|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
30-287 |
2.66e-72 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 233.66 E-value: 2.66e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 30 AAQARLKDL-EALLNSKEAALSTALSEKRTLEGELHDLRGQVAKL--------------EAALGEAKKQLQDEMLRRVDA 94
Cdd:pfam00038 43 AEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFrqkyedelnlrtsaENDLVGLRKDLDEATLARVDL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 95 ENRLQTMKEELDFQKNIYSEELRETKRRH--ETRLVEIDNGKQREfesrLADALQELRAQHEDQVEQYKKELEKTYSAKL 172
Cdd:pfam00038 123 EAKIESLKEELAFLKKNHEEEVRELQAQVsdTQVNVEMDAARKLD----LTSALAEIRAQYEEIAAKNREEAEEWYQSKL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 173 DNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRAR 252
Cdd:pfam00038 199 EELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQE 278
|
250 260 270
....*....|....*....|....*....|....*
gi 2243207293 253 MQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEER 287
Cdd:pfam00038 279 MARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| LTD |
pfam00932 |
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ... |
335-442 |
2.79e-21 |
|
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: 89.02 E-value: 2.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 335 ARTSGRVAVEEVDEEG-----KFVRLRNKSNEDQSMGNWQIKRQNGDdpllTYRFPPKFTLKAGQVVTIWAAG----AGA 405
Cdd:pfam00932 1 SSATGDVVISEVVYDGsggndEFIELYNTGSKAVDLSGWKLQDASGG----TYTFPNGTTLAPGQTVVVWTGSgtnsATA 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2243207293 406 THSPPTDLVWKAQNTWgcgnslrTALINSTGEEVAMR 442
Cdd:pfam00932 77 GYWGPSNAVWNNGGDA-------VALYDANGELVDSV 106
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
23-287 |
4.10e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.91 E-value: 4.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 23 KKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMK 102
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 103 EELDfQKNIYSEELRETKRRHETRLVEIDNgKQREFESRLADALQELRAQHEDQVEQyKKELEKTYSAKLDNARQSAERN 182
Cdd:COG1196 323 EELA-ELEEELEELEEELEELEEELEEAEE-ELEEAEAELAEAEEALLEAEAELAEA-EEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 183 SNLVGAAhEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQE 262
Cdd:COG1196 400 AQLEELE-EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
250 260
....*....|....*....|....*
gi 2243207293 263 LLDIKLALDMEIHAYRKLLEGEEER 287
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADY 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
30-290 |
1.74e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 30 AAQARL-KDLEALLNSKEAALstALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELdfq 108
Cdd:COG1196 209 AEKAERyRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 109 kniysEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKtysAKLDNARQSAERNSNLVGA 188
Cdd:COG1196 284 -----EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE---EELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 189 AHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKL 268
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260
....*....|....*....|..
gi 2243207293 269 ALDMEIHAYRKLLEGEEERLRL 290
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEE 457
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
25-288 |
1.78e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 25 EGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRlqtmKEE 104
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE----IEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 105 LDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRlaDALQELRAQHEDQveqykkelektySAKLDNARQSAERNSN 184
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR--EALDELRAELTLL------------NEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 185 LVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLAR---ERDTSRRLLAEKEREMAEMRARMQQQLDEYQ 261
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnERASLEEALALLRSELEELSEELRELESKRS 911
|
250 260
....*....|....*....|....*..
gi 2243207293 262 ELLDIKLALDMEIHAYRKLLEGEEERL 288
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
62-348 |
2.41e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 62 ELHDLRGQVAKLEAALGEAKKQLQdemlrrvDAENRLQTMKEELdfqkniysEELRETKRRHETRLVEIDNGKQR----- 136
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALA-------ELRKELEELEEEL--------EQLRKELEELSRQISALRKDLARleaev 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 137 EFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSnLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAA 216
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA-QIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 217 KEAKLRDLEDSLARERDTSRRLLAEKER----------EMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEE 286
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEElsedieslaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2243207293 287 RLRlspSPTSQRSRGRASSHSSQTQGGGSVTKKRKLESTESR--SSFSQHARTSGRVAVEEVDE 348
Cdd:TIGR02168 902 ELR---ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNlqERLSEEYSLTLEEAEALENK 962
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
14-253 |
3.63e-12 |
|
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: 68.25 E-value: 3.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 14 AEAMVDGNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVD 93
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 94 AENRLQTMKEEldfqkniYSEELRET-KRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEktysaKL 172
Cdd:COG4942 95 LRAELEAQKEE-------LAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-----EL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 173 DNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRAR 252
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
.
gi 2243207293 253 M 253
Cdd:COG4942 243 T 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
30-302 |
9.56e-12 |
|
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: 66.71 E-value: 9.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 30 AAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQK 109
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 110 NIYSEELRET-KRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEktysakldnarqsaernsnlvga 188
Cdd:COG4942 104 EELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----------------------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 189 aheelqqsriridslsaQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKL 268
Cdd:COG4942 161 -----------------ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250 260 270
....*....|....*....|....*....|....
gi 2243207293 269 ALDMEIhayRKLLEGEEERLRLSPSPTSQRSRGR 302
Cdd:COG4942 224 ELEALI---ARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
22-289 |
1.78e-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: 67.39 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 22 TKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLeaalgEAKKQLQDEMLRRVDAEN-RLQT 100
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL-----EQQKQILRERLANLERQLeELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 101 MKEELDFQKNIYSEELRETKRRHETRLVEIDNgkQREFESRLADALQELraqhEDQVEQYKKELEkTYSAKLDNARQSAE 180
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELES--LEAELEELEAELEEL----ESRLEELEEQLE-TLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 181 RNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLaaKEAKLRDLEDSLArERDTSRRLLAEKEREMAEMRARMQQQLDEY 260
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKL--EEAELKELQAELE-ELEEELEELQEELERLEEALEELREELEEA 473
|
250 260
....*....|....*....|....*....
gi 2243207293 261 QELLDIKLALDMEIHAYRKLLEGEEERLR 289
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
31-295 |
6.96e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.32 E-value: 6.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 31 AQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAA---------LGEAKKQLQD--EMLRRVDAEN-RL 98
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswdeidVASAEREIAEleAELERLDASSdDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 99 QTMKEELdfqkniysEELRETKRRHETRLVEIdNGKQREFESRLADAlQELRAQHEDQVEQYKKELEKTYSAKLDnARQS 178
Cdd:COG4913 688 AALEEQL--------EELEAELEELEEELDEL-KGEIGRLEKELEQA-EEELDELQDRLEAAEDLARLELRALLE-ERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 179 AERNSNLVGAAHEELQQsriRIDSLSAQLSQLQKQLAAK--------EAKLRDLEDSLARERDTSRRLLAEKEREMAEMR 250
Cdd:COG4913 757 AALGDAVERELRENLEE---RIDALRARLNRAEEELERAmrafnrewPAETADLDADLESLPEYLALLDRLEEDGLPEYE 833
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2243207293 251 ARMQQQLDE--YQELLDIKLALDMEIHAYRKLLE-----------GEEERLRLSPSPT 295
Cdd:COG4913 834 ERFKELLNEnsIEFVADLLSKLRRAIREIKERIDplndslkripfGPGRYLRLEARPR 891
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
29-289 |
7.35e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 29 IAAQARLKDLEALLnskeAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELdFQ 108
Cdd:COG1196 218 LKEELKELEAELLL----LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE-YE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 109 KNIYSEELRETKRRHETRLveIDNGKQREfesRLADALQELRAQHEDQVEQYKKELEKtySAKLDNARQSAERNsnLVGA 188
Cdd:COG1196 293 LLAELARLEQDIARLEERR--RELEERLE---ELEEELAELEEELEELEEELEELEEE--LEEAEEELEEAEAE--LAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 189 AHEELQQSRIRIDSLSAQLSQLQKQLAA--KEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDI 266
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEAlrAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
250 260
....*....|....*....|...
gi 2243207293 267 KLALDMEIHAYRKLLEGEEERLR 289
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLA 466
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
11-252 |
6.04e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 6.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 11 EPDAEAMVDgntkkegdliAAQARLKDLEALlnskEAALSTALSEKRTLEgelhDLRGQVAKLEAALGEA-KKQLQDEML 89
Cdd:COG4913 220 EPDTFEAAD----------ALVEHFDDLERA----HEALEDAREQIELLE----PIRELAERYAAARERLaELEYLRAAL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 90 RRVDAENRLQTMKEELdfqkniysEELRETKRRHETRLVEIDNgKQREFESRLADALQELRAQHEDQVEQYKKELEKTyS 169
Cdd:COG4913 282 RLWFAQRRLELLEAEL--------EELRAELARLEAELERLEA-RLDALREELDELEAQIRGNGGDRLEQLEREIERL-E 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 170 AKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEM 249
Cdd:COG4913 352 RELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
...
gi 2243207293 250 RAR 252
Cdd:COG4913 432 ERR 434
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
25-286 |
8.21e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.01 E-value: 8.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 25 EGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQ--DEMLRRVDAE-NRLQTM 101
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSslEQEIENVKSElKELEAR 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 102 KEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADalQELRAQHEDQVEQyKKELEKTYsakLDNARQSAER 181
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSR--IEARLREIEQKLN-RLTLEKEY---LEKEIQELQE 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 182 NSNLVGAAHEELQQsriRIDSLSAQLSQLQKQLAAKEAKLRDLEDS---LARERDTSRRLLAEKEREMAEMRARMQQQLD 258
Cdd:TIGR02169 841 QRIDLKEQIKSIEK---EIENLNGKKEELEEELEELEAALRDLESRlgdLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
250 260
....*....|....*....|....*...
gi 2243207293 259 EYQELLDIKLALDMEIHAYRKLLEGEEE 286
Cdd:TIGR02169 918 RLSELKAKLEALEEELSEIEDPKGEDEE 945
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
28-349 |
2.63e-09 |
|
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: 60.07 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 28 LIAAQARLKDLEALLNSKEAALSTaLSEKRTLEGELHDLRGQVAKLEAAL-GEAKKQLQDEMLRRVDAENRLQTMKEELD 106
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKS-LERQAEKAERYKELKAELRELELALlVLRLEELREELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 107 FQKNIYSEELRETKRRH---ETRLVEID------NGKQREFESRLAdALQELRAQHEDQVEQYKKELEKTYSAKLDNARQ 177
Cdd:TIGR02168 260 AELQELEEKLEELRLEVselEEEIEELQkelyalANEISRLEQQKQ-ILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 178 SAERNsnlvgaahEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDslarERDTSRRLLAEKEREMAEMRARMQQQL 257
Cdd:TIGR02168 339 LAELE--------EKLEELKEELESLEAELEELEAELEELESRLEELEE----QLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 258 DEYQELLDIKLALDMEIHA-YRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHAR 336
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEElLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
330
....*....|...
gi 2243207293 337 TSGRVAVEEVDEE 349
Cdd:TIGR02168 487 LQARLDSLERLQE 499
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
90-289 |
1.37e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 90 RRVDAENRLQTMKEELD-------------------------FQKniYSEELREtkRRHETRLVEID--NGKQREFESRL 142
Cdd:COG1196 173 RKEEAERKLEATEENLErledilgelerqleplerqaekaerYRE--LKEELKE--LEAELLLLKLRelEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 143 ADALQELR------AQHEDQVEQYKKELE------KTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQL 210
Cdd:COG1196 249 EELEAELEeleaelAELEAELEELRLELEelelelEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 211 QKQLAAKEAKLRDLEDSLAR---ERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEER 287
Cdd:COG1196 329 EEELEELEEELEELEEELEEaeeELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
..
gi 2243207293 288 LR 289
Cdd:COG1196 409 EE 410
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
13-265 |
1.43e-07 |
|
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: 54.13 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 13 DAEAMVDGNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEK----RTLEGELHDLRGQVAKLEAALGEAKK------ 82
Cdd:pfam07888 84 ELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHeariRELEEDIKTLTQRVLERETELERMKErakkag 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 83 -QLQDEMLRRVDAENRLQTMKEEL-----DFQKNIYSEELRETK----RRHETRLVEIDNGKQR---EFESRLAD--ALQ 147
Cdd:pfam07888 164 aQRKEEEAERKQLQAKLQQTEEELrslskEFQELRNSLAQRDTQvlqlQDTITTLTQKLTTAHRkeaENEALLEElrSLQ 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 148 ELRAQHEDQVEQYKKELEKTYS------AKLDNAR-QSAERNSNLVGAA-------------HEELQQS----RIRIDSL 203
Cdd:pfam07888 244 ERLNASERKVEGLGEELSSMAAqrdrtqAELHQARlQAAQLTLQLADASlalregrarwaqeRETLQQSaeadKDRIEKL 323
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2243207293 204 SAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQ-------QQLDEYQELLD 265
Cdd:pfam07888 324 SAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRvaqkekeQLQAEKQELLE 392
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
34-289 |
2.42e-07 |
|
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: 54.03 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 34 RLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQL--------------------QDEMLRRV- 92
Cdd:pfam01576 750 QVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLkklqaqmkdlqreleearasRDEILAQSk 829
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 93 DAENRLQTMKEE-LDFQKNIYSEE--------------------------LRETKRRHETRLVEIDngKQREFESRLADA 145
Cdd:pfam01576 830 ESEKKLKNLEAElLQLQEDLAASErarrqaqqerdeladeiasgasgksaLQDEKRRLEARIAQLE--EELEEEQSNTEL 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 146 LQELRAQHEDQVEQYKKEL--EKTYSAKLDNARQSAERNSNLVGAAHEELQqsriridslSAQLSQLQKQLAAKEAKLRD 223
Cdd:pfam01576 908 LNDRLRKSTLQVEQLTTELaaERSTSQKSESARQQLERQNKELKAKLQEME---------GTVKSKFKSSIAALEAKIAQ 978
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2243207293 224 LEDSL---ARERDTSRRLLAEKEREMAEMRARMQ---QQLDEYQELLDiKLALDMEiHAYRKLLEGEEERLR 289
Cdd:pfam01576 979 LEEQLeqeSRERQAANKLVRRTEKKLKEVLLQVEderRHADQYKDQAE-KGNSRMK-QLKRQLEEAEEEASR 1048
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
26-286 |
2.95e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 26 GDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQ-------DEMLRRVDAENRL 98
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelrallEERFAAALGDAVE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 99 QTMKEELdfQKNIysEELRETKRRHETRLVEIDNGKQREFESRLAD------ALQELRAQHEDQVEQykkELEKtYSAKL 172
Cdd:COG4913 765 RELRENL--EERI--DALRARLNRAEEELERAMRAFNREWPAETADldadleSLPEYLALLDRLEED---GLPE-YEERF 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 173 DNARQSAERN--SNLVGAAHEELQQSRIRIDSLSAQLSQLQ------KQLAAKEAKL-------RDLEDSLARERDTSRR 237
Cdd:COG4913 837 KELLNENSIEfvADLLSKLRRAIREIKERIDPLNDSLKRIPfgpgryLRLEARPRPDpevrefrQELRAVTSGASLFDEE 916
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2243207293 238 LLAEKEREMAEMRARMQQQlDEYQELLDIKLALD----MEIHAYRKLLEGEEE 286
Cdd:COG4913 917 LSEARFAALKRLIERLRSE-EEESDRRWRARVLDvrnhLEFDAEEIDREDGEE 968
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
86-291 |
3.24e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 86 DEMLRRVDAENRLQTMKEELDFQKNIYSEELRE---TKRRHETRLVEID-NGKQREFESRLADALQE--LRAQHEDQVEQ 159
Cdd:COG3206 93 RPVLERVVDKLNLDEDPLGEEASREAAIERLRKnltVEPVKGSNVIEISyTSPDPELAAAVANALAEayLEQNLELRREE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 160 YKKELE------KTYSAKLDNARQSAE--RNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARE 231
Cdd:COG3206 173 ARKALEfleeqlPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2243207293 232 RDTSRRLLAekEREMAEMRARMQQQLDEYQELL--------DIKlALDMEIHAYRKLLEGEEERLRLS 291
Cdd:COG3206 253 PDALPELLQ--SPVIQQLRAQLAELEAELAELSarytpnhpDVI-ALRAQIAALRAQLQQEAQRILAS 317
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
10-262 |
5.44e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 10 LEPDAEAMVDGNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQD-EM 88
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEaEA 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 89 LRR----------VDAENRLQTMkEELDFQKNIYSEELRETKRRHETRLVEIDNGKQ-REFESRL------ADALQELRA 151
Cdd:PRK02224 448 LLEagkcpecgqpVEGSPHVETI-EEDRERVEELEAELEDLEEEVEEVEERLERAEDlVEAEDRIerleerREDLEELIA 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 152 QHEDQVEQYKKELE--KTYSAKLDNARQSAERNSNlvgAAHEELQQSRIRIDSLSAQLSQLQKQLAAkeakLRDLEDSLA 229
Cdd:PRK02224 527 ERRETIEEKRERAEelRERAAELEAEAEEKREAAA---EAEEEAEEAREEVAELNSKLAELKERIES----LERIRTLLA 599
|
250 260 270
....*....|....*....|....*....|....*
gi 2243207293 230 RERDTSRRL--LAEKEREMAEMRARMQQQLDEYQE 262
Cdd:PRK02224 600 AIADAEDEIerLREKREALAELNDERRERLAEKRE 634
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
31-291 |
7.16e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 31 AQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELdfqkn 110
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL----- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 111 iysEELRETKRRHETRLveiDNGKQREFESRLADA---------------LQELRAQHEDQVEQYKKELEKTYSAK---- 171
Cdd:PRK02224 436 ---RTARERVEEAEALL---EAGKCPECGQPVEGSphvetieedrerveeLEAELEDLEEEVEEVEERLERAEDLVeaed 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 172 -LDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTsrrlLAEKEREMAEMR 250
Cdd:PRK02224 510 rIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE----VAELNSKLAELK 585
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2243207293 251 ARMqQQLDEYQELLDIKLALDMEIHAYRKLLEG-----EEERLRLS 291
Cdd:PRK02224 586 ERI-ESLERIRTLLAAIADAEDEIERLREKREAlaelnDERRERLA 630
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
11-263 |
9.11e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 9.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 11 EPDAEAMVDGNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQdemlr 90
Cdd:PRK02224 306 DADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVE----- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 91 rvDAENRLqtmkEELDfqkniysEELRETKRRHETRLVEIDNgkqrefesrLADALQELRAQHEDQVEQykkelEKTYSA 170
Cdd:PRK02224 381 --DRREEI----EELE-------EEIEELRERFGDAPVDLGN---------AEDFLEELREERDELRER-----EAELEA 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 171 KLDNARQSAERNSNLV-------------GAAH-EELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLED---------S 227
Cdd:PRK02224 434 TLRTARERVEEAEALLeagkcpecgqpveGSPHvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDlveaedrieR 513
|
250 260 270
....*....|....*....|....*....|....*.
gi 2243207293 228 LARERDTSRRLLAEKEREMAEMRARMQQQLDEYQEL 263
Cdd:PRK02224 514 LEERREDLEELIAERRETIEEKRERAEELRERAAEL 549
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
39-317 |
1.76e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 39 EALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRE 118
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 119 TKR--RHETRLVEIDNGKQ-REFESRLaDALQELRAQHEDQVEQYKKELEKtysakLDNARQSAERNSNLVGAAHEELQQ 195
Cdd:COG3883 95 LYRsgGSVSYLDVLLGSESfSDFLDRL-SALSKIADADADLLEELKADKAE-----LEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 196 SRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIH 275
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2243207293 276 AYRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQTQGGGSVT 317
Cdd:COG3883 249 AGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAG 290
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
25-256 |
1.91e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 25 EGDLIAAQARLKDL--EALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQ--DEMLRRVDAENRLQT 100
Cdd:COG3206 188 RKELEEAEAALEEFrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGsgPDALPELLQSPVIQQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 101 MKEELdfqkniyseelretkrrhetrlveidngkqREFESRLADALQELRAQHEDqVEQYKKELEKTysakldnARQSAE 180
Cdd:COG3206 268 LRAQL------------------------------AELEAELAELSARYTPNHPD-VIALRAQIAAL-------RAQLQQ 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2243207293 181 RNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQ---LAAKEAKLRDLEdslaRERDTSRRLLAEKEREMAEMRARMQQQ 256
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQAQLAQLEARlaeLPELEAELRRLE----REVEVARELYESLLQRLEEARLAEALT 384
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
28-190 |
2.81e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 28 LIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQ-----LQDEM----LRRVDAENRL 98
Cdd:COG1579 33 LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyeaLQKEIeslkRRISDLEDEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 99 QTMKEELDFQKniysEELRETKRRHETRLVEIDNgKQREFESRLADaLQELRAQHEDQVEQYKKELEKTYSAKLDNARqs 178
Cdd:COG1579 113 LELMERIEELE----EELAELEAELAELEAELEE-KKAELDEELAE-LEAELEELEAEREELAAKIPPELLALYERIR-- 184
|
170
....*....|..
gi 2243207293 179 aeRNSNLVGAAH 190
Cdd:COG1579 185 --KRKNGLAVVP 194
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
131-289 |
2.86e-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: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 131 DNGKQREFESRLADALQELRAQHEDQVEQYKKELEkTYSAKLDNARQSAERNSNL--VGAAHEELQQSRIRIDSL---SA 205
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLAEYSWDEidVASAEREIAELEAELERLdasSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 206 QLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEReMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEE 285
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ-AEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVE 764
|
....
gi 2243207293 286 ERLR 289
Cdd:COG4913 765 RELR 768
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
25-282 |
3.14e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 25 EGDLIAA-QARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAA--LGEAKKQLQDEMLRRVDAENR-LQT 100
Cdd:PRK03918 450 RKELLEEyTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAeqLKELEEKLKKYNLEELEKKAEeYEK 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 101 MKEELDFQKNIYSEELRETKRRHE--TRLVEIDNgKQREFESRLADALQELRA---QHEDQVEQYKKELEKTYSA--KLD 173
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEKLEElkKKLAELEK-KLDELEEELAELLKELEElgfESVEELEERLKELEPFYNEylELK 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 174 NARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTsrrllaEKEREMAEMRARM 253
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYL------ELSRELAGLRAEL 682
|
250 260 270
....*....|....*....|....*....|..
gi 2243207293 254 QQ---QLDEYQELLDIKLALDMEIHAYRKLLE 282
Cdd:PRK03918 683 EElekRREEIKKTLEKLKEELEEREKAKKELE 714
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
62-263 |
3.32e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 62 ELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELdfqkniysEELRETKRRHETRLVEIDNgKQREFESR 141
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEL--------EDLEKEIKRLELEIEEVEA-RIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 142 LAdalqelRAQHEDQVEQYKKELEKtysakLDNARQSAErnsnlvgaahEELQQSRIRIDSLSAQLSQLQKQLAAKEAKL 221
Cdd:COG1579 82 LG------NVRNNKEYEALQKEIES-----LKRRISDLE----------DEILELMERIEELEEELAELEAELAELEAEL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2243207293 222 RDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQL-DEYQEL 263
Cdd:COG1579 141 EEKKAELDEELAELEAELEELEAEREELAAKIPPELlALYERI 183
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
40-249 |
3.58e-06 |
|
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: 50.34 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 40 ALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQdeMLRRV----------DAENRLQTMKEELDFqk 109
Cdd:COG3096 829 AFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQ--LLNKLlpqanlladeTLADRLEELREELDA-- 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 110 niySEELRETKRRHETRLVEIDngkqrefesRLADALQELRAQHEDQVEQYK--KELEKTYSAKLDNARQSAERNSNLVG 187
Cdd:COG3096 905 ---AQEAQAFIQQHGKALAQLE---------PLVAVLQSDPEQFEQLQADYLqaKEQQRRLKQQIFALSEVVQRRPHFSY 972
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2243207293 188 A-AHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLED----------SLARERDTSRRLLAEKEREMAEM 249
Cdd:COG3096 973 EdAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAqysqynqvlaSLKSSRDAKQQTLQELEQELEEL 1045
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
12-267 |
3.99e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.91 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 12 PDAEAMVDGNTKKEgdliaAQARLKDL--EALLNSKEAALSTALSEkrTLegelhDLRGQVAKLEAALGEAKKQLQDeml 89
Cdd:PRK11281 27 ARAASNGDLPTEAD-----VQAQLDALnkQKLLEAEDKLVQQDLEQ--TL-----ALLDKIDRQKEETEQLKQQLAQ--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 90 rrvdAENRLQTMKEELDFQKNIYSEELRETkrrhetrlveIDNGKQREFESRLADALQELraqhedqvEQYKKELEkTYS 169
Cdd:PRK11281 92 ----APAKLRQAQAELEALKDDNDEETRET----------LSTLSLRQLESRLAQTLDQL--------QNAQNDLA-EYN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 170 AKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSA--------QLSQLQKQLAAKEAKLrDLEDSLARERDTSRRLLAE 241
Cdd:PRK11281 149 SQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVggkalrpsQRVLLQAEQALLNAQN-DLQRKSLEGNTQLQDLLQK 227
|
250 260
....*....|....*....|....*.
gi 2243207293 242 KEREMAEMRARMQQQLDEYQELLDIK 267
Cdd:PRK11281 228 QRDYLTARIQRLEHQLQLLQEAINSK 253
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
21-264 |
5.33e-06 |
|
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: 49.40 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 21 NTKKEGDLIAAQARLKDleallnsKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQlqdemlrRVDAENRLQT 100
Cdd:pfam01576 238 LAKKEEELQAALARLEE-------ETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQ-------RRDLGEELEA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 101 MKEELD--FQKNIYSEELReTKRRHETRLVEidngKQREFESRLADA-LQELRAQHEDQVEQYKKELEKTYSAK--LDNA 175
Cdd:pfam01576 304 LKTELEdtLDTTAAQQELR-SKREQEVTELK----KALEEETRSHEAqLQEMRQKHTQALEELTEQLEQAKRNKanLEKA 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 176 RQSAERNSNLVGAAHEELQQSRI----RIDSLSAQLSQLQKQLAAKEAKLRDLEDSLAR---ERDTSRRLLAEKERE--- 245
Cdd:pfam01576 379 KQALESENAELQAELRTLQQAKQdsehKRKKLEGQLQELQARLSESERQRAELAEKLSKlqsELESVSSLLNEAEGKnik 458
|
250
....*....|....*....
gi 2243207293 246 MAEMRARMQQQLDEYQELL 264
Cdd:pfam01576 459 LSKDVSSLESQLQDTQELL 477
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
21-220 |
5.56e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 21 NTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALgeakkQLQDEMLRRVDAENRLQT 100
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 101 MKEELdfqkniysEELRETKRRHETRLVEIDNGKQ--REFESRLADALQELRAQHEDQVEQYKKELEktysaKLDNARQS 178
Cdd:COG4717 144 LPERL--------EELEERLEELRELEEELEELEAelAELQEELEELLEQLSLATEEELQDLAEELE-----ELQQRLAE 210
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2243207293 179 AErnsnlvgaahEELQQSRIRIDSLSAQLSQLQKQLAAKEAK 220
Cdd:COG4717 211 LE----------EELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
23-290 |
6.46e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 23 KKEGDLIAAQARLKDLEAL---LNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQD--EMLRRVDAENR 97
Cdd:PRK03918 218 ELREELEKLEKEVKELEELkeeIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 98 LQTMKEELDFQKN-------IYSEELRETKRR------HETRLVEIDNgKQREFESRL------ADALQELRAQhEDQVE 158
Cdd:PRK03918 298 LSEFYEEYLDELReiekrlsRLEEEINGIEERikeleeKEERLEELKK-KLKELEKRLeeleerHELYEEAKAK-KEELE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 159 QYKKELEKTYSAKLDNARQSAERnsnlvgaAHEELQQsriRIDSLSAQLSQLQKQLAAKEAKLRDLEdSLARERDTSRRL 238
Cdd:PRK03918 376 RLKKRLTGLTPEKLEKELEELEK-------AKEEIEE---EISKITARIGELKKEIKELKKAIEELK-KAKGKCPVCGRE 444
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2243207293 239 LAEKERE--MAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRL 290
Cdd:PRK03918 445 LTEEHRKelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
90-349 |
7.62e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 7.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 90 RRVDAENRLQTMKEELDFQKNI-----------------------YSEELRET-------------KRRHETRLVEIDNG 133
Cdd:TIGR02168 173 RRKETERKLERTRENLDRLEDIlnelerqlkslerqaekaerykeLKAELRELelallvlrleelrEELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 134 KQREFESRLADALQELRAQHEDQVEQYKKELEKtYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQ 213
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEE-LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 214 LAAKEAKLRDLE----------DSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEG 283
Cdd:TIGR02168 332 LDELAEELAELEekleelkeelESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2243207293 284 EEERLRLSPSPTSQRSRgRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEE 349
Cdd:TIGR02168 412 LEDRRERLQQEIEELLK-KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
54-288 |
8.43e-06 |
|
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: 48.91 E-value: 8.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 54 SEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAEnRLQTMKEELdfQKNIYSEELREtKRRHETRLVEIDNg 133
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEK--REYEGYELLKE-KEALERQKEAIER- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 134 kqrefesRLADALQELraqheDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGaahEELQQSRIRIDSLSAQLSQL--- 210
Cdd:TIGR02169 245 -------QLASLEEEL-----EKLTEEISELEKRLEEIEQLLEELNKKIKDLGE---EEQLRVKEKIGELEAEIASLers 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 211 -------QKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEG 283
Cdd:TIGR02169 310 iaekereLEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
....*
gi 2243207293 284 EEERL 288
Cdd:TIGR02169 390 YREKL 394
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
33-289 |
1.40e-05 |
|
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: 48.25 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 33 ARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEE---LDFQK 109
Cdd:pfam01576 68 ARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDillLEDQN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 110 NIYSEElretKRRHETRLVEIDNGKQREFESrlADALQELRAQHEDQVEQYKKELEKTysaklDNARQSAERNSNLVGAA 189
Cdd:pfam01576 148 SKLSKE----RKLLEERISEFTSNLAEEEEK--AKSLSKLKNKHEAMISDLEERLKKE-----EKGRQELEKAKRKLEGE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 190 HEELQQsriRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERdTSRRLLAEKEREmaemrarMQQQLDEYQELLDIKLA 269
Cdd:pfam01576 217 STDLQE---QIAELQAQIAELRAQLAKKEEELQAALARLEEET-AQKNNALKKIRE-------LEAQISELQEDLESERA 285
|
250 260
....*....|....*....|
gi 2243207293 270 LDMEIHAYRKLLEGEEERLR 289
Cdd:pfam01576 286 ARNKAEKQRRDLGEELEALK 305
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
56-289 |
3.11e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 56 KRTLEGELHDLRGQVAKLEAALGEAKKQLQDemlrrvdAENRLQTMKEeldfQKNIYSeeLRETKRRHETRLVEIdngkq 135
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEE-------AEAALEEFRQ----KNGLVD--LSEEAKLLLQQLSEL----- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 136 refESRLADAlQELRAQHEDQVEQYKKELEKTYSAkldnarQSAERNSNLVGAAHEELQQSRIRIDSLSAQLS------- 208
Cdd:COG3206 225 ---ESQLAEA-RAELAEAEARLAALRAQLGSGPDA------LPELLQSPVIQQLRAQLAELEAELAELSARYTpnhpdvi 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 209 QLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERL 288
Cdd:COG3206 295 ALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRL 374
|
.
gi 2243207293 289 R 289
Cdd:COG3206 375 E 375
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
27-246 |
4.17e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 27 DLIAAQARLKDLEALLNSkeAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDemlrrvdAENRLQTMKEELD 106
Cdd:COG4913 263 RYAAARERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDA-------LREELDELEAQIR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 107 FQKNIYSEELRETKRRHETRLVEIdngkQREFEsRLADALQELRAQHEDQVEQYKkelektysAKLDNARQSAERNSNLV 186
Cdd:COG4913 334 GNGGDRLEQLEREIERLERELEER----ERRRA-RLEALLAALGLPLPASAEEFA--------ALRAEAAALLEALEEEL 400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 187 GAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREM 246
Cdd:COG4913 401 EALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
54-252 |
4.89e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 54 SEKRTLEGELHDLRGQVAKLEAALGEAKKQLQD--EMLRRVDA-ENRLQTMKEELDFQKNIYsEELRETKRRHETRLVEI 130
Cdd:COG1340 78 EERDELNEKLNELREELDELRKELAELNKAGGSidKLRKEIERlEWRQQTEVLSPEEEKELV-EKIKELEKELEKAKKAL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 131 DNGKQREFESRLADALQELRAQHEDQVEQYKKELEKtYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQL 210
Cdd:COG1340 157 EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQE-LHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIEL 235
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2243207293 211 QKqlaakeaKLRDLEDSLARERDTSRRLLAEKEREMAEMRAR 252
Cdd:COG1340 236 QK-------ELRELRKELKKLRKKQRALKREKEKEELEEKAE 270
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
29-226 |
5.46e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 29 IAAQARLKDLEALLNSKEAALStalsEKRTLEGELHDLRGQVAKLEAALGEAKKQLqdEMLRRVDAENRLQTMKEELDFQ 108
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREEL--EKLEKLLQLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 109 KNIYSEELRETKRRHEtrlveidngkqrefesRLADALQELRAQhEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGA 188
Cdd:COG4717 141 LAELPERLEELEERLE----------------ELRELEEELEEL-EAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190
....*....|....*....|....*....|....*...
gi 2243207293 189 AHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLED 226
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
197-289 |
7.72e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.84 E-value: 7.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 197 RIRIDSLSAQLSQLQKQLAA----KEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALD- 271
Cdd:COG0542 403 RMEIDSKPEELDELERRLEQleieKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEq 482
|
90 100
....*....|....*....|
gi 2243207293 272 --MEIHAYRKLLEGEEERLR 289
Cdd:COG0542 483 ryGKIPELEKELAELEEELA 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
14-263 |
8.78e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 8.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 14 AEAMVDGNTKKEGDLIAAQARLKD-----LEALLNSKEAALstALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEM 88
Cdd:COG1196 545 AAALQNIVVEDDEVAAAAIEYLKAakagrATFLPLDKIRAR--AALAAALARGAIGAAVDLVASDLREADARYYVLGDTL 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 89 LRRVDAENRLQTMKEELDfqkniySEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTY 168
Cdd:COG1196 623 LGRTLVAARLEAALRRAV------TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELE 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 169 SAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDtsrrlLAEKEREMAE 248
Cdd:COG1196 697 EALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD-----LEELERELER 771
|
250 260
....*....|....*....|..
gi 2243207293 249 MRARMQQ-------QLDEYQEL 263
Cdd:COG1196 772 LEREIEAlgpvnllAIEEYEEL 793
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
33-258 |
1.01e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 44.67 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 33 ARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDE---MLRRVDA-ENRLQTMKE---EL 105
Cdd:pfam19220 188 AELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAErasLRMKLEAlTARAAATEQllaEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 106 DFQKNIYSEELRETKRRHETRLVEIDNgkqreFESRLAdalqELRAQHEDQVEQYKKelektysakLDNARQSAERNSNL 185
Cdd:pfam19220 268 RNQLRDRDEAIRAAERRLKEASIERDT-----LERRLA----GLEADLERRTQQFQE---------MQRARAELEERAEM 329
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2243207293 186 VG---AAHE-ELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDledslarerdTSRRLLAEKEREMAEmRARMQQQLD 258
Cdd:pfam19220 330 LTkalAAKDaALERAEERIASLSDRIAELTKRFEVERAALEQ----------ANRRLKEELQRERAE-RALAQGALE 395
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
23-288 |
1.14e-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: 45.17 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 23 KKEGDLIAAQARLKDLE----------ALLNSKEAALSTALSEkrtLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRV 92
Cdd:pfam01576 409 KLEGQLQELQARLSESErqraelaeklSKLQSELESVSSLLNE---AEGKNIKLSKDVSSLESQLQDTQELLQEETRQKL 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 93 DAENRLQTMKEEldfqKNIYSEELRE--TKRRHETRLVEIDNGKQREFESRLADALQELraqheDQVEQYKKELEKtysa 170
Cdd:pfam01576 486 NLSTRLRQLEDE----RNSLQEQLEEeeEAKRNVERQLSTLQAQLSDMKKKLEEDAGTL-----EALEEGKKRLQR---- 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 171 KLDNARQSAERNSnlvgAAHEELQQSRIR----IDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREM 246
Cdd:pfam01576 553 ELEALTQQLEEKA----AAYDKLEKTKNRlqqeLDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAE 628
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2243207293 247 AEMRARMQQQLDEYQELLDIKLALDmEIHAYRKLLEGEEERL 288
Cdd:pfam01576 629 AEAREKETRALSLARALEEALEAKE-ELERTNKQLRAEMEDL 669
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
67-354 |
1.30e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.73 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 67 RGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKE----ELDFQKNIYSEELR---ETKR-----RHETRLVEIDNGK 134
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKarqaEMDRQAAIYAEQERmamEREReleriRQEERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 135 QREFESRLAD--ALQELRAQHEDQVEQYKKELEKTYSAKLdnarQSAERnsnlvgaaHEELQQSRIRIDSLSAQlsqlqk 212
Cdd:pfam17380 367 QEEIAMEISRmrELERLQMERQQKNERVRQELEAARKVKI----LEEER--------QRKIQQQKVEMEQIRAE------ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 213 QLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRA----RMQQQLDEYQELLDIKLA-------LDMEIHAYRKLL 281
Cdd:pfam17380 429 QEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQqeeeRKRKKLELEKEKRDRKRAeeqrrkiLEKELEERKQAM 508
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2243207293 282 EGEEERLRLSPSPTSQRSRGRASSHSSQTqgggSVTKKRKLESTESRSSFSQHAR--TSGRVAVEEVDEEGKFVR 354
Cdd:pfam17380 509 IEEERKRKLLEKEMEERQKAIYEEERRRE----AEEERRKQQEMEERRRIQEQMRkaTEERSRLEAMEREREMMR 579
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
46-305 |
1.73e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 46 EAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQ--DEMLRRVD--AENRLQTMKEELDFQkniySEELRETKR 121
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSalNRLLPRLNllADETLADRVEEIREQ----LDEAEEAKR 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 122 ---RHETRLVEIDngkqrefesRLADALQELRAQHeDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRI 198
Cdd:PRK04863 912 fvqQHGNALAQLE---------PIVSVLQSDPEQF-EQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLA 981
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 199 RIDSLSAQLSQLQKQLAAKEAKLRD-LEDSLARERDTSRRLLAEKERemaemRARMQQQLDEY-QELLDIKLALDmeiha 276
Cdd:PRK04863 982 KNSDLNEKLRQRLEQAEQERTRAREqLRQAQAQLAQYNQVLASLKSS-----YDAKRQMLQELkQELQDLGVPAD----- 1051
|
250 260 270
....*....|....*....|....*....|..
gi 2243207293 277 yrkllEGEEERLRLSPSPTSQR---SRGRASS 305
Cdd:PRK04863 1052 -----SGAEERARARRDELHARlsaNRSRRNQ 1078
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
25-179 |
1.95e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 25 EGDLIAAQARLKDLEALLNSKEAALSTALSEKRTL--EGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMK 102
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALR 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 103 EELDFQKNIYSEELRETKRRHETRLVEIdNGKQREFESRLADA------LQELRAQHEDQVEQYKKELEKTYSAKLDNAR 176
Cdd:COG3206 305 AQLQQEAQRILASLEAELEALQAREASL-QAQLAQLEARLAELpeleaeLRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
...
gi 2243207293 177 QSA 179
Cdd:COG3206 384 TVG 386
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
74-263 |
1.95e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 74 EAALGEAKKQLQDEMLRR------VDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQ 147
Cdd:COG4717 306 ELQALPALEELEEEELEEllaalgLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 148 ELRAQHEdQVEQYKKELEK--TYSAKLDNARQSAERNSNLVGAA--HEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRD 223
Cdd:COG4717 386 ELRAALE-QAEEYQELKEEleELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2243207293 224 LEDSlarerdtsrRLLAEKEREMAEMRARMQQQLDEYQEL 263
Cdd:COG4717 465 LEED---------GELAELLQELEELKAELRELAEEWAAL 495
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
30-262 |
1.96e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 44.36 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 30 AAQARLKDLEALLNSKEAALSTALSEKRTLEGElhdlrgQVAKLEAALGEAKKQLQDEMLRRVDAENRL-QTMKEELDFQ 108
Cdd:pfam09731 129 ALEEVLKEAISKAESATAVAKEAKDDAIQAVKA------HTDSLKEASDTAEISREKATDSALQKAEALaEKLKEVINLA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 109 KNIYSEELRETK-RRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVE----QYKKELEKTY-----SAKLDNARQS 178
Cdd:pfam09731 203 KQSEEEAAPPLLdAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVAseriVFQQELVSIFpdiipVLKEDNLLSN 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 179 AERNSnLVGAAHEELQQSRIRIDSLSAQLSQ-LQKQLAAKEAKLRDLEDSLARE-----RDTSRRLLAEKEREMAEMRAR 252
Cdd:pfam09731 283 DDLNS-LIAHAHREIDQLSKKLAELKKREEKhIERALEKQKEELDKLAEELSARleevrAADEAQLRLEFEREREEIRES 361
|
250
....*....|
gi 2243207293 253 MQQQLDEYQE 262
Cdd:pfam09731 362 YEEKLRTELE 371
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
37-288 |
2.12e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 37 DLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEML--RRVDAENRLQTMKEELDFQKNIYSE 114
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVcgRELTEEHRKELLEEYTAELKRIEKE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 115 --ELRETKRRHETRLVEIDNGKQREfesrladalQELRAQHE--DQVEQYKKELEKTYSAKLdnarqsaERNSNLVGAAH 190
Cdd:PRK03918 468 lkEIEEKERKLRKELRELEKVLKKE---------SELIKLKElaEQLKELEEKLKKYNLEEL-------EKKAEEYEKLK 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 191 EELQQSRIRIDSLSAQLSQLQ---KQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIK 267
Cdd:PRK03918 532 EKLIKLKGEIKSLKKELEKLEelkKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAE 611
|
250 260
....*....|....*....|.
gi 2243207293 268 laldMEIHAYRKLLEGEEERL 288
Cdd:PRK03918 612 ----KELEREEKELKKLEEEL 628
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
58-289 |
2.17e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 58 TLEGELHDLRGQV--AKLEAALGEAKKQLQDEMLRRVDAEnrlqtmKEELDFQKNIYSEELRETKRR-HE-TRLVEIDNG 133
Cdd:TIGR02169 643 TLEGELFEKSGAMtgGSRAPRGGILFSRSEPAELQRLRER------LEGLKRELSSLQSELRRIENRlDElSQELSDASR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 134 KQREFESRLADALQELRAQHEdQVEQYKKELEKTySAKLDNARQSaernsnlvgaaheelqqsrirIDSLSAQLSQLQKQ 213
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKE-RLEELEEDLSSL-EQEIENVKSE---------------------LKELEARIEELEED 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 214 LAAKEAKLRDLEDSLARER-DTSRRLLAEKEREMAEMRARMQ-------------QQL-DEYQELLDIKLALDMEIHAYR 278
Cdd:TIGR02169 774 LHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLReieqklnrltlekEYLeKEIQELQEQRIDLKEQIKSIE 853
|
250
....*....|.
gi 2243207293 279 KLLEGEEERLR 289
Cdd:TIGR02169 854 KEIENLNGKKE 864
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
30-250 |
2.64e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 30 AAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRG--------------QVAKLEAALGEAKKQLqDEMLRRV--- 92
Cdd:pfam10174 349 ALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDmldvkerkinvlqkKIENLQEQLRDKDKQL-AGLKERVksl 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 93 --DAENR---LQTMKEELDFQKNIYsEELRETKRRHE-TRLVEIDNGKQrefesRLADALQELRAQHEDQVEQYKKELEK 166
Cdd:pfam10174 428 qtDSSNTdtaLTTLEEALSEKERII-ERLKEQREREDrERLEELESLKK-----ENKDLKEKVSALQPELTEKESSLIDL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 167 TYSAKldNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEA------KLRDLEDSLARERDTSRRLLA 240
Cdd:pfam10174 502 KEHAS--SLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTnpeindRIRLLEQEVARYKEESGKAQA 579
|
250
....*....|
gi 2243207293 241 EKEREMAEMR 250
Cdd:pfam10174 580 EVERLLGILR 589
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
154-272 |
2.87e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 43.30 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 154 EDQVEQYKKELEKTYsAKLDNARQsaernsnlvgaAHEELQQSRIRID------SLSAQLSQLQKQLAAKEAKLRDLEDS 227
Cdd:COG3524 176 EDAVRFAEEEVERAE-ERLRDARE-----------ALLAFRNRNGILDpeataeALLQLIATLEGQLAELEAELAALRSY 243
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2243207293 228 L---ARERDTSRRLLAEKEREMAEMRARM---------QQQLDEYQEL-LDIKLALDM 272
Cdd:COG3524 244 LspnSPQVRQLRRRIAALEKQIAAERARLtgasggdslASLLAEYERLeLEREFAEKA 301
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
81-285 |
3.48e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 81 KKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSE------ELRETKRRHETRLVEID------NGKQREFESRLAD--AL 146
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVLREINEisselpELREELEKLEKEVKELEelkeeiEELEKELESLEGSkrKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 147 QELRAQHEDQVEQYKKELEKTYS--AKLDNARQSAERNSNLVgaahEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDL 224
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEkvKELKELKEKAEEYIKLS----EFYEEYLDELREIEKRLSRLEEEINGIEERIKEL 333
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2243207293 225 EDSLARERDTSRRlLAEKEREMAEmrarmqqqLDEYQELLDIKLALDMEIHAYRKLLEGEE 285
Cdd:PRK03918 334 EEKEERLEELKKK-LKELEKRLEE--------LEERHELYEEAKAKKEELERLKKRLTGLT 385
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
146-291 |
3.82e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 146 LQELRAQHEDQVEQYKKELEKTYSAK---LDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLR 222
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKpelNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2243207293 223 DLEDSLARERDTSRRllAEKEREMAEMRARMQ---QQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLS 291
Cdd:COG4717 120 KLEKLLQLLPLYQEL--EALEAELAELPERLEeleERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
33-289 |
4.91e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 33 ARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKqlqdemLRRVDAENRLQTMKEELDFQKniY 112
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE------LKEEIEELEKELESLEGSKRK--L 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 113 SEELRETKRRHETRLVEIdngkqREFESRLAD--ALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSnlVGAAH 190
Cdd:PRK03918 258 EEKIRELEERIEELKKEI-----EELEEKVKElkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING--IEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 191 EELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARErDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLAl 270
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK-EELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS- 408
|
250
....*....|....*....
gi 2243207293 271 dmEIHAYRKLLEGEEERLR 289
Cdd:PRK03918 409 --KITARIGELKKEIKELK 425
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
30-181 |
6.12e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 30 AAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLqdemlrrVDAENRLQTMKEELDFQK 109
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL-------AQLELRLEGLEVRIDNLQ 942
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2243207293 110 NIYSEELRETKRRHETRLVEIDNG--KQREFESRLADALQELRAQHEDQVEQYKKELE-----KTYSAKLDNARQSAER 181
Cdd:TIGR02168 943 ERLSEEYSLTLEEAEALENKIEDDeeEARRRLKRLENKIKELGPVNLAAIEEYEELKErydflTAQKEDLTEAKETLEE 1021
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
27-349 |
7.37e-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: 42.41 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 27 DLIAAQAR---------LKDLEALLNSKEAALSTAlseKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENR 97
Cdd:pfam15921 302 EIIQEQARnqnsmymrqLSDLESTVSQLRSELREA---KRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 98 LQTMKEELDFQKNIYSEELRETKR---RHETRLVEIDNgKQREFESRLADaLQELRAQHEDQVEQYKKELEKTYSAkLDN 174
Cdd:pfam15921 379 LQKLLADLHKREKELSLEKEQNKRlwdRDTGNSITIDH-LRRELDDRNME-VQRLEALLKAMKSECQGQMERQMAA-IQG 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 175 ARQSAERNSNLVGaaheELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERdtsrRLLAEKEREMAEMRARMQ 254
Cdd:pfam15921 456 KNESLEKVSSLTA----QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKE----RAIEATNAEITKLRSRVD 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 255 QQLDEYQELldiklaldmeihayrkllEGEEERLRlspsptsqRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQH 334
Cdd:pfam15921 528 LKLQELQHL------------------KNEGDHLR--------NVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQH 581
|
330
....*....|....*
gi 2243207293 335 ARTSGRVAVEEVDEE 349
Cdd:pfam15921 582 GRTAGAMQVEKAQLE 596
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
142-250 |
7.88e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 142 LADALQELRAQhEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQS---RIRIDSLSAQLSQLQKQLAAKE 218
Cdd:PRK09039 79 LQDSVANLRAS-LSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSaraLAQVELLNQQIAALRRQLAALE 157
|
90 100 110
....*....|....*....|....*....|....*....
gi 2243207293 219 AKLRDLE----DSLARERDTSRRL---LAEKEREMAEMR 250
Cdd:PRK09039 158 AALDASEkrdrESQAKIADLGRRLnvaLAQRVQELNRYR 196
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
32-289 |
7.97e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 32 QARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLqDEMLRRVdaeNRLQTMKEELDFQKNI 111
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKR-DELNEKV---KELKEERDELNEKLNE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 112 YSEELRETKRRH-ETRLVEID-NGKQREFEsRLADALQ--ELRAQHEDQVEQYKKELEKtysaKLDNARQSAERNSNLVG 187
Cdd:COG1340 90 LREELDELRKELaELNKAGGSiDKLRKEIE-RLEWRQQteVLSPEEEKELVEKIKELEK----ELEKAKKALEKNEKLKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 188 AAhEELQQSRIRIDSLSAQLsqlqKQLAAKEAKLRDLEDSLARERDTSRrllaEKEREMAEMRARMQQQLDEYQELLDik 267
Cdd:COG1340 165 LR-AELKELRKEAEEIHKKI----KELAEEAQELHEEMIELYKEADELR----KEADELHKEIVEAQEKADELHEEII-- 233
|
250 260
....*....|....*....|..
gi 2243207293 268 lALDMEIHAYRKLLEGEEERLR 289
Cdd:COG1340 234 -ELQKELRELRKELKKLRKKQR 254
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
22-289 |
8.13e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 22 TKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAK------KQLQDEMLRRVDAE 95
Cdd:TIGR04523 148 KKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKkkiqknKSLESQISELKKQN 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 96 NRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDN------GKQREFE------SRLADALQELRAQHEDQVEQYKKE 163
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKikkqlsEKQKELEqnnkkiKELEKQLNQLKSEISDLNNQKEQD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 164 LEKTYSAKLDNARQSAERNSNlvgaaheELQQSRIRIDSLSAQLSQLQKQLAAKEAklrdledslarERDTSRRLLAEKE 243
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQN-------QISQNNKIISQLNEQISQLKKELTNSES-----------ENSEKQRELEEKQ 369
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2243207293 244 REMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLR 289
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK 415
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
28-166 |
8.35e-04 |
|
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: 41.06 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 28 LIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQD--EMLRRVDAENRLQTMKEEL 105
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeEQLGNVRNNKEYEALQKEI 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2243207293 106 DFQK---NIYSEELRETKRRHETRLVEIDNGKQRefESRLADALQELRAQHEDQVEQYKKELEK 166
Cdd:COG1579 99 ESLKrriSDLEDEILELMERIEELEEELAELEAE--LAELEAELEEKKAELDEELAELEAELEE 160
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
37-256 |
8.48e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.25 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 37 DLEALLNSKEAALSTALSEKRTLEGELHD-LRGQVAKLEAALGEAKKQLQDEMLRRVDAE-NRLQTMKEELDFQKNIYSE 114
Cdd:pfam15709 308 NMESEEERSEEDPSKALLEKREQEKASRDrLRAERAEMRRLEVERKRREQEEQRRLQQEQlERAEKMREELELEQQRRFE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 115 ELRETKRRHETrlveiDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNlvgaaheelq 194
Cdd:pfam15709 388 EIRLRKQRLEE-----ERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQ---------- 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2243207293 195 qsriRIDSLSAQLSQLQKQLA--AKEAKLRDLEDSlaRERDTSRRLLAEKEREMAEMRARMQQQ 256
Cdd:pfam15709 453 ----RQKELEMQLAEEQKRLMemAEEERLEYQRQK--QEAEEKARLEAEERRQKEEEAARLALE 510
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
70-288 |
1.06e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 70 VAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYS---------------EELRETKRRHETRLVEIDNGK 134
Cdd:PRK04863 437 ADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQlvrkiagevsrseawDVARELLRRLREQRHLAEQLQ 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 135 QREfeSRLADALQELRAQHedQVEQYKKELEKTYSAKLDNA---RQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQ 211
Cdd:PRK04863 517 QLR--MRLSELEQRLRQQQ--RAERLLAEFCKRLGKNLDDEdelEQLQEELEARLESLSESVSEARERRMALRQQLEQLQ 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 212 ---KQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEmrarMQQQLDEYQELldiKLALDmEIHAYRKLLEGEEERL 288
Cdd:PRK04863 593 ariQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEY----MQQLLEREREL---TVERD-ELAARKQALDEEIERL 664
|
|
| COG0610 |
COG0610 |
Type I site-specific restriction-modification system, R (restriction) subunit and related ... |
65-287 |
1.24e-03 |
|
Type I site-specific restriction-modification system, R (restriction) subunit and related helicases ... [Defense mechanisms];
Pssm-ID: 440375 [Multi-domain] Cd Length: 936 Bit Score: 41.78 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 65 DLRGQVAKLEAALGE-AKKQLQDEMLrrVDAENRLQTMKEELDFQKNIYSEElretkrrhetrlVEIDNGKQREFESRLA 143
Cdd:COG0610 648 DYRGIFENLKKALALySEEDGKEDVL--TDPEEALEELKEALDELRALFPEG------------VDFSAFDPTEKLEALD 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 144 DALQELRAQHEDQVEQYK--KELEKTYSAkldnARQSAErnsnLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAK--EA 219
Cdd:COG0610 714 EAVERFLGDEEARKEFKKlfKELSRLYNL----LSPDDE----FGDLELEKYRDDVSFYLALRAKLRKLGEKLDLKeyEE 785
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2243207293 220 KLRDL-EDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEER 287
Cdd:COG0610 786 KIRQLlDEAIDLERKEIKPRIKQNPVQYRKFSELLEEIIEEYNNGALDADEVLEELEELAKEVKEEEER 854
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
28-267 |
1.28e-03 |
|
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: 41.63 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 28 LIAAQARLKDLEALLNSKEAALSTALsekRTLEGELHDLRGQVAKLEAA-------LGEAKKQLQDEMLRRVDAENRLQT 100
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQELIFLL---QAREKEIHDLEIQLTAIKTSeehylkeVEDLKTELEKEKLKNIELTAHCDK 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 101 MKEELDFQKNIYSEELRETKRRHETRlveIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKT---YSAKLDNARQ 177
Cdd:pfam05483 497 LLLENKELTQEASDMTLELKKHQEDI---INCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKgdeVKCKLDKSEE 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 178 SAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQK---QLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQ 254
Cdd:pfam05483 574 NARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKnieELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFE 653
|
250
....*....|...
gi 2243207293 255 QQLDEYQELLDIK 267
Cdd:pfam05483 654 EIIDNYQKEIEDK 666
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-240 |
1.28e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 2 DLEAWDPHLEPDAEAMVDGNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAK 81
Cdd:COG1196 606 SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 82 KQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQyk 161
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE-- 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 162 kELEKtysaKLDNARQSAER--NSNLvgAAHEELQQSRIRIDSLSAQLSQLQKqlaAKEaKLRDLEDSLarERDTSRRLL 239
Cdd:COG1196 764 -ELER----ELERLEREIEAlgPVNL--LAIEEYEELEERYDFLSEQREDLEE---ARE-TLEEAIEEI--DRETRERFL 830
|
.
gi 2243207293 240 A 240
Cdd:COG1196 831 E 831
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
139-275 |
1.44e-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: 41.86 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 139 ESRLADALQELRAQH--EDQVEQYKKELEKTYSAKLD----NARQSAERNSNLVGAAheELQQSRIRIDSLSAQLSQLQK 212
Cdd:COG3096 518 RAQLAELEQRLRQQQnaERLLEEFCQRIGQQLDAAEEleelLAELEAQLEELEEQAA--EAVEQRSELRQQLEQLRARIK 595
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 213 QLAAKEAKLRDLEDSLARERDTSRRLLAEKeremAEMRARMQQQLD-------EYQELLDIKLALDMEIH 275
Cdd:COG3096 596 ELAARAPAWLAAQDALERLREQSGEALADS----QEVTAAMQQLLErereatvERDELAARKQALESQIE 661
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
113-289 |
1.47e-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: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 113 SEELRETKRRHETRLVEIDNGKQREfesRLADALQELRAqHEDQVEQYKKELEKTYS------------------AKLDN 174
Cdd:COG2433 312 KEDLSVEEKLHLAREYGYDNDHERD---ALAAALKAYDA-YKNKFERVEKKVPPDVDrdevkarvirglsieealEELIE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 175 ARQSAERNSNLVGAAHEElqqsrIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLlaekEREMAEMRARMQ 254
Cdd:COG2433 388 KELPEEEPEAEREKEHEE-----RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERL----ERELSEARSEER 458
|
170 180 190
....*....|....*....|....*....|....*
gi 2243207293 255 QQLDEYQELldikLALDMEIHAYRKLLEGEEERLR 289
Cdd:COG2433 459 REIRKDREI----SRLDREIERLERELEEERERIE 489
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
25-106 |
1.52e-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: 40.87 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 25 EGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEA-ALGEAKKQLQDEMLRRVDAENRLQTMKE 103
Cdd:TIGR04320 260 QAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAqALQTAQNNLATAQAALANAEARLAKAKE 339
|
...
gi 2243207293 104 ELD 106
Cdd:TIGR04320 340 ALA 342
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
203-264 |
1.65e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.10 E-value: 1.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2243207293 203 LSAQLSQLQKQLAAKEAKLRDLEDSLARERDT-SRRLLAEKEREMAEMRARMQQQLDEYQELL 264
Cdd:smart00935 23 LEKEFKKRQAELEKLEKELQKLKEKLQKDAATlSEAAREKKEKELQKKVQEFQRKQQKLQQDL 85
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
203-264 |
1.82e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 38.71 E-value: 1.82e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2243207293 203 LSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELL 264
Cdd:pfam03938 24 LEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQEL 85
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
199-265 |
1.85e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 1.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2243207293 199 RIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKER------EMAEMRARMQQQLDEYQELLD 265
Cdd:PRK09039 54 ALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRlqallaELAGAGAAAEGRAGELAQELD 126
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
23-253 |
2.28e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.98 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 23 KKEGDLIAAQARLKDLE---ALLNSKEAALSTALSE-KRTLEGELHDL-------RGQVAKLEAALGEAKKQLQDEmLRR 91
Cdd:pfam12128 608 KAEEALQSAREKQAAAEeqlVQANGELEKASREETFaRTALKNARLDLrrlfdekQSEKDKKNKALAERKDSANER-LNS 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 92 VDAEnrlqtmKEELDFQKNIYSEELRETKRRHET------RLVEIDNGKQREFESRLADALQELRAQHEDQVE-QYKKEL 164
Cdd:pfam12128 687 LEAQ------LKQLDKKHQAWLEEQKEQKREARTekqaywQVVEGALDAQLALLKAAIAARRSGAKAELKALEtWYKRDL 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 165 E----------------KTYSAKLDNARQ-SAERNSNLVGAAHEELQQS---RIRIDSLSAQLSQLQKQLAAKEAKLRDL 224
Cdd:pfam12128 761 AslgvdpdviaklkreiRTLERKIERIAVrRQEVLRYFDWYQETWLQRRprlATQLSNIERAISELQQQLARLIADTKLR 840
|
250 260
....*....|....*....|....*....
gi 2243207293 225 EDSLARERDTSRRLLAEKEREMAEMRARM 253
Cdd:pfam12128 841 RAKLEMERKASEKQQVRLSENLRGLRCEM 869
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
32-311 |
2.80e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 32 QARLKDLEALLNSKEAALSTALSEKRTLEGELHDLR-------GQVAKLEAALGEAKKQLQ-------DEMLRRVDAENR 97
Cdd:pfam01576 186 EAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQeqiaelqAQIAELRAQLAKKEEELQaalarleEETAQKNNALKK 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 98 LQTMKEEL-DFQKNIYSEELRETKRRHETR-LVEIDNGKQREFESRL--ADALQELRAQHEDQVEQYKKELE---KTYSA 170
Cdd:pfam01576 266 IRELEAQIsELQEDLESERAARNKAEKQRRdLGEELEALKTELEDTLdtTAAQQELRSKREQEVTELKKALEeetRSHEA 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 171 KLDNARQsaeRNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLlaekEREMAEMR 250
Cdd:pfam01576 346 QLQEMRQ---KHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKL----EGQLQELQ 418
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2243207293 251 ARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERlrlspsptSQRSRGRASSHSSQTQ 311
Cdd:pfam01576 419 ARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGK--------NIKLSKDVSSLESQLQ 471
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
141-290 |
3.04e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 141 RLADALQELRAQHEdQVEQYKKELEKtYSAKLDNARQsAERNSNLVGAAHEELQQSRIRIDSLSAQ---LSQLQKQLAAK 217
Cdd:COG4717 92 ELQEELEELEEELE-ELEAELEELRE-ELEKLEKLLQ-LLPLYQELEALEAELAELPERLEELEERleeLRELEEELEEL 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2243207293 218 EAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDiklALDMEIHAYRKLLEGEEERLRL 290
Cdd:COG4717 169 EAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE---EAQEELEELEEELEQLENELEA 238
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
27-265 |
3.24e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 27 DLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEE-L 105
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEkL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 106 DFQKNIysEELRETKRRHETRLVEID--NGKQREFESRLADaLQELRAQHEDQVEQYKKELEKTySAKLDNARQSAERNS 183
Cdd:TIGR04523 184 NIQKNI--DKIKNKLLKLELLLSNLKkkIQKNKSLESQISE-LKKQNNQLKDNIEKKQQEINEK-TTEISNTQTQLNQLK 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 184 NLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSlaRERDTSRRL---LAEKEREMAEmrarMQQQLDEY 260
Cdd:TIGR04523 260 DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ--KEQDWNKELkseLKNQEKKLEE----IQNQISQN 333
|
....*
gi 2243207293 261 QELLD 265
Cdd:TIGR04523 334 NKIIS 338
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
11-166 |
3.34e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 11 EPDAEAMVDgNTKKEgdliaAQARLKdlEALLNSKEAALStalsEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLR 90
Cdd:PRK12704 37 EEEAKRILE-EAKKE-----AEAIKK--EALLEAKEEIHK----LRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 91 RVDAENRLQTMKEELDFQKNIY---SEELRETKRRHETRLVEIDNGKQREFESRLADALQElRAQHEDQV------EQYK 161
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELekkEEELEELIEEQLQELERISGLTAEEAKEILLEKVEE-EARHEAAVlikeieEEAK 183
|
....*
gi 2243207293 162 KELEK 166
Cdd:PRK12704 184 EEADK 188
|
|
| LCD1 |
pfam09798 |
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. ... |
203-329 |
3.61e-03 |
|
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. In Schizosaccharomyces pombe this protein is called Rad26 and in Saccharomyces cerevisiae it is called LCD1.
Pssm-ID: 462906 Cd Length: 615 Bit Score: 39.99 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 203 LSAQLSQLQKQLAAKEAKLRDLEDSLARerdtsrrllaEKEREMAEMRArmqqqldEYQELLDIKLALDMEIhayRKLle 282
Cdd:pfam09798 2 LRDKLELLQQEKEKELEKLKNSYEELKS----------SHEEELEKLKQ-------EVQKLEDEKKFLLNEL---RSL-- 59
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2243207293 283 geeerlrLSPSPTSQRSRGRASSHSSQtqgggSVTKKRKLESTESRS 329
Cdd:pfam09798 60 -------SATSPASSQSHETDTDDSSS-----VSLKKRKIEESTAES 94
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
71-164 |
3.97e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 37.95 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 71 AKLEAALGEAKKQLQDEmlrrvdaENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELR 150
Cdd:smart00935 21 KQLEKEFKKRQAELEKL-------EKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEEL 93
|
90
....*....|....
gi 2243207293 151 AQHEDQVEQYKKEL 164
Cdd:smart00935 94 QKILDKINKAIKEV 107
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
158-326 |
4.41e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.04 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 158 EQYKKELEKTYSAKLDN------ARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARE 231
Cdd:PRK10929 26 KQITQELEQAKAAKTPAqaeiveALQSALNWLEERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 232 R------DTSRRLLaEKEREmaemrarMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSqrSRGRASS 305
Cdd:PRK10929 106 AleqeilQVSSQLL-EKSRQ-------AQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNT--PLAQAQL 175
|
170 180
....*....|....*....|.
gi 2243207293 306 HSSQTQgggSVTKKRKLESTE 326
Cdd:PRK10929 176 TALQAE---SAALKALVDELE 193
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
94-288 |
4.63e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 94 AENRLQTMKEELDFQKNIYSEELRETKrrhetrlvEIDNgKQREFESRLADALQELRaQHEDQVEQYKKELEKtysakld 173
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTE--------NIEE-LIKEKEKELEEVLREIN-EISSELPELREELEK------- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 174 narqsaernsnlVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRlLAEKEREMAEMRARM 253
Cdd:PRK03918 226 ------------LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKA 292
|
170 180 190
....*....|....*....|....*....|....*...
gi 2243207293 254 QQQL---DEYQELLDIKLALDMEIHAYRKLLEGEEERL 288
Cdd:PRK03918 293 EEYIklsEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
192-288 |
4.65e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 192 ELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLAR---ERDTSRRLLAEKEREMAEMRARM---QQQLD------E 259
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAaktELEDLEKEIKRLELEIEEVEARIkkyEEQLGnvrnnkE 90
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2243207293 260 YQELL--------------DIKLALDMEIHAYRKLLEGEEERL 288
Cdd:COG1579 91 YEALQkeieslkrrisdleDEILELMERIEELEEELAELEAEL 133
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
30-262 |
5.04e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 30 AAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQK 109
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE 1645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 110 NIYSEELRETKRRHETRLVEIdnGKQREFESRLADALQELRAQHEDQVEQYKKELEKtySAKLDNARQSAERNSNLVGAA 189
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEE--AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE--AKKAEELKKKEAEEKKKAEEL 1721
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2243207293 190 HEELQQSRIRIDSLSAQLSQLQKQlaAKEAKLRDLEDSLARERDTSRRLLAEKEREmaEMRARMQQQLDEYQE 262
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKK--AEEAKKDEEEKKKIAHLKKEEEKKAEEIRK--EKEAVIEEELDEEDE 1790
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
25-256 |
5.93e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 25 EGDLIAAQARLKDLEALLNS----------KEAALSTALSEKR----TLEGELHDLRGQVAKLEA------ALGEAKKQL 84
Cdd:PRK02224 432 EATLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEDRerveELEAELEDLEEEVEEVEErleraeDLVEAEDRI 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 85 QDEMLRRVDAENRLQTMKEELDfQKNIYSEELRETKRRHETRLVEID--------------------NGKQREFESRL-- 142
Cdd:PRK02224 512 ERLEERREDLEELIAERRETIE-EKRERAEELRERAAELEAEAEEKReaaaeaeeeaeeareevaelNSKLAELKERIes 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 143 --------------ADALQELRAQHEDQVEQYKKELEKtYSAKLDNARQSAERnsnLVGAAHEELQQSRIR--------- 199
Cdd:PRK02224 591 lerirtllaaiadaEDEIERLREKREALAELNDERRER-LAEKRERKRELEAE---FDEARIEEAREDKERaeeyleqve 666
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2243207293 200 --IDSLSAQLSQLQKQLAAKEAKLRDLEdSLARERDT--SRRLLAEKEREMAE--------MRARMQQQ 256
Cdd:PRK02224 667 ekLDELREERDDLQAEIGAVENELEELE-ELRERREAleNRVEALEALYDEAEelesmygdLRAELRQR 734
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
93-265 |
6.63e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 38.01 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 93 DAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEkTYSAKL 172
Cdd:pfam01442 4 DSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLE-PYTEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 173 -DNARQSAERNSNLVGAAHEELQQS-RIRIDSLSAQLSQLQKQLAAK-EAKLRDLEDSLARERDTSRRLLAEKERemaEM 249
Cdd:pfam01442 83 rKRLNADAEELQEKLAPYGEELRERlEQNVDALRARLAPYAEELRQKlAERLEELKESLAPYAEEVQAQLSQRLQ---EL 159
|
170
....*....|....*.
gi 2243207293 250 RARMQQQLDEYQELLD 265
Cdd:pfam01442 160 REKLEPQAEDLREKLD 175
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
202-287 |
6.75e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 38.79 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 202 SLSAQLSQLQKQLAAKEA---KLRDLEDSLARERDTSRRLLAEKEREMAEMR---ARMQQQLdeyqELLDIKL-ALDMEI 274
Cdd:PRK09039 78 DLQDSVANLRASLSAAEAersRLQALLAELAGAGAAAEGRAGELAQELDSEKqvsARALAQV----ELLNQQIaALRRQL 153
|
90
....*....|...
gi 2243207293 275 HAYRKLLEGEEER 287
Cdd:PRK09039 154 AALEAALDASEKR 166
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
28-290 |
6.80e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.57 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 28 LIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMK----- 102
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKlekih 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 103 -----------EELDFQKNIYSEELRETKRRHETRLVEIdNGKQREFESRLADALQELRA------------QHEDQVEQ 159
Cdd:TIGR00618 461 lqesaqslkerEQQLQTKEQIHLQETRKKAVVLARLLEL-QEEPCPLCGSCIHPNPARQDidnpgpltrrmqRGEQTYAQ 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 160 YKKELEKT-------------YSAKLDNARQS--------------------------------AERNSNLVGAAHEELQ 194
Cdd:TIGR00618 540 LETSEEDVyhqltserkqrasLKEQMQEIQQSfsiltqcdnrskedipnlqnitvrlqdlteklSEAEDMLACEQHALLR 619
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 195 QSRIRID--SLSAQLSQLQKQLAAKEAKLRDLEDSLA--RERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLAL 270
Cdd:TIGR00618 620 KLQPEQDlqDVRLHLQQCSQELALKLTALHALQLTLTqeRVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML 699
|
330 340
....*....|....*....|
gi 2243207293 271 DMEIHAYRKLLEGEEERLRL 290
Cdd:TIGR00618 700 AQCQTLLRELETHIEEYDRE 719
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
29-269 |
7.07e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.56 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 29 IAAQARLKDLEALlnSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDemlrrvdAENRLQTMKEELDFQ 108
Cdd:PRK04863 277 HANERRVHLEEAL--ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQA-------ASDHLNLVQTALRQQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 109 KNI--YSEELRETKRRHE--TRLVEIDNGKQREFESRLADALQE---LRAQHEDQVEQYkkELEKTYSAKLDNARQSAER 181
Cdd:PRK04863 348 EKIerYQADLEELEERLEeqNEVVEEADEQQEENEARAEAAEEEvdeLKSQLADYQQAL--DVQQTRAIQYQQAVQALER 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 182 NSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDslARERDTS-----RRLLAEKEREMA-------EM 249
Cdd:PRK04863 426 AKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQA--AHSQFEQayqlvRKIAGEVSRSEAwdvarelLR 503
|
250 260
....*....|....*....|
gi 2243207293 250 RARMQQQLDEYQELLDIKLA 269
Cdd:PRK04863 504 RLREQRHLAEQLQQLRMRLS 523
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
28-335 |
7.40e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.73 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 28 LIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELD- 106
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEe 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 107 -------FQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSA 179
Cdd:COG4372 113 lqeeleeLQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 180 ERNSnLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDE 259
Cdd:COG4372 193 NRNA-EKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2243207293 260 YQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHA 335
Cdd:COG4372 272 DTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLL 347
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
29-265 |
8.36e-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: 39.00 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 29 IAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQtmKEELDFQ 108
Cdd:pfam01576 127 VTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLK--KEEKGRQ 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 109 kniyseELRETKRRHETRLVEIdngkqREFESRLADALQELRAQ---HEDQVEQYKKELEKTYSAKlDNARQSAERNSNL 185
Cdd:pfam01576 205 ------ELEKAKRKLEGESTDL-----QEQIAELQAQIAELRAQlakKEEELQAALARLEEETAQK-NNALKKIRELEAQ 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 186 VGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLA--------RERDTS--RRLLAEK----EREMAEMRA 251
Cdd:pfam01576 273 ISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAaqqelrskREQEVTelKKALEEEtrshEAQLQEMRQ 352
|
250
....*....|....
gi 2243207293 252 RMQQQLDEYQELLD 265
Cdd:pfam01576 353 KHTQALEELTEQLE 366
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
58-209 |
8.84e-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: 39.17 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 58 TLEGELHDLRGQVAKLEAALgEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRE-TKRRHETR--LVEIdNGK 134
Cdd:COG3096 516 QLRAQLAELEQRLRQQQNAE-RLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEaVEQRSELRqqLEQL-RAR 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243207293 135 QREFESR------LADALQELRAQHEDQVEQykkelektySAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLS 208
Cdd:COG3096 594 IKELAARapawlaAQDALERLREQSGEALAD---------SQEVTAAMQQLLEREREATVERDELAARKQALESQIERLS 664
|
.
gi 2243207293 209 Q 209
Cdd:COG3096 665 Q 665
|
|
| |
