|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
48-305 |
2.43e-70 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 226.73 E-value: 2.43e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 48 AAQARLKDL-EALLNSKEAALSTALSEKRTLEGELHDLRGQVAKL--------------EAALGEAKKQLQDEMLRRVDA 112
Cdd:pfam00038 43 AEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFrqkyedelnlrtsaENDLVGLRKDLDEATLARVDL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 113 ENRLQTMKEELDFQKNIYSEELRETKRRH--ETRLVEIDNGKQREfesrLADALQELRAQHEDQVEQYKKELEKTYSAKL 190
Cdd:pfam00038 123 EAKIESLKEELAFLKKNHEEEVRELQAQVsdTQVNVEMDAARKLD----LTSALAEIRAQYEEIAAKNREEAEEWYQSKL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 191 DNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRAR 270
Cdd:pfam00038 199 EELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQE 278
|
250 260 270
....*....|....*....|....*....|....*
gi 544063464 271 MQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEER 305
Cdd:pfam00038 279 MARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| LTD |
pfam00932 |
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ... |
353-460 |
2.20e-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: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 353 ARTSGRVAVEEVDEEG-----KFVRLRNKSNEDQSMGNWQIKRQNGDdpllTYRFPPKFTLKAGQVVTIWAAG----AGA 423
Cdd:pfam00932 1 SSATGDVVISEVVYDGsggndEFIELYNTGSKAVDLSGWKLQDASGG----TYTFPNGTTLAPGQTVVVWTGSgtnsATA 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 544063464 424 THSPPTDLVWKAQNTWgcgnslrTALINSTGEEVAMR 460
Cdd:pfam00932 77 GYWGPSNAVWNNGGDA-------VALYDANGELVDSV 106
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
41-305 |
2.84e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.83 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 41 KKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMK 120
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 121 EELDfQKNIYSEELRETKRRHETRLVEIDNgKQREFESRLADALQELRAQHEDQVEQyKKELEKTYSAKLDNARQSAERN 200
Cdd:COG1196 323 EELA-ELEEELEELEEELEELEEELEEAEE-ELEEAEAELAEAEEALLEAEAELAEA-EEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 201 SNLVGAAhEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQE 280
Cdd:COG1196 400 AQLEELE-EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
250 260
....*....|....*....|....*
gi 544063464 281 LLDIKLALDMEIHAYRKLLEGEEER 305
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADY 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
28-306 |
2.32e-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: 69.70 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 28 GRTRAKPGSPLNTKKEgdLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEML 107
Cdd:TIGR02168 663 GGSAKTNSSILERRRE--IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 108 RRVDAENRLQTMKEELdfqKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTyS 187
Cdd:TIGR02168 741 EVEQLEERIAQLSKEL---TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-N 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 188 AKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLAR---ERDTSRRLLAEKEREM 264
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnERASLEEALALLRSEL 896
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 544063464 265 AEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERL 306
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
48-308 |
9.63e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 9.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 48 AAQARL-KDLEALLNSKEAALstALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELdfq 126
Cdd:COG1196 209 AEKAERyRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 127 kniysEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKtysAKLDNARQSAERNSNLVGA 206
Cdd:COG1196 284 -----EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE---EELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 207 AHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKL 286
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260
....*....|....*....|..
gi 544063464 287 ALDMEIHAYRKLLEGEEERLRL 308
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEE 457
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
41-271 |
2.86e-11 |
|
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: 65.17 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 41 KKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMK 120
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 121 EEldfqkniYSEELRET-KRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEktysaKLDNARQSAER 199
Cdd:COG4942 104 EE-------LAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-----ELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544063464 200 NSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARM 271
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
48-320 |
5.76e-11 |
|
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: 64.01 E-value: 5.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 48 AAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQK 127
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 128 NIYSEELRET-KRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEktysakldnarqsaernsnlvga 206
Cdd:COG4942 104 EELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----------------------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 207 aheelqqsriridslsaQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKL 286
Cdd:COG4942 161 -----------------ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250 260 270
....*....|....*....|....*....|....
gi 544063464 287 ALDMEIhayRKLLEGEEERLRLSPSPTSQRSRGR 320
Cdd:COG4942 224 ELEALI---ARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
40-307 |
9.85e-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: 64.31 E-value: 9.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 40 TKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLeaalgEAKKQLQDEMLRRVDAEN-RLQT 118
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL-----EQQKQILRERLANLERQLeELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 119 MKEELDFQKNIYSEELRETKRRHETRLVEIDNgkQREFESRLADALQELraqhEDQVEQYKKELEkTYSAKLDNARQSAE 198
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELES--LEAELEELEAELEEL----ESRLEELEEQLE-TLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 199 RNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLaaKEAKLRDLEDSLArERDTSRRLLAEKEREMAEMRARMQQQLDEY 278
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKL--EEAELKELQAELE-ELEEELEELQEELERLEEALEELREELEEA 473
|
250 260
....*....|....*....|....*....
gi 544063464 279 QELLDIKLALDMEIHAYRKLLEGEEERLR 307
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
47-307 |
4.28e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 47 IAAQARLKDLEALLnskeAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELdFQ 126
Cdd:COG1196 218 LKEELKELEAELLL----LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE-YE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 127 KNIYSEELRETKRRHETRLveIDNGKQREfesRLADALQELRAQHEDQVEQYKKELEKtysaKLDNARQSAERNSNLVGA 206
Cdd:COG1196 293 LLAELARLEQDIARLEERR--RELEERLE---ELEEELAELEEELEELEEELEELEEE----LEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 207 AHEELQQSRIRIDSLSAQLSQLQKQLAA--KEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDI 284
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEAlrAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
250 260
....*....|....*....|...
gi 544063464 285 KLALDMEIHAYRKLLEGEEERLR 307
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLA 466
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
49-313 |
7.27e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 7.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 49 AQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAA---------LGEAKKQLQD--EMLRRVDAEN-RL 116
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswdeidVASAEREIAEleAELERLDASSdDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 117 QTMKEELdfqkniysEELRETKRRHETRLVEIdNGKQREFESRLADAlQELRAQHEDQVEQYKKELEKTYSAKLDnARQS 196
Cdd:COG4913 688 AALEEQL--------EELEAELEELEEELDEL-KGEIGRLEKELEQA-EEELDELQDRLEAAEDLARLELRALLE-ERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 197 AERNSNLVGAAHEELQQsriRIDSLSAQLSQLQKQLAAK--------EAKLRDLEDSLARERDTSRRLLAEKEREMAEMR 268
Cdd:COG4913 757 AALGDAVERELRENLEE---RIDALRARLNRAEEELERAmrafnrewPAETADLDADLESLPEYLALLDRLEEDGLPEYE 833
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 544063464 269 ARMQQQLDE--YQELLDIKLALDMEIHAYRKLLE-----------GEEERLRLSPSPT 313
Cdd:COG4913 834 ERFKELLNEnsIEFVADLLSKLRRAIREIKERIDplndslkripfGPGRYLRLEARPR 891
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
43-270 |
2.80e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 43 EGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEgelhDLRGQVAKLEAALGEA-KKQLQDEMLRRVDAENRLQTMKE 121
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIELLE----PIRELAERYAAARERLaELEYLRAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 122 ELdfqkniysEELRETKRRHETRLVEIDNgKQREFESRLADALQELRAQHEDQVEQYKKELEKTySAKLDNARQSAERNS 201
Cdd:COG4913 296 EL--------EELRAELARLEAELERLEA-RLDALREELDELEAQIRGNGGDRLEQLEREIERL-ERELEERERRRARLE 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544063464 202 NLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRAR 270
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
43-304 |
3.29e-09 |
|
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: 59.70 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 43 EGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQ--DEMLRRVDAE-NRLQTM 119
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSslEQEIENVKSElKELEAR 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 120 KEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADalQELRAQHEDQVEQyKKELEKTYsakLDNARQSAER 199
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSR--IEARLREIEQKLN-RLTLEKEY---LEKEIQELQE 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 200 NSNLVGAAHEELQQsriRIDSLSAQLSQLQKQLAAKEAKLRDLEDS---LARERDTSRRLLAEKEREMAEMRARMQQQLD 276
Cdd:TIGR02169 841 QRIDLKEQIKSIEK---EIENLNGKKEELEEELEELEAALRDLESRlgdLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
250 260
....*....|....*....|....*...
gi 544063464 277 EYQELLDIKLALDMEIHAYRKLLEGEEE 304
Cdd:TIGR02169 918 RLSELKAKLEALEEELSEIEDPKGEDEE 945
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
46-367 |
1.62e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 46 LIAAQARLKDLEALLNSKEAALSTaLSEKRTLEGELHDLRGQVAKLEAAL-GEAKKQLQDEMLRRVDAENRLQTMKEELD 124
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKS-LERQAEKAERYKELKAELRELELALlVLRLEELREELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 125 FQKNIYSEELRETKRRH---ETRLVEID------NGKQREFESRLAdALQELRAQHEDQVEQYKKELEKTYSAKLDNARQ 195
Cdd:TIGR02168 260 AELQELEEKLEELRLEVselEEEIEELQkelyalANEISRLEQQKQ-ILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 196 SAERNsnlvgaahEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDslarERDTSRRLLAEKEREMAEMRARMQQQL 275
Cdd:TIGR02168 339 LAELE--------EKLEELKEELESLEAELEELEAELEELESRLEELEE----QLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 276 DEYQELLDIKLALDMEIHA-YRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHAR 354
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEElLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
330
....*....|...
gi 544063464 355 TSGRVAVEEVDEE 367
Cdd:TIGR02168 487 LQARLDSLERLQE 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
43-281 |
4.55e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 4.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 43 EGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEE 122
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 123 LDFQKnIYSEELRETKRRHETRLVEIdNGKQREFESRLA------DALQELRAQHEDQVEQYKKELEK------TYSAKL 190
Cdd:TIGR02168 833 IAATE-RRLEDLEEQIEELSEDIESL-AAEIEELEELIEeleselEALLNERASLEEALALLRSELEElseelrELESKR 910
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 191 DNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQK---QLAAKEAKLRDLEDSLARERdtsrrlLAEKEREMAEM 267
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSltlEEAEALENKIEDDEEEARRR------LKRLENKIKEL 984
|
250
....*....|....
gi 544063464 268 RARMQQQLDEYQEL 281
Cdd:TIGR02168 985 GPVNLAAIEEYEEL 998
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
108-307 |
1.06e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 108 RRVDAENRLQTMKEELD-------------------------FQKniYSEELREtkRRHETRLVEID--NGKQREFESRL 160
Cdd:COG1196 173 RKEEAERKLEATEENLErledilgelerqleplerqaekaerYRE--LKEELKE--LEAELLLLKLRelEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 161 ADALQELR------AQHEDQVEQYKKELE------KTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQL 228
Cdd:COG1196 249 EELEAELEeleaelAELEAELEELRLELEelelelEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 229 QKQLAAKEAKLRDLEDSLAR---ERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEER 305
Cdd:COG1196 329 EEELEELEEELEELEEELEEaeeELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
..
gi 544063464 306 LR 307
Cdd:COG1196 409 EE 410
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
104-309 |
8.87e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 8.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 104 DEMLRRVDAENRLQTMKEELDFQKNIYSEELRE---TKRRHETRLVEID-NGKQREFESRLADALQE--LRAQHEDQVEQ 177
Cdd:COG3206 93 RPVLERVVDKLNLDEDPLGEEASREAAIERLRKnltVEPVKGSNVIEISyTSPDPELAAAVANALAEayLEQNLELRREE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 178 YKKELE------KTYSAKLDNARQSAE--RNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARE 249
Cdd:COG3206 173 ARKALEfleeqlPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544063464 250 RDTSRRLLAekEREMAEMRARMQQQLDEYQELL--------DIKlALDMEIHAYRKLLEGEEERLRLS 309
Cdd:COG3206 253 PDALPELLQ--SPVIQQLRAQLAELEAELAELSarytpnhpDVI-ALRAQIAALRAQLQQEAQRILAS 317
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
4-283 |
1.66e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 4 LLCLGNLEDARERTGTllaQHPAWGRTRAKPGSPLNTKKEGdliAAQARLKDLEALLNSKEAALStalsekrTLEGELHD 83
Cdd:PRK02224 158 LLQLGKLEEYRERASD---ARLGVERVLSDQRGSLDQLKAQ---IEEKEEKDLHERLNGLESELA-------ELDEEIER 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 84 LRGQVAKLEAALGEAKKQLQD-----EMLRRVDAE-NRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQR-EF 156
Cdd:PRK02224 225 YEEQREQARETRDEADEVLEEheerrEELETLEAEiEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEaGL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 157 ESRLADALQELRAQHEDQVEQYKKELE----------KTYSAKLDNARQSAERNSNLVGAAHE---ELQQSRIRIDSLSA 223
Cdd:PRK02224 305 DDADAEAVEARREELEDRDEELRDRLEecrvaaqahnEEAESLREDADDLEERAEELREEAAElesELEEAREAVEDRRE 384
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544063464 224 QLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKER---EMAEMRARMQ---QQLDEYQELLD 283
Cdd:PRK02224 385 EIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDElreREAELEATLRtarERVEEAEALLE 450
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
57-335 |
1.79e-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: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 57 EALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRE 136
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 137 TKR--RHETRLVEIDNGKQ-REFESRLaDALQELRAQHEDQVEQYKKELEKtysakLDNARQSAERNSNLVGAAHEELQQ 213
Cdd:COG3883 95 LYRsgGSVSYLDVLLGSESfSDFLDRL-SALSKIADADADLLEELKADKAE-----LEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 214 SRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIH 293
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 544063464 294 AYRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQTQGGGSVT 335
Cdd:COG3883 249 AGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAG 290
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
49-309 |
2.24e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 49 AQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELdfqkn 128
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL----- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 129 iysEELRETKRRHETRLveiDNGKQREFESRLADA---------------LQELRAQHEDQVEQYKKELEKTYSAK---- 189
Cdd:PRK02224 436 ---RTARERVEEAEALL---EAGKCPECGQPVEGSphvetieedrerveeLEAELEDLEEEVEEVEERLERAEDLVeaed 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 190 -LDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTsrrlLAEKEREMAEMR 268
Cdd:PRK02224 510 rIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE----VAELNSKLAELK 585
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 544063464 269 ARMqQQLDEYQELLDIKLALDMEIHAYRKLLEG-----EEERLRLS 309
Cdd:PRK02224 586 ERI-ESLERIRTLLAAIADAEDEIERLREKREAlaelnDERRERLA 630
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
44-304 |
2.32e-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: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 44 GDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQ-------DEMLRRVDAENRL 116
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelrallEERFAAALGDAVE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 117 QTMKEELdfQKNIysEELRETKRRHETRLVEIDNGKQREFESRLAD------ALQELRAQHEDQVEQykkELEKtYSAKL 190
Cdd:COG4913 765 RELRENL--EERI--DALRARLNRAEEELERAMRAFNREWPAETADldadleSLPEYLALLDRLEED---GLPE-YEERF 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 191 DNARQSAERN--SNLVGAAHEELQQSRIRIDSLSAQLSQLQ------KQLAAKEAKL-------RDLEDSLARERDTSRR 255
Cdd:COG4913 837 KELLNENSIEfvADLLSKLRRAIREIKERIDPLNDSLKRIPfgpgryLRLEARPRPDpevrefrQELRAVTSGASLFDEE 916
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 544063464 256 LLAEKEREMAEMRARMQQQlDEYQELLDIKLALD----MEIHAYRKLLEGEEE 304
Cdd:COG4913 917 LSEARFAALKRLIERLRSE-EEESDRRWRARVLDvrnhLEFDAEEIDREDGEE 968
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
40-283 |
2.57e-06 |
|
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: 49.89 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 40 TKKEGDLIAAQARLKDLEALLNSKEAALSTALSEK----RTLEGELHDLRGQVAKLEAALGEAKK-------QLQDEMLR 108
Cdd:pfam07888 93 REKHEELEEKYKELSASSEELSEEKDALLAQRAAHeariRELEEDIKTLTQRVLERETELERMKErakkagaQRKEEEAE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 109 RVDAENRLQTMKEEL-----DFQKNIYSEELRETK----RRHETRLVEIDNGKQR---EFESRLAD--ALQELRAQHEDQ 174
Cdd:pfam07888 173 RKQLQAKLQQTEEELrslskEFQELRNSLAQRDTQvlqlQDTITTLTQKLTTAHRkeaENEALLEElrSLQERLNASERK 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 175 VEQYKKELEKTYS------AKLDNAR-QSAERNSNLVGAA-------------HEELQQS----RIRIDSLSAQLSQLQK 230
Cdd:pfam07888 253 VEGLGEELSSMAAqrdrtqAELHQARlQAAQLTLQLADASlalregrarwaqeRETLQQSaeadKDRIEKLSAELQRLEE 332
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 231 QLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQ-------QQLDEYQELLD 283
Cdd:pfam07888 333 RLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRvaqkekeQLQAEKQELLE 392
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
20-285 |
2.95e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.91 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 20 LLAQHPAWgrTRAKPGSPLNTKKEgdliaAQARLKDL--EALLNSKEAALSTALSEkrTLegelhDLRGQVAKLEAALGE 97
Cdd:PRK11281 19 LLCLSSAF--ARAASNGDLPTEAD-----VQAQLDALnkQKLLEAEDKLVQQDLEQ--TL-----ALLDKIDRQKEETEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 98 AKKQLQDemlrrvdAENRLQTMKEELDFQKNIYSEELRETkrrhetrlveIDNGKQREFESRLADALQELraqhedqvEQ 177
Cdd:PRK11281 85 LKQQLAQ-------APAKLRQAQAELEALKDDNDEETRET----------LSTLSLRQLESRLAQTLDQL--------QN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 178 YKKELEkTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSA--------QLSQLQKQLAAKEAKLrDLEDSLARE 249
Cdd:PRK11281 140 AQNDLA-EYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVggkalrpsQRVLLQAEQALLNAQN-DLQRKSLEG 217
|
250 260 270
....*....|....*....|....*....|....*.
gi 544063464 250 RDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIK 285
Cdd:PRK11281 218 NTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAINSK 253
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
43-274 |
5.18e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 43 EGDLIAAQARLKDL--EALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQ--DEMLRRVDAENRLQT 118
Cdd:COG3206 188 RKELEEAEAALEEFrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGsgPDALPELLQSPVIQQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 119 MKEELdfqkniyseelretkrrhetrlveidngkqREFESRLADALQELRAQHEDqVEQYKKELEKTysakldnARQSAE 198
Cdd:COG3206 268 LRAQL------------------------------AELEAELAELSARYTPNHPD-VIALRAQIAAL-------RAQLQQ 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544063464 199 RNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQ---LAAKEAKLRDLEdslaRERDTSRRLLAEKEREMAEMRARMQQQ 274
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQAQLAQLEARlaeLPELEAELRRLE----REVEVARELYESLLQRLEEARLAEALT 384
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
52-307 |
6.03e-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: 49.02 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 52 RLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQL--------------------QDEMLRRV- 110
Cdd:pfam01576 750 QVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLkklqaqmkdlqreleearasRDEILAQSk 829
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 111 DAENRLQTMKEE-LDFQKNIYSEE--------------------------LRETKRRHETRLVEIDngKQREFESRLADA 163
Cdd:pfam01576 830 ESEKKLKNLEAElLQLQEDLAASErarrqaqqerdeladeiasgasgksaLQDEKRRLEARIAQLE--EELEEEQSNTEL 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 164 LQELRAQHEDQVEQYKKEL--EKTYSAKLDNARQSAERNSNLVGAAHEELQqsriridslSAQLSQLQKQLAAKEAKLRD 241
Cdd:pfam01576 908 LNDRLRKSTLQVEQLTTELaaERSTSQKSESARQQLERQNKELKAKLQEME---------GTVKSKFKSSIAALEAKIAQ 978
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544063464 242 LEDSL---ARERDTSRRLLAEKEREMAEMRARMQ---QQLDEYQELLDiKLALDMEiHAYRKLLEGEEERLR 307
Cdd:pfam01576 979 LEEQLeqeSRERQAANKLVRRTEKKLKEVLLQVEderRHADQYKDQAE-KGNSRMK-QLKRQLEEAEEEASR 1048
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
35-300 |
6.32e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 35 GSPLNTKKEGDLIAA-QARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAA--LGEAKKQLQDEMLRRVD 111
Cdd:PRK03918 442 GRELTEEHRKELLEEyTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAeqLKELEEKLKKYNLEELE 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 112 AENR-LQTMKEELDFQKNIYSEELRETKRRHE--TRLVEIDNgKQREFESRLADALQELRA---QHEDQVEQYKKELEKT 185
Cdd:PRK03918 522 KKAEeYEKLKEKLIKLKGEIKSLKKELEKLEElkKKLAELEK-KLDELEEELAELLKELEElgfESVEELEERLKELEPF 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 186 YSA--KLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTsrrllaEKERE 263
Cdd:PRK03918 601 YNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYL------ELSRE 674
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 544063464 264 MAEMRARMQQ---QLDEYQELLDIKLALDMEIHAYRKLLE 300
Cdd:PRK03918 675 LAGLRAELEElekRREEIKKTLEKLKEELEEREKAKKELE 714
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
149-307 |
8.73e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 8.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 149 DNGKQREFESRLADALQELRAQHEDQVEQYKKELEkTYSAKLDNARQSAERNSNL--VGAAHEELQQSRIRIDSL---SA 223
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLAEYSWDEidVASAEREIAELEAELERLdasSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 224 QLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEReMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEE 303
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ-AEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVE 764
|
....
gi 544063464 304 ERLR 307
Cdd:COG4913 765 RELR 768
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
50-281 |
8.83e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 8.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 50 QARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDE-------MLRRVDAENRLQTMKEE 122
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDdadaeavEARREELEDRDEELRDR 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 123 LDFQK------NIYSEELRETKRRHETRLVEIDN----------------GKQREFESRLADALQELRAQHED------Q 174
Cdd:PRK02224 330 LEECRvaaqahNEEAESLREDADDLEERAEELREeaaeleseleeareavEDRREEIEELEEEIEELRERFGDapvdlgN 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 175 VEQYKKEL----------EKTYSAKLDNARQSAERNSNLV-------------GAAH-EELQQSRIRIDSLSAQLSQLQK 230
Cdd:PRK02224 410 AEDFLEELreerdelrerEAELEATLRTARERVEEAEALLeagkcpecgqpveGSPHvETIEEDRERVEELEAELEDLEE 489
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 231 QLAAKEAKLRDLED---------SLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQEL 281
Cdd:PRK02224 490 EVEEVEERLERAEDlveaedrieRLEERREDLEELIAERRETIEEKRERAEELRERAAEL 549
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
58-267 |
1.28e-05 |
|
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: 48.02 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 58 ALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQdeMLRRV----------DAENRLQTMKEELDFqk 127
Cdd:COG3096 829 AFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQ--LLNKLlpqanlladeTLADRLEELREELDA-- 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 128 niySEELRETKRRHETRLVEIDngkqrefesRLADALQELRAQHEDQVEQYK--KELEKTYSAKLDNARQSAERNSNLVG 205
Cdd:COG3096 905 ---AQEAQAFIQQHGKALAQLE---------PLVAVLQSDPEQFEQLQADYLqaKEQQRRLKQQIFALSEVVQRRPHFSY 972
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544063464 206 A-AHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLED----------SLARERDTSRRLLAEKEREMAEM 267
Cdd:COG3096 973 EdAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAqysqynqvlaSLKSSRDAKQQTLQELEQELEEL 1045
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
40-280 |
1.29e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 40 TKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQD-EMLRR--------- 109
Cdd:PRK02224 380 EDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEaEALLEagkcpecgq 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 110 -VDAENRLQTMkEELDFQKNIYSEELRETKRRHETRLVEIDNGKQ-REFESRL------ADALQELRAQHEDQVEQYKKE 181
Cdd:PRK02224 460 pVEGSPHVETI-EEDRERVEELEAELEDLEEEVEEVEERLERAEDlVEAEDRIerleerREDLEELIAERRETIEEKRER 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 182 LE--KTYSAKLDNARQSAERNSNlvgAAHEELQQSRIRIDSLSAQLSQLQKQLAAkeakLRDLEDSLARERDTSRRL--L 257
Cdd:PRK02224 539 AEelRERAAELEAEAEEKREAAA---EAEEEAEEAREEVAELNSKLAELKERIES----LERIRTLLAAIADAEDEIerL 611
|
250 260
....*....|....*....|...
gi 544063464 258 AEKEREMAEMRARMQQQLDEYQE 280
Cdd:PRK02224 612 REKREALAELNDERRERLAEKRE 634
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
46-184 |
2.53e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 46 LIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQ-----LQDEM----LRRVDAENRL 116
Cdd:COG1579 33 LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyeaLQKEIeslkRRISDLEDEI 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544063464 117 QTMKEELDFQKniysEELRETKRRHETRLVEIDNgKQREFESRLADaLQELRAQHEDQVEQYKKELEK 184
Cdd:COG1579 113 LELMERIEELE----EELAELEAELAELEAELEE-KKAELDEELAE-LEAELEELEAEREELAAKIPP 174
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
108-306 |
3.18e-05 |
|
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: 46.59 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 108 RRVDAENRLQTMKEELDFQKNIyseeLRETKRRHETrlveidngkqREFESRLADALQELRAQHED--------QVEQYK 179
Cdd:TIGR02168 173 RRKETERKLERTRENLDRLEDI----LNELERQLKS----------LERQAEKAERYKELKAELRElelallvlRLEELR 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 180 KELEKTYSAKLDNARQSAERNSNLVgAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAE 259
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQ-ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 544063464 260 KEREMAEmRARMQQQLDEYQELLDiklALDMEIHAYRKLLEGEEERL 306
Cdd:TIGR02168 318 LEELEAQ-LEELESKLDELAEELA---ELEEKLEELKEELESLEAEL 360
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
80-281 |
3.51e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 80 ELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELdfqkniysEELRETKRRHETRLVEIDNgKQREFESR 159
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEL--------EDLEKEIKRLELEIEEVEA-RIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 160 LAdalqelRAQHEDQVEQYKKELEKtysakLDNARQSAErnsnlvgaahEELQQSRIRIDSLSAQLSQLQKQLAAKEAKL 239
Cdd:COG1579 82 LG------NVRNNKEYEALQKEIES-----LKRRISDLE----------DEILELMERIEELEEELAELEAELAELEAEL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 544063464 240 RDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQL-DEYQEL 281
Cdd:COG1579 141 EEKKAELDEELAELEAELEELEAEREELAAKIPPELlALYERI 183
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
72-306 |
3.64e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 72 SEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAEnRLQTMKEELdfQKNIYSEELREtKRRHETRLVEIDNg 151
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEK--REYEGYELLKE-KEALERQKEAIER- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 152 kqrefesRLADALQELraqheDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGaahEELQQSRIRIDSLSAQLSQL--- 228
Cdd:TIGR02169 245 -------QLASLEEEL-----EKLTEEISELEKRLEEIEQLLEELNKKIKDLGE---EEQLRVKEKIGELEAEIASLers 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 229 -------QKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEG 301
Cdd:TIGR02169 310 iaekereLEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
....*
gi 544063464 302 EEERL 306
Cdd:TIGR02169 390 YREKL 394
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
36-308 |
5.58e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 36 SPLNTKKEGDLIAAQARLKDLEAL---LNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDA 112
Cdd:PRK03918 213 SSELPELREELEKLEKEVKELEELkeeIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 113 ENRLQTMKEELDFQKNIYSEELRETKRRH-----ETRLVEIDNGKQR-----EFESRLADALQELRAQHE--DQVEQYKK 180
Cdd:PRK03918 293 EEYIKLSEFYEEYLDELREIEKRLSRLEEeingiEERIKELEEKEERleelkKKLKELEKRLEELEERHElyEEAKAKKE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 181 ELEKTYSAKLDNARQSAERNSNLVGAAHEELQQsriRIDSLSAQLSQLQKQLAAKEAKLRDLEdSLARERDTSRRLLAEK 260
Cdd:PRK03918 373 ELERLKKRLTGLTPEKLEKELEELEKAKEEIEE---EISKITARIGELKKEIKELKKAIEELK-KAKGKCPVCGRELTEE 448
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 544063464 261 ERE--MAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRL 308
Cdd:PRK03918 449 HRKelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL 498
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
74-307 |
7.36e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 74 KRTLEGELHDLRGQVAKLEAALGEAKKQLQDemlrrvdAENRLQTMKEeldfQKNIYSeeLRETKRRHETRLVEIdngkq 153
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEE-------AEAALEEFRQ----KNGLVD--LSEEAKLLLQQLSEL----- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 154 refESRLADAlQELRAQHEDQVEQYKKELEKTYSAkldnarQSAERNSNLVGAAHEELQQSRIRIDSLSAQLS------- 226
Cdd:COG3206 225 ---ESQLAEA-RAELAEAEARLAALRAQLGSGPDA------LPELLQSPVIQQLRAQLAELEAELAELSARYTpnhpdvi 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 227 QLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERL 306
Cdd:COG3206 295 ALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRL 374
|
.
gi 544063464 307 R 307
Cdd:COG3206 375 E 375
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
215-307 |
9.13e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 9.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 215 RIRIDSLSAQLSQLQKQLAA----KEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALD- 289
Cdd:COG0542 403 RMEIDSKPEELDELERRLEQleieKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEq 482
|
90 100
....*....|....*....|
gi 544063464 290 --MEIHAYRKLLEGEEERLR 307
Cdd:COG0542 483 ryGKIPELEKELAELEEELA 502
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
51-307 |
1.07e-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: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 51 ARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIY 130
Cdd:pfam01576 68 ARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 131 SEELREtKRRHETRLVEIDNGKQREFESrlADALQELRAQHEDQVEQYKKELEKTysaklDNARQSAERNSNLVGAAHEE 210
Cdd:pfam01576 148 SKLSKE-RKLLEERISEFTSNLAEEEEK--AKSLSKLKNKHEAMISDLEERLKKE-----EKGRQELEKAKRKLEGESTD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 211 LQQsriRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERdTSRRLLAEKEREmaemrarMQQQLDEYQELLDIKLALDM 290
Cdd:pfam01576 220 LQE---QIAELQAQIAELRAQLAKKEEELQAALARLEEET-AQKNNALKKIRE-------LEAQISELQEDLESERAARN 288
|
250
....*....|....*..
gi 544063464 291 EIHAYRKLLEGEEERLR 307
Cdd:pfam01576 289 KAEKQRRDLGEELEALK 305
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
45-264 |
1.41e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 45 DLIAAQARLKDLEALLNSkeAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDemlrrvdAENRLQTMKEELD 124
Cdd:COG4913 263 RYAAARERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDA-------LREELDELEAQIR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 125 FQKNIYSEELRETKRRHETRLVEIDNGkqrefESRLADALQELRAQHEDQVEQYKkelektysAKLDNARQSAERNSNLV 204
Cdd:COG4913 334 GNGGDRLEQLEREIERLERELEERERR-----RARLEALLAALGLPLPASAEEFA--------ALRAEAAALLEALEEEL 400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 205 GAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREM 264
Cdd:COG4913 401 EALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
43-197 |
3.51e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 43 EGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEG--ELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMK 120
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALR 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 121 EELDFQKNIYSEELRETKRRHETRLVEIdNGKQREFESRLADA------LQELRAQHEDQVEQYKKELEKTYSAKLDNAR 194
Cdd:COG3206 305 AQLQQEAQRILASLEAELEALQAREASL-QAQLAQLEARLAELpeleaeLRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
...
gi 544063464 195 QSA 197
Cdd:COG3206 384 TVG 386
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
172-290 |
3.96e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.53 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 172 EDQVEQYKKELEKTYsAKLDNARQsaernsnlvgaAHEELQQSRIRID------SLSAQLSQLQKQLAAKEAKLRDLEDS 245
Cdd:COG3524 176 EDAVRFAEEEVERAE-ERLRDARE-----------ALLAFRNRNGILDpeataeALLQLIATLEGQLAELEAELAALRSY 243
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 544063464 246 L---ARERDTSRRLLAEKEREMAEMRARM---------QQQLDEYQEL-LDIKLALDM 290
Cdd:COG3524 244 LspnSPQVRQLRRRIAALEKQIAAERARLtgasggdslASLLAEYERLeLEREFAEKA 301
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
72-270 |
5.05e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 72 SEKRTLEGELHDLRGQVAKLEAALGEAKKQLQD--EMLRRVDA-ENRLQTMKEELDFQKNIYsEELRETKRRHETRLVEI 148
Cdd:COG1340 78 EERDELNEKLNELREELDELRKELAELNKAGGSidKLRKEIERlEWRQQTEVLSPEEEKELV-EKIKELEKELEKAKKAL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 149 DNGKQREFESRLADALQELRAQHEDQVEQYKKELEKtYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQL 228
Cdd:COG1340 157 EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQE-LHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIEL 235
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 544063464 229 QKqlaakeaKLRDLEDSLARERDTSRRLLAEKEREMAEMRAR 270
Cdd:COG1340 236 QK-------ELRELRKELKKLRKKQRALKREKEKEELEEKAE 270
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
29-280 |
5.31e-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: 42.44 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 29 RTRAKPGSPLNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGElhdlrgQVAKLEAALGEAKKQLQDEM-L 107
Cdd:pfam09731 110 KDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKA------HTDSLKEASDTAEISREKATdS 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 108 RRVDAENRLQTMKEELDFQKNIYSEELRETK-RRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVE----QYKKEL 182
Cdd:pfam09731 184 ALQKAEALAEKLKEVINLAKQSEEEAAPPLLdAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVAseriVFQQEL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 183 EKTY-----SAKLDNARQSAERNSnLVGAAHEELQQSRIRIDSLSAQLSQ-LQKQLAAKEAKLRDLEDSLARE-----RD 251
Cdd:pfam09731 264 VSIFpdiipVLKEDNLLSNDDLNS-LIAHAHREIDQLSKKLAELKKREEKhIERALEKQKEELDKLAEELSARleevrAA 342
|
250 260
....*....|....*....|....*....
gi 544063464 252 TSRRLLAEKEREMAEMRARMQQQLDEYQE 280
Cdd:pfam09731 343 DEAQLRLEFEREREEIRESYEEKLRTELE 371
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
47-244 |
5.82e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 47 IAAQARLKDLEALLNSKEAALStalsEKRTLEGELHDLRGQVAKLEAALGEAKKQLqdEMLRRVDAENRLQTMKEELDFQ 126
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREEL--EKLEKLLQLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 127 KNIYSEELRETKRRHEtrlveidngkqrefesRLADALQELRAQhEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGA 206
Cdd:COG4717 141 LAELPERLEELEERLE----------------ELRELEEELEEL-EAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190
....*....|....*....|....*....|....*...
gi 544063464 207 AHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLED 244
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
64-323 |
6.28e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 64 EAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQ--DEMLRRVD--AENRLQTMKEELDFQkniySEELRETKR 139
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSalNRLLPRLNllADETLADRVEEIREQ----LDEAEEAKR 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 140 ---RHETRLVEIDngkqrefesRLADALQELRAQHeDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRI 216
Cdd:PRK04863 912 fvqQHGNALAQLE---------PIVSVLQSDPEQF-EQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLA 981
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 217 RIDSLSAQLSQLQKQLAAKEAKLRD-LEDSLARERDTSRRLLAEKERemaemRARMQQQLDEY-QELLDIKLALDmeiha 294
Cdd:PRK04863 982 KNSDLNEKLRQRLEQAEQERTRAREqLRQAQAQLAQYNQVLASLKSS-----YDAKRQMLQELkQELQDLGVPAD----- 1051
|
250 260 270
....*....|....*....|....*....|..
gi 544063464 295 yrkllEGEEERLRLSPSPTSQR---SRGRASS 323
Cdd:PRK04863 1052 -----SGAEERARARRDELHARlsaNRSRRNQ 1078
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
85-372 |
7.49e-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: 42.03 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 85 RGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKE----ELDFQKNIYSEELR---ETKR-----RHETRLVEIDNGK 152
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKarqaEMDRQAAIYAEQERmamEREReleriRQEERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 153 QREFESRLAD--ALQELRAQHEDQVEQYKKELEKTYSAKLdnarQSAERnsnlvgaaHEELQQSRIRIDSLSAQlsqlqk 230
Cdd:pfam17380 367 QEEIAMEISRmrELERLQMERQQKNERVRQELEAARKVKI----LEEER--------QRKIQQQKVEMEQIRAE------ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 231 QLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRA----RMQQQLDEYQELLDIKLA-------LDMEIHAYRKLL 299
Cdd:pfam17380 429 QEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQqeeeRKRKKLELEKEKRDRKRAeeqrrkiLEKELEERKQAM 508
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544063464 300 EGEEERLRLSPSPTSQRSRGRASSHSSQTqgggSVTKKRKLESTESRSSFSQHAR--TSGRVAVEEVDEEGKFVR 372
Cdd:pfam17380 509 IEEERKRKLLEKEMEERQKAIYEEERRRE----AEEERRKQQEMEERRRIQEQMRkaTEERSRLEAMEREREMMR 579
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
115-307 |
9.10e-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: 41.98 E-value: 9.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 115 RLQTMKEELDFQKNIYSEELRETKRR-HE-TRLVEIDNGKQREFESRLADALQELRAQHEdQVEQYKKELEKTySAKLDN 192
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRlDElSQELSDASRKIGEIEKEIEQLEQEEEKLKE-RLEELEEDLSSL-EQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 193 ARQSaernsnlvgaaheelqqsrirIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARER-DTSRRLLAEKEREMAEMRARM 271
Cdd:TIGR02169 756 VKSE---------------------LKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARL 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 544063464 272 Q-------------QQL-DEYQELLDIKLALDMEIHAYRKLLEGEEERLR 307
Cdd:TIGR02169 815 ReieqklnrltlekEYLeKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
41-306 |
1.11e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 41 KKEGDLIAAQARLKDLE----------ALLNSKEAALSTALSEkrtLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRV 110
Cdd:pfam01576 409 KLEGQLQELQARLSESErqraelaeklSKLQSELESVSSLLNE---AEGKNIKLSKDVSSLESQLQDTQELLQEETRQKL 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 111 DAENRLQTMKEELDFQKNIYSEElrETKRRHETRLVEIDNGKQREFESRLADALQELraqheDQVEQYKKELEKtysaKL 190
Cdd:pfam01576 486 NLSTRLRQLEDERNSLQEQLEEE--EEAKRNVERQLSTLQAQLSDMKKKLEEDAGTL-----EALEEGKKRLQR----EL 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 191 DNARQSAERNSnlvgAAHEELQQSRIR----IDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAE 266
Cdd:pfam01576 555 EALTQQLEEKA----AAYDKLEKTKNRlqqeLDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAE 630
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 544063464 267 MRARMQQQLDEYQELLDIKLALDmEIHAYRKLLEGEEERL 306
Cdd:pfam01576 631 AREKETRALSLARALEEALEAKE-ELERTNKQLRAEMEDL 669
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
160-268 |
1.17e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 160 LADALQELRAQhEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQS---RIRIDSLSAQLSQLQKQLAAKE 236
Cdd:PRK09039 79 LQDSVANLRAS-LSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSaraLAQVELLNQQIAALRRQLAALE 157
|
90 100 110
....*....|....*....|....*....|....*....
gi 544063464 237 AKLRDLE----DSLARERDTSRRL---LAEKEREMAEMR 268
Cdd:PRK09039 158 AALDASEkrdrESQAKIADLGRRLnvaLAQRVQELNRYR 196
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
48-199 |
1.51e-03 |
|
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: 41.20 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 48 AAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLqdemlrrVDAENRLQTMKEELDFQK 127
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL-------AQLELRLEGLEVRIDNLQ 942
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544063464 128 NIYSEELRETKRRHETRLVEIDNG--KQREFESRLADALQELRAQHEDQVEQYKKELE-----KTYSAKLDNARQSAER 199
Cdd:TIGR02168 943 ERLSEEYSLTLEEAEALENKIEDDeeEARRRLKRLENKIKELGPVNLAAIEEYEELKErydflTAQKEDLTEAKETLEE 1021
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
48-268 |
1.70e-03 |
|
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: 40.96 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 48 AAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRG--------------QVAKLEAALGEAKKQLqDEMLRRV--- 110
Cdd:pfam10174 349 ALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDmldvkerkinvlqkKIENLQEQLRDKDKQL-AGLKERVksl 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 111 --DAENR---LQTMKEELDFQKNIYsEELRETKRRHE-TRLVEIDNGKQrefesRLADALQELRAQHEDQVEQYKKELEK 184
Cdd:pfam10174 428 qtDSSNTdtaLTTLEEALSEKERII-ERLKEQREREDrERLEELESLKK-----ENKDLKEKVSALQPELTEKESSLIDL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 185 TYSAKldNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEA------KLRDLEDSLARERDTSRRLLA 258
Cdd:pfam10174 502 KEHAS--SLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTnpeindRIRLLEQEVARYKEESGKAQA 579
|
250
....*....|
gi 544063464 259 EKEREMAEMR 268
Cdd:pfam10174 580 EVERLLGILR 589
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
55-306 |
1.71e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 55 DLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEML--RRVDAENRLQTMKEELDFQKNIYSE 132
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVcgRELTEEHRKELLEEYTAELKRIEKE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 133 --ELRETKRRHETRLVEIDNGKQREfesrladalQELRAQHE--DQVEQYKKELEKTYSAKLdnarqsaERNSNLVGAAH 208
Cdd:PRK03918 468 lkEIEEKERKLRKELRELEKVLKKE---------SELIKLKElaEQLKELEEKLKKYNLEEL-------EKKAEEYEKLK 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 209 EELQQSRIRIDSLSAQLSQLQ---KQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIK 285
Cdd:PRK03918 532 EKLIKLKGEIKSLKKELEKLEelkKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAE 611
|
250 260
....*....|....*....|.
gi 544063464 286 laldMEIHAYRKLLEGEEERL 306
Cdd:PRK03918 612 ----KELEREEKELKKLEEEL 628
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
92-281 |
2.07e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 92 EAALGEAKKQLQDEMLRR------VDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQ 165
Cdd:COG4717 306 ELQALPALEELEEEELEEllaalgLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 166 ELRAQHEdQVEQYKKELEK--TYSAKLDNARQSAERNSNLVGAA--HEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRD 241
Cdd:COG4717 386 ELRAALE-QAEEYQELKEEleELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 544063464 242 LEDSlarerdtsrRLLAEKEREMAEMRARMQQQLDEYQEL 281
Cdd:COG4717 465 LEED---------GELAELLQELEELKAELRELAEEWAAL 495
|
|
| COG0610 |
COG0610 |
Type I site-specific restriction-modification system, R (restriction) subunit and related ... |
83-305 |
2.07e-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: 40.62 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 83 DLRGQVAKLEAALGE-AKKQLQDEMLrrVDAENRLQTMKEELDFQKNIYSEElretkrrhetrlVEIDNGKQREFESRLA 161
Cdd:COG0610 648 DYRGIFENLKKALALySEEDGKEDVL--TDPEEALEELKEALDELRALFPEG------------VDFSAFDPTEKLEALD 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 162 DALQELRAQHEDQVEQYK--KELEKTYSAkldnARQSAErnsnLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAK--EA 237
Cdd:COG0610 714 EAVERFLGDEEARKEFKKlfKELSRLYNL----LSPDDE----FGDLELEKYRDDVSFYLALRAKLRKLGEKLDLKeyEE 785
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544063464 238 KLRDL-EDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEER 305
Cdd:COG0610 786 KIRQLlDEAIDLERKEIKPRIKQNPVQYRKFSELLEEIIEEYNNGALDADEVLEELEELAKEVKEEEER 854
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
51-276 |
2.14e-03 |
|
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: 40.44 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 51 ARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDE---MLRRVDA-ENRLQTMKE---EL 123
Cdd:pfam19220 188 AELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAErasLRMKLEAlTARAAATEQllaEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 124 DFQKNIYSEELRETKRRHETRLVEIDNgkqreFESRLAdalqELRAQHEDQVEQYKKelektysakLDNARQSAERNSNL 203
Cdd:pfam19220 268 RNQLRDRDEAIRAAERRLKEASIERDT-----LERRLA----GLEADLERRTQQFQE---------MQRARAELEERAEM 329
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544063464 204 VG---AAHE-ELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDledslarerdTSRRLLAEKEREMAEmRARMQQQLD 276
Cdd:pfam19220 330 LTkalAAKDaALERAEERIASLSDRIAELTKRFEVERAALEQ----------ANRRLKEELQRERAE-RALAQGALE 395
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
221-282 |
2.15e-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: 38.33 E-value: 2.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544063464 221 LSAQLSQLQKQLAAKEAKLRDLEDSLARERDT-SRRLLAEKEREMAEMRARMQQQLDEYQELL 282
Cdd:smart00935 23 LEKEFKKRQAELEKLEKELQKLKEKLQKDAATlSEAAREKKEKELQKKVQEFQRKQQKLQQDL 85
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
217-283 |
2.25e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 2.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544063464 217 RIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKER------EMAEMRARMQQQLDEYQELLD 283
Cdd:PRK09039 54 ALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRlqallaELAGAGAAAEGRAGELAQELD 126
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
164-309 |
2.40e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 164 LQELRAQHEDQVEQYKKELEKTYSAK---LDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLR 240
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKpelNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544063464 241 DLEDSLARERDTSRRllAEKEREMAEMRARMQ---QQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLS 309
Cdd:COG4717 120 KLEKLLQLLPLYQEL--EALEAELAELPERLEeleERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
221-282 |
2.40e-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: 38.33 E-value: 2.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544063464 221 LSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELL 282
Cdd:pfam03938 24 LEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQEL 85
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
45-281 |
2.51e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 45 DLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELD 124
Cdd:COG1196 561 AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 125 fqkniySEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLV 204
Cdd:COG1196 641 ------TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 205 GAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDtsrrlLAEKEREMAEMRARMQQ-------QLDE 277
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD-----LEELERELERLEREIEAlgpvnllAIEE 789
|
....
gi 544063464 278 YQEL 281
Cdd:COG1196 790 YEEL 793
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
131-307 |
2.54e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 131 SEELRETKRRHETRLVEIDNGKQREfesRLADALQELRAqHEDQVEQYKKELEKTYS------------------AKLDN 192
Cdd:COG2433 312 KEDLSVEEKLHLAREYGYDNDHERD---ALAAALKAYDA-YKNKFERVEKKVPPDVDrdevkarvirglsieealEELIE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 193 ARQSAERNSNLVGAAHEElqqsrIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLlaekEREMAEMRARMQ 272
Cdd:COG2433 388 KELPEEEPEAEREKEHEE-----RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERL----ERELSEARSEER 458
|
170 180 190
....*....|....*....|....*....|....*
gi 544063464 273 QQLDEYQELldikLALDMEIHAYRKLLEGEEERLR 307
Cdd:COG2433 459 REIRKDREI----SRLDREIERLERELEEERERIE 489
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
31-303 |
2.75e-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: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 31 RAKPGSPLNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQ------- 103
Cdd:pfam01576 174 KAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQaalarle 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 104 DEMLRRVDAENRLQTMKEEL-DFQKNIYSEELRETKRRHETR-LVEIDNGKQREFESRL--ADALQELRAQHEDQVEQYK 179
Cdd:pfam01576 254 EETAQKNNALKKIRELEAQIsELQEDLESERAARNKAEKQRRdLGEELEALKTELEDTLdtTAAQQELRSKREQEVTELK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 180 KELE---KTYSAKLDNARQsaeRNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRL 256
Cdd:pfam01576 334 KALEeetRSHEAQLQEMRQ---KHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKL 410
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 544063464 257 laekEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEE 303
Cdd:pfam01576 411 ----EGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAE 453
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
99-303 |
2.84e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 99 KKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSE------ELRETKRRHETRLVEID------NGKQREFESRLAD--AL 164
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVLREINEisselpELREELEKLEKEVKELEelkeeiEELEKELESLEGSkrKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 165 QELRAQHEDQVEQYKKELEKTYS--AKLDNARQSAERNSNLVgaahEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDL 242
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEkvKELKELKEKAEEYIKLS----EFYEEYLDELREIEKRLSRLEEEINGIEERIKEL 333
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544063464 243 EDSLARERDTSRRlLAEKEREMAEmrarmqqqLDEYQELLDIKLALDMEIHAYRKLLEGEE 303
Cdd:PRK03918 334 EEKEERLEELKKK-LKELEKRLEE--------LEERHELYEEAKAKKEELERLKKRLTGLT 385
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
88-306 |
3.09e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 88 VAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYS---------------EELRETKRRHETRLVEIDNGK 152
Cdd:PRK04863 437 ADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQlvrkiagevsrseawDVARELLRRLREQRHLAEQLQ 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 153 QREfeSRLADALQELRAQHedQVEQYKKELEKTYSAKLDNA---RQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQ 229
Cdd:PRK04863 517 QLR--MRLSELEQRLRQQQ--RAERLLAEFCKRLGKNLDDEdelEQLQEELEARLESLSESVSEARERRMALRQQLEQLQ 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 230 ---KQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEmrarMQQQLDEYQELldiKLALDmEIHAYRKLLEGEEERL 306
Cdd:PRK04863 593 ariQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEY----MQQLLEREREL---TVERD-ELAARKQALDEEIERL 664
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
40-307 |
3.11e-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: 40.00 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 40 TKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAK------KQLQDEMLRRVDAE 113
Cdd:TIGR04523 148 KKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKkkiqknKSLESQISELKKQN 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 114 NRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDN------GKQREFE------SRLADALQELRAQHEDQVEQYKKE 181
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKikkqlsEKQKELEqnnkkiKELEKQLNQLKSEISDLNNQKEQD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 182 LEKTYSAKLDNARQSAERNSNlvgaaheELQQSRIRIDSLSAQLSQLQKQLAAKEAklrdledslarERDTSRRLLAEKE 261
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQN-------QISQNNKIISQLNEQISQLKKELTNSES-----------ENSEKQRELEEKQ 369
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 544063464 262 REMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLR 307
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK 415
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
45-367 |
3.21e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.10 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 45 DLIAAQAR---------LKDLEALLNSKEAALSTAlseKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENR 115
Cdd:pfam15921 302 EIIQEQARnqnsmymrqLSDLESTVSQLRSELREA---KRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 116 LQTMKEELDFQKNIYSEELRETKR---RHETRLVEIDNgKQREFESRLADaLQELRAQHEDQVEQYKKELEKTYSAkLDN 192
Cdd:pfam15921 379 LQKLLADLHKREKELSLEKEQNKRlwdRDTGNSITIDH-LRRELDDRNME-VQRLEALLKAMKSECQGQMERQMAA-IQG 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 193 ARQSAERNSNLVGaaheELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERdtsrRLLAEKEREMAEMRARMQ 272
Cdd:pfam15921 456 KNESLEKVSSLTA----QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKE----RAIEATNAEITKLRSRVD 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 273 QQLDEYQELldiklaldmeihayrkllEGEEERLRlspsptsqRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQH 352
Cdd:pfam15921 528 LKLQELQHL------------------KNEGDHLR--------NVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQH 581
|
330
....*....|....*
gi 544063464 353 ARTSGRVAVEEVDEE 367
Cdd:pfam15921 582 GRTAGAMQVEKAQLE 596
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
157-293 |
3.29e-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: 40.32 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 157 ESRLADALQELRAQH--EDQVEQYKKELEKTYSAKLD----NARQSAERNSNLVGAAheELQQSRIRIDSLSAQLSQLQK 230
Cdd:COG3096 518 RAQLAELEQRLRQQQnaERLLEEFCQRIGQQLDAAEEleelLAELEAQLEELEEQAA--EAVEQRSELRQQLEQLRARIK 595
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 231 QLAAKEAKLRDLEDSLARERDTSRRLLAEKeremAEMRARMQQQLD-------EYQELLDIKLALDMEIH 293
Cdd:COG3096 596 ELAARAPAWLAAQDALERLREQSGEALADS----QEVTAAMQQLLErereatvERDELAARKQALESQIE 661
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
51-307 |
3.38e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 51 ARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKqlqdemLRRVDAENRLQTMKEELDFQKniY 130
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE------LKEEIEELEKELESLEGSKRK--L 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 131 SEELRETKRRHETRLVEIdngkqREFESRLAD--ALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSnlVGAAH 208
Cdd:PRK03918 258 EEKIRELEERIEELKKEI-----EELEEKVKElkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING--IEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 209 EELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARErDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLAl 288
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK-EELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS- 408
|
250
....*....|....*....
gi 544063464 289 dmEIHAYRKLLEGEEERLR 307
Cdd:PRK03918 409 --KITARIGELKKEIKELK 425
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
46-184 |
3.52e-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: 39.14 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 46 LIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQD--EMLRRVDAENRLQTMKEEL 123
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeEQLGNVRNNKEYEALQKEI 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544063464 124 DFQK---NIYSEELRETKRRHETRLVEIDNGKQRefESRLADALQELRAQHEDQVEQYKKELEK 184
Cdd:COG1579 99 ESLKrriSDLEDEILELMERIEELEEELAELEAE--LAELEAELEEKKAELDEELAELEAELEE 160
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
46-285 |
4.48e-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: 39.70 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 46 LIAAQARLKDLEALLNSKEAALSTALsekRTLEGELHDLRGQVAKLEAA-------LGEAKKQLQDEMLRRVDAENRLQT 118
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQELIFLL---QAREKEIHDLEIQLTAIKTSeehylkeVEDLKTELEKEKLKNIELTAHCDK 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 119 MKEELDFQKNIYSEELRETKRRHETRlveIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKT---YSAKLDNARQ 195
Cdd:pfam05483 497 LLLENKELTQEASDMTLELKKHQEDI---INCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKgdeVKCKLDKSEE 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 196 SAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQK---QLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQ 272
Cdd:pfam05483 574 NARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKnieELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFE 653
|
250
....*....|...
gi 544063464 273 QQLDEYQELLDIK 285
Cdd:pfam05483 654 EIIDNYQKEIEDK 666
|
|
| LCD1 |
pfam09798 |
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. ... |
221-347 |
5.08e-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: 39.61 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 221 LSAQLSQLQKQLAAKEAKLRDLEDSLARerdtsrrllaEKEREMAEMRArmqqqldEYQELLDIKLALDMEIhayRKLle 300
Cdd:pfam09798 2 LRDKLELLQQEKEKELEKLKNSYEELKS----------SHEEELEKLKQ-------EVQKLEDEKKFLLNEL---RSL-- 59
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 544063464 301 geeerlrLSPSPTSQRSRGRASSHSSQtqgggSVTKKRKLESTESRS 347
Cdd:pfam09798 60 -------SATSPASSQSHETDTDDSSS-----VSLKKRKIEESTAES 94
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
89-182 |
5.23e-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: 37.18 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 89 AKLEAALGEAKKQLQDEmlrrvdaENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELR 168
Cdd:smart00935 21 KQLEKEFKKRQAELEKL-------EKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEEL 93
|
90
....*....|....
gi 544063464 169 AQHEDQVEQYKKEL 182
Cdd:smart00935 94 QKILDKINKAIKEV 107
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
55-274 |
5.38e-03 |
|
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: 39.16 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 55 DLEALLNSKEAALSTALSEKRTLEGELHD-LRGQVAKLEAALGEAKKQLQDEMLRRVDAE-NRLQTMKEELDFQKNIYSE 132
Cdd:pfam15709 308 NMESEEERSEEDPSKALLEKREQEKASRDrLRAERAEMRRLEVERKRREQEEQRRLQQEQlERAEKMREELELEQQRRFE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 133 ELRETKRRHETrlveiDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNlvgaaheelq 212
Cdd:pfam15709 388 EIRLRKQRLEE-----ERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQ---------- 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544063464 213 qsriRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQ 274
Cdd:pfam15709 453 ----RQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALE 510
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
176-344 |
6.28e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 39.27 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 176 EQYKKELEKTYSAKLDN------ARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARE 249
Cdd:PRK10929 26 KQITQELEQAKAAKTPAqaeiveALQSALNWLEERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 250 R------DTSRRLLaEKEREmaemrarMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSqrSRGRASS 323
Cdd:PRK10929 106 AleqeilQVSSQLL-EKSRQ-------AQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNT--PLAQAQL 175
|
170 180
....*....|....*....|.
gi 544063464 324 HSSQTQgggSVTKKRKLESTE 344
Cdd:PRK10929 176 TALQAE---SAALKALVDELE 193
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
48-280 |
7.47e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 48 AAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQK 127
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE 1645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 128 NIYSEELRETKRRHETRLVEIdnGKQREFESRLADALQELRAQHEDQVEQYKKELEKtySAKLDNARQSAERNSNLVGAA 207
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEE--AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE--AKKAEELKKKEAEEKKKAEEL 1721
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544063464 208 HEELQQSRIRIDSLSAQLSQLQKQlaAKEAKLRDLEDSLARERDTSRRLLAEKEREmaEMRARMQQQLDEYQE 280
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKK--AEEAKKDEEEKKKIAHLKKEEEKKAEEIRK--EKEAVIEEELDEEDE 1790
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
38-184 |
9.16e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.61 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 38 LNTKKEGDLIAAQAR-----LKDlEALLNSKEAALStalsEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDA 112
Cdd:PRK12704 34 KEAEEEAKRILEEAKkeaeaIKK-EALLEAKEEIHK----LRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 113 ENRLQTMKEELDFQKNIY---SEELRETKRRHETRLVEIDNGKQREFESRLADALQElRAQHEDQV------EQYKKELE 183
Cdd:PRK12704 109 EEELEKKEKELEQKQQELekkEEELEELIEEQLQELERISGLTAEEAKEILLEKVEE-EARHEAAVlikeieEEAKEEAD 187
|
.
gi 544063464 184 K 184
Cdd:PRK12704 188 K 188
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
172-243 |
9.51e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 38.00 E-value: 9.51e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544063464 172 EDQVEQYKKELEKTYsAKLDNARQSAERNSNLVG---AAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLE 243
Cdd:COG0845 60 QAALAQAQAQLAAAQ-AQLELAKAELERYKALLKkgaVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTT 133
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
45-258 |
9.59e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 38.76 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 45 DLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELD 124
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 125 FQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQykkELEKtysaKLDNARQSAER--NSN 202
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE---ELER----ELERLEREIEAlgPVN 783
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 544063464 203 LvgAAHEELQQSRIRIDSLSAQLSQLQKqlaAKEaKLRDLEDSLarERDTSRRLLA 258
Cdd:COG1196 784 L--LAIEEYEELEERYDFLSEQREDLEE---ARE-TLEEAIEEI--DRETRERFLE 831
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
56-271 |
9.68e-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: 38.67 E-value: 9.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 56 LEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQ--DEMLRRVDAENR------------------ 115
Cdd:pfam12128 602 LRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKnaRLDLRRLFDEKQsekdkknkalaerkdsan 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 116 -----LQTMKEELDFQKNIYSEELRETKRRHET------RLVEIDNGKQREFESRLADALQELRAQHEDQVE-QYKKELE 183
Cdd:pfam12128 682 erlnsLEAQLKQLDKKHQAWLEEQKEQKREARTekqaywQVVEGALDAQLALLKAAIAARRSGAKAELKALEtWYKRDLA 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 184 ----------------KTYSAKLDNARQ-SAERNSNLVGAAHEELQQS---RIRIDSLSAQLSQLQKQLAAKEAKLRDLE 243
Cdd:pfam12128 762 slgvdpdviaklkreiRTLERKIERIAVrRQEVLRYFDWYQETWLQRRprlATQLSNIERAISELQQQLARLIADTKLRR 841
|
250 260
....*....|....*....|....*...
gi 544063464 244 DSLARERDTSRRLLAEKEREMAEMRARM 271
Cdd:pfam12128 842 AKLEMERKASEKQQVRLSENLRGLRCEM 869
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
220-305 |
9.90e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 38.02 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544063464 220 SLSAQLSQLQKQLAAKEA---KLRDLEDSLARERDTSRRLLAEKEREMAEMR---ARMQQQLdeyqELLDIKL-ALDMEI 292
Cdd:PRK09039 78 DLQDSVANLRASLSAAEAersRLQALLAELAGAGAAAEGRAGELAQELDSEKqvsARALAQV----ELLNQQIaALRRQL 153
|
90
....*....|...
gi 544063464 293 HAYRKLLEGEEER 305
Cdd:PRK09039 154 AALEAALDASEKR 166
|
|
| |
