEKLER--QAEKAERYQELKAELRELE--------LALLLAKLKELRK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 247 LhemREQHDAQVRLYKEELEQTYhAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELE 326
Cdd:COG1196 240 E---LEELEEELSRLEEELEELQ-EELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELE 315
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 188219589 327 DMLAKERDNSRRMLSDREREMAEIRDQmQQQLSDYEQLLDVKLALDMEISAYRKLLEGEEERLK 390
Cdd:COG1196 316 NELEELEERLEELKEKIEALKEELEER-ETLLEELEQLLAELEEAKEELEEKLSALLEELEELF 378
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
85-389 |
3.89e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 40.25 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 85 TELADARRALDDTARERAKLQIELGKFKAEHD------QLLLN-------YAKKESDLSGAQIKLREYEAALNSKDAALA 151
Cdd:COG3096 300 QQLAAEQYRHVDMSRELAELNGAEGDLEADYQaasdhlNLVQTalrqqekIERYQADLEELTIRLEEQNEVVEEANERQE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 152 TALGDKKSLEGDLEDLKDQIAQLEASLSAAK----------------KQLADETLLKVD--------LENRCQSLTED-L 206
Cdd:COG3096 380 ENEARAEAAELEVDELKSQLADYQQALDVQQtraiqyqqaiaaleraKELCHLPDLTADsaeewletFQAKEEEATEKlL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 207 EFRKNMYEEEINETRRKHETRLV-----EV------DSGRQIEYEYKLAQALhemrEQHDAQVRLYKEELEQTYHAKLEN 275
Cdd:COG3096 460 SLEQKMSMAQAAHSQFEQAYQLVvaiagELarseawDVARELLREGPDQRHL----AEQVQPLRMRLSELEQRLRQQQSA 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 276 ARLSSEMNTSTVNSAREELMES-----RMRIESLSSQLSNlQKESRACLEriQELEDMLAKERDNSRRM---------LS 341
Cdd:COG3096 536 ERLLADFCKRQGKNLDAEELEAlhqelEALIESLSDSVSN-AREQRMALR--QEQEQLQSRIQSLMQRApvwlaaqnaLE 612
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 188219589 342 DREREMAEIRDQMQQQLSDYEQLLDVKLALDME---ISAYRKLLEGEEERL 389
Cdd:COG3096 613 QLSEQSGEEFTDSQDVTEYMQQLLEREREATVErdeLGARKNALDEEIERL 663
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
21-331 |
4.41e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 21 TPLSPTRLSRLQEKEELR--ELNDRLAVYIDKVRSLETENSALQLQVTEREEVR------GRELT-----GLKALYETEL 87
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAkeEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcGRELTeehrkELLEEYTAEL 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 88 ADARRALDDTARERAKLQ---IELGKFKAEHDQLLLNYAK-----------KESDLSGAQIKLREYE------AALNSKD 147
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRkelRELEKVLKKESELIKLKELaeqlkeleeklKKYNLEELEKKAEEYEklkeklIKLKGEI 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 148 AALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLADETLLKV-DLENRCQSL----TEDLEFRKNMYEEEINETRR 222
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVeELEERLKELepfyNEYLELKDAEKELEREEKEL 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 223 KHETRLVEvdsgRQIEYEYKLAQALHEMREQHDAQVRLYKEEleqtYHAKLENARLSSEMNTSTVNSAREELMESRMRIE 302
Cdd:PRK03918 622 KKLEEELD----KAFEELAETEKRLEELRKELEELEKKYSEE----EYEELREEYLELSRELAGLRAELEELEKRREEIK 693
|
330 340
....*....|....*....|....*....
gi 188219589 303 SLSSQLSNLQKESRACLERIQELEDMLAK 331
Cdd:PRK03918 694 KTLEKLKEELEEREKAKKELEKLEKALER 722
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
29-356 |
6.48e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 29 SRLQEKEElRELNDRLAvyidkvrSLETENSALQLQVTEREEVRGREltglkalyetelADARRALDDTARERAKLQIEL 108
Cdd:PRK02224 194 AQIEEKEE-KDLHERLN-------GLESELAELDEEIERYEEQREQA------------RETRDEADEVLEEHEERREEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 109 GKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLADE 188
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEC 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 189 TLLKVDLENRCQSLTE---DLEFRKNMYEEEINE----------TRRKHETRLVEVDSG-RQIEYEYKLAQALHEMREQH 254
Cdd:PRK02224 334 RVAAQAHNEEAESLREdadDLEERAEELREEAAEleseleeareAVEDRREEIEELEEEiEELRERFGDAPVDLGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 255 DAQVRLYKEEL---EQTYHAKLENARLSSEMNTSTVNSAR--------------EELMESRMRIESLSSQLSNLQKESRA 317
Cdd:PRK02224 414 LEELREERDELrerEAELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEE 493
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 188219589 318 CLERIQELEDM---------LAKERDNSRRMLSDREREMAEIRDQMQQ 356
Cdd:PRK02224 494 VEERLERAEDLveaedrierLEERREDLEELIAERRETIEEKRERAEE 541
|
|
| HlyD |
pfam00529 |
HlyD membrane-fusion protein of T1SS; HlyD is a component of the prototypical alpha-haemolysin ... |
104-268 |
6.75e-03 |
|
HlyD membrane-fusion protein of T1SS; HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD and HlyB are inner-membrane proteins and specific components of the transport apparatus of alpha-haemolysin. 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: 38.94 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 104 LQIELGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGdkksLEGDLEDLKDQIAQLEASLSAAKK 183
Cdd:pfam00529 49 FQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDG----ATAQLRAAQAAVKAAQAQLAQAQI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 184 QLAD-ETLLKVDLENRCQSLTEDLEFRKNmyEEEINETRRKHETRLVEVDSGRQieyeyKLAQALHEMREQHDAQVRLYK 262
Cdd:pfam00529 125 DLARrRVLAPIGGISRESLVTAGALVAQA--QANLLATVAQLDQIYVQITQSAA-----ENQAEVRSELSGAQLQIAEAE 197
|
....*.
gi 188219589 263 EELEQT 268
Cdd:pfam00529 198 AELKLA 203
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
168-387 |
8.12e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 428520 [Multi-domain] Cd Length: 660 Bit Score: 38.94 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 168 KDQIAQLEASLSAAKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEEINETRRKheTRLVEVDSGRQIEYEYKLAQAl 247
Cdd:pfam05557 26 KRARIELERKASALARQLERESDRNQELQKRIRLLEKREAEAEEALREQAELNRLK--KKNLEALNKKLNEKESQLADA- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 248 hemreqHDAQVRLYKEELEqtYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLE---RIQE 324
Cdd:pfam05557 103 ------REVISCLKNELSE--LRRQIQRQELELSSTNSELEELQERLDLQKAKAQEAEQLRQNLEAQQSSLAEaeqRIKE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188219589 325 LEDMLAKERDNSRRMLSDRER--EMAEIRDQMQQQLSDYEQL---LDVKLALDMEISAYRKLLEGEEE 387
Cdd:pfam05557 175 LEFEIQSQEQDSEIVKNSKSElaRIPELERELERLREHNKHLnenIENKLLLKEEVEDLKRKLEREEG 242
|
|
|