|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
1-200 |
1.15e-69 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 224.41 E-value: 1.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 1 MLRRVDAENRLQTMKEELDFQKNIYSEELRETKRRH--ETRLVEIDNGKQREfesrLADALQELRAQHEDQVEQYKKELE 78
Cdd:pfam00038 116 TLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVsdTQVNVEMDAARKLD----LTSALAEIRAQYEEIAAKNREEAE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 79 KTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKERE 158
Cdd:pfam00038 192 EWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAE 271
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2244985380 159 MAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEER 200
Cdd:pfam00038 272 LQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| LTD |
pfam00932 |
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ... |
248-355 |
2.07e-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: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 248 ARTSGRVAVEEVDEEG-----KFVRLRNKSNEDQSMGNWQIKRQNGDdpllTYRFPPKFTLKAGQVVTIWAAG----AGA 318
Cdd:pfam00932 1 SSATGDVVISEVVYDGsggndEFIELYNTGSKAVDLSGWKLQDASGG----TYTFPNGTTLAPGQTVVVWTGSgtnsATA 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2244985380 319 THSPPTDLVWKAQNTWgcgnslrTALINSTGEEVAMR 355
Cdd:pfam00932 77 GYWGPSNAVWNNGGDA-------VALYDANGELVDSV 106
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-276 |
1.72e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 3 RRVDAENRLQTMKEELD-------------------------FQKniYSEELREtkRRHETRLVEID--NGKQREFESRL 55
Cdd:COG1196 173 RKEEAERKLEATEENLErledilgelerqleplerqaekaerYRE--LKEELKE--LEAELLLLKLRelEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 56 ADALQELR------AQHEDQVEQYKKELE------KTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQL 123
Cdd:COG1196 249 EELEAELEeleaelAELEAELEELRLELEelelelEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 124 QKQLAAKEAKLRDLEDSLAR---ERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEER 200
Cdd:COG1196 329 EEELEELEEELEELEEELEEaeeELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2244985380 201 LrlspsptsQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQ 276
Cdd:COG1196 409 E--------EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-203 |
2.23e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 2 LRRVDAENRLQTMKEELDFQKNIySEELRETKRRHETRLVEIDNgKQREFESRLADALQELRA-----QHEDQVEQYKKE 76
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAE-LEELEAELAELEAELEELRL-ELEELELELEEAQAEEYEllaelARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 77 LEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKE 156
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2244985380 157 REMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRL 203
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-202 |
5.68e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 5.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 2 LRRVDAE-NRLQTMKEELDFQKNIYSEELRETKRRHETRLVEID--NGKQREFESRLADALQELRAQHEDQvEQYKKELE 78
Cdd:COG1196 241 LEELEAElEELEAELEELEAELAELEAELEELRLELEELELELEeaQAEEYELLAELARLEQDIARLEERR-RELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 79 KTYSAKLDNARQSAERNSNLVgAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLL---AEK 155
Cdd:COG1196 320 ELEEELAELEEELEELEEELE-ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALraaAEL 398
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2244985380 156 EREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLR 202
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1-165 |
5.77e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 1 MLRRVDAENRLQTMKEELdfqkniysEELRETKRRHETRLVEIDNgKQREFESRLADALQELRAQHEDQVEQYKKELEKT 80
Cdd:COG4913 280 ALRLWFAQRRLELLEAEL--------EELRAELARLEAELERLEA-RLDALREELDELEAQIRGNGGDRLEQLEREIERL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 81 ySAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMA 160
Cdd:COG4913 351 -ERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
....*
gi 2244985380 161 EMRAR 165
Cdd:COG4913 430 SLERR 434
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
6-215 |
1.73e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 6 DAENRLQTMKEELDfQKNIYSEELRETKRRHETRLVEID-------------NGKQREFESRLADA---LQELRAQHEDQ 69
Cdd:COG4942 24 EAEAELEQLQQEIA-ELEKELAALKKEEKALLKQLAALErriaalarriralEQELAALEAELAELekeIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 70 VEQYKKELEKTYSAKL----------DNARQsAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLED 139
Cdd:COG4942 103 KEELAELLRALYRLGRqpplalllspEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2244985380 140 SLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIhayRKLLEGEEERLRLSPSPTSQRSRGR 215
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI---ARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1-204 |
1.81e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 1 MLRRVDAENRLQTMKEELDFQKNIYSEELRE---TKRRHETRLVEID-NGKQREFESRLADALQE--LRAQHEDQVEQYK 74
Cdd:COG3206 95 VLERVVDKLNLDEDPLGEEASREAAIERLRKnltVEPVKGSNVIEISyTSPDPELAAAVANALAEayLEQNLELRREEAR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 75 KELE------KTYSAKLDNARQSAE--RNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERD 146
Cdd:COG3206 175 KALEfleeqlPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPD 254
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2244985380 147 TSRRLLAekEREMAEMRARMQQQLDEYQELL--------DIKlALDMEIHAYRKLLEGEEERLRLS 204
Cdd:COG3206 255 ALPELLQ--SPVIQQLRAQLAELEAELAELSarytpnhpDVI-ALRAQIAALRAQLQQEAQRILAS 317
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-262 |
3.20e-07 |
|
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: 53.14 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 7 AENRLQTMKEELDFQKNIYSEELRETKRRH---ETRLVEID------NGKQREFESRLAdALQELRAQHEDQVEQYKKEL 77
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVselEEEIEELQkelyalANEISRLEQQKQ-ILRERLANLERQLEELEAQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 78 EKTYSAKLDNARQSAERNsnlvgaahEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDslarERDTSRRLLAEKER 157
Cdd:TIGR02168 326 EELESKLDELAEELAELE--------EKLEELKEELESLEAELEELEAELEELESRLEELEE----QLETLRSKVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 158 EMAEMRARMQQQLDEYQELLDIKLALDMEIHA-YRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQTQGGGSVTKKRKLE 236
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEElLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEA 473
|
250 260
....*....|....*....|....*.
gi 2244985380 237 STESRSSFSQHARTSGRVAVEEVDEE 262
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQE 499
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-200 |
4.33e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 3 RRVDAENRLQTMKEE---LDFQKNIYSEELRETKRRHETRLVEidngkQREFESRLADALQELRAQHEDQVEQyKKELEK 79
Cdd:COG1196 310 RRRELEERLEELEEElaeLEEELEELEEELEELEEELEEAEEE-----LEEAEAELAEAEEALLEAEAELAEA-EEELEE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 80 TYSAKLDNARQSAERNSNLVGAAhEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREM 159
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELE-EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2244985380 160 AEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEER 200
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
44-202 |
1.17e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 44 DNGKQREFESRLADALQELRAQHEDQVEQYKKELEkTYSAKLDNARQSAERNSNL--VGAAHEELQQSRIRIDSL---SA 118
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLAEYSWDEidVASAEREIAELEAELERLdasSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 119 QLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEReMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEE 198
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ-AEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVE 764
|
....
gi 2244985380 199 ERLR 202
Cdd:COG4913 765 RELR 768
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-262 |
1.76e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 3 RRVDAENRLQTMKEELDFQKNI-----------------------YSEELRET-------------KRRHETRLVEIDNG 46
Cdd:TIGR02168 173 RRKETERKLERTRENLDRLEDIlnelerqlkslerqaekaerykeLKAELRELelallvlrleelrEELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 47 KQREFESRLADALQELRAQHEDQVEQYKKELEKtYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQ 126
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEE-LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 127 LAAKEAKLRDLE----------DSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEG 196
Cdd:TIGR02168 332 LDELAEELAELEekleelkeelESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2244985380 197 EEERLRLSPSPTSQRSRgRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEE 262
Cdd:TIGR02168 412 LEDRRERLQQEIEELLK-KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9-201 |
2.96e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 9 NRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQRefesrlADALQELRAQHEDQVEQYKKELEKTySAKLDNA 88
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ------IEQLKEELKALREALDELRAELTLL-NEEAANL 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 89 RQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLAR---ERDTSRRLLAEKEREMAEMRAR 165
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnERASLEEALALLRSELEELSEE 902
|
170 180 190
....*....|....*....|....*....|....*.
gi 2244985380 166 MQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERL 201
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-175 |
5.54e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 3 RRVDAENRLQTMKEELDFQKNIYS------EELRETKRRHETRLVEIDngKQREFESRLADALQELRAQHEDQVEQYKKE 76
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELEsleaelEELEAELEELESRLEELE--EQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 77 LEktySAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARerdtSRRLLAEKE 156
Cdd:TIGR02168 409 LE---RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE----AEQALDAAE 481
|
170 180
....*....|....*....|....*
gi 2244985380 157 REMAEMRAR------MQQQLDEYQE 175
Cdd:TIGR02168 482 RELAQLQARldslerLQENLEGFSE 506
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
29-202 |
9.66e-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: 48.25 E-value: 9.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 29 LRETKRRHETRLVEIDngKQREFESRLADALQELRAQHEDQVEQYKKEL--EKTYSAKLDNARQSAERNSNLVGAAHEEL 106
Cdd:pfam01576 880 LQDEKRRLEARIAQLE--EELEEEQSNTELLNDRLRKSTLQVEQLTTELaaERSTSQKSESARQQLERQNKELKAKLQEM 957
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 107 QqsriridslSAQLSQLQKQLAAKEAKLRDLEDSL---ARERDTSRRLLAEKEREMAEMRARMQ---QQLDEYQELLDiK 180
Cdd:pfam01576 958 E---------GTVKSKFKSSIAALEAKIAQLEEQLeqeSRERQAANKLVRRTEKKLKEVLLQVEderRHADQYKDQAE-K 1027
|
170 180
....*....|....*....|..
gi 2244985380 181 LALDMEiHAYRKLLEGEEERLR 202
Cdd:pfam01576 1028 GNSRMK-QLKRQLEEAEEEASR 1048
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
4-178 |
1.34e-05 |
|
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: 47.58 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 4 RVDAENRLQTMKEEL-----DFQKNIYSEELRETK----RRHETRLVEIDNGKQR---EFESRLAD--ALQELRAQHEDQ 69
Cdd:pfam07888 173 RKQLQAKLQQTEEELrslskEFQELRNSLAQRDTQvlqlQDTITTLTQKLTTAHRkeaENEALLEElrSLQERLNASERK 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 70 VEQYKKELEKTYS------AKLDNAR-QSAERNSNLVGAA-------------HEELQQS----RIRIDSLSAQLSQLQK 125
Cdd:pfam07888 253 VEGLGEELSSMAAqrdrtqAELHQARlQAAQLTLQLADASlalregrarwaqeRETLQQSaeadKDRIEKLSAELQRLEE 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 126 QLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQ-------QQLDEYQELLD 178
Cdd:pfam07888 333 RLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRvaqkekeQLQAEKQELLE 392
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
10-176 |
1.39e-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: 46.46 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 10 RLQTMKEELDfqkniyseELRETKRRHETRLVEIDNgKQREFESRLADALQEL------RAQHEDQVEQYKKELEKtYSA 83
Cdd:COG1579 11 DLQELDSELD--------RLEHRLKELPAELAELED-ELAALEARLEAAKTELedlekeIKRLELEIEEVEARIKK-YEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 84 KLDNAR------------QSAERNsnlVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRL 151
Cdd:COG1579 81 QLGNVRnnkeyealqkeiESLKRR---ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170 180
....*....|....*....|....*.
gi 2244985380 152 LAEKEREMAEMRARMQQQL-DEYQEL 176
Cdd:COG1579 158 LEELEAEREELAAKIPPELlALYERI 183
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
10-199 |
2.72e-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: 46.98 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 10 RLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADalQELRAQHEDQVEQyKKELEKTYsakLDNAR 89
Cdd:TIGR02169 762 ELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSR--IEARLREIEQKLN-RLTLEKEY---LEKEI 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 90 QSAERNSNLVGAAHEELQQsriRIDSLSAQLSQLQKQLAAKEAKLRDLEDS---LARERDTSRRLLAEKEREMAEMRARM 166
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEK---EIENLNGKKEELEEELEELEAALRDLESRlgdLKKERDELEAQLRELERKIEELEAQI 912
|
170 180 190
....*....|....*....|....*....|...
gi 2244985380 167 QQQLDEYQELLDIKLALDMEIHAYRKLLEGEEE 199
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
30-201 |
3.52e-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: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 30 RETKRRHETRLVEIDNGKQREFESRLADALQELRaQHEDQVEQYKKELEKTY------SAKLDNARQSAERNSNLVGAAH 103
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELE-ELEEELEQLRKELEELSrqisalRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 104 EELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLAR---ERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIK 180
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180
....*....|....*....|.
gi 2244985380 181 LALDMEIHAYRKLLEGEEERL 201
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDI 854
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
110-202 |
3.83e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 46.23 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 110 RIRIDSLSAQLSQLQKQLAA----KEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALD- 184
Cdd:COG0542 403 RMEIDSKPEELDELERRLEQleieKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEq 482
|
90 100
....*....|....*....|
gi 2244985380 185 --MEIHAYRKLLEGEEERLR 202
Cdd:COG0542 483 ryGKIPELEKELAELEEELA 502
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
82-177 |
3.95e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 82 SAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARerdtSRRLLAEKEREMAE 161
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA----LEAELAELEKEIAE 94
|
90
....*....|....*.
gi 2244985380 162 MRARMQQQLDEYQELL 177
Cdd:COG4942 95 LRAELEAQKEELAELL 110
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
8-202 |
4.74e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 8 ENRLQTMKEELDFQKNiyseELRETKRRHetRLVEIDNGKQREFE--SRLADALQELRAQH---EDQVEQYKKELEKTYS 82
Cdd:COG3206 181 EEQLPELRKELEEAEA----ALEEFRQKN--GLVDLSEEAKLLLQqlSELESQLAEARAELaeaEARLAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 83 AkldnarQSAERNSNLVGAAHEELQQSRIRIDSLSAQLS-------QLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEK 155
Cdd:COG3206 255 A------LPELLQSPVIQQLRAQLAELEAELAELSARYTpnhpdviALRAQIAALRAQLQQEAQRILASLEAELEALQAR 328
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2244985380 156 EREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLR 202
Cdd:COG3206 329 EASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
27-176 |
4.78e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 27 EELRETKRRHETRLVEIDNgKQREFESRLADA----------LQELRAQHEDQVEQykkelEKTYSAKLDNARQSAERNS 96
Cdd:PRK02224 373 EEAREAVEDRREEIEELEE-EIEELRERFGDApvdlgnaedfLEELREERDELRER-----EAELEATLRTARERVEEAE 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 97 NLV-------------GAAH-EELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLED---------SLARERDTSRRLLA 153
Cdd:PRK02224 447 ALLeagkcpecgqpveGSPHvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDlveaedrieRLEERREDLEELIA 526
|
170 180
....*....|....*....|...
gi 2244985380 154 EKEREMAEMRARMQQQLDEYQEL 176
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAEL 549
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
10-202 |
6.65e-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: 45.44 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 10 RLQTMKEELDFQKNIYSEELRETKRR-HE-TRLVEIDNGKQREFESRLADALQELRAQHEdQVEQYKKELEKTySAKLDN 87
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRlDElSQELSDASRKIGEIEKEIEQLEQEEEKLKE-RLEELEEDLSSL-EQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 88 ARQSaernsnlvgaaheelqqsrirIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARER-DTSRRLLAEKEREMAEMRARM 166
Cdd:TIGR02169 756 VKSE---------------------LKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARL 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2244985380 167 Q-------------QQL-DEYQELLDIKLALDMEIHAYRKLLEGEEERLR 202
Cdd:TIGR02169 815 ReieqklnrltlekEYLeKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
33-176 |
9.66e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 9.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 33 KRRHETRLVEIDNGKQREFESRLADALQELRAQHEdQVEQYKKELEK--TYSAKLDNARQSAERNSNLVGAA--HEELQQ 108
Cdd:COG4717 358 ELEEELQLEELEQEIAALLAEAGVEDEEELRAALE-QAEEYQELKEEleELEEQLEELLGELEELLEALDEEelEEELEE 436
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2244985380 109 SRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSlarerdtsrRLLAEKEREMAEMRARMQQQLDEYQEL 176
Cdd:COG4717 437 LEEELEELEEELEELREELAELEAELEQLEED---------GELAELLQELEELKAELRELAEEWAAL 495
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
59-204 |
1.02e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 59 LQELRAQHEDQVEQYKKELEKTYSAK---LDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLR 135
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKpelNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2244985380 136 DLEDSLARERDTSRRllAEKEREMAEMRARMQ---QQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLS 204
Cdd:COG4717 120 KLEKLLQLLPLYQEL--EALEAELAELPERLEeleERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1-201 |
1.64e-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: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 1 MLRRVDAENRLQTMKEELDFQKNIYsEELRETKRRhetrlveidngkqrefesrlADALQELRAQHEDQVEqykkelekt 80
Cdd:COG4913 217 MLEEPDTFEAADALVEHFDDLERAH-EALEDAREQ--------------------IELLEPIRELAERYAA--------- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 81 ysAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLA------RERDTSRRLLAE 154
Cdd:COG4913 267 --ARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDeleaqiRGNGGDRLEQLE 344
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2244985380 155 KEREMAEM-RARMQQQLDEYQELL-DIKLALDMEIHAYRKLLEGEEERL 201
Cdd:COG4913 345 REIERLEReLEERERRRARLEALLaALGLPLPASAEEFAALRAEAAALL 393
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
67-185 |
1.84e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 43.69 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 67 EDQVEQYKKELEKTYsAKLDNARQsaernsnlvgaAHEELQQSRIRID------SLSAQLSQLQKQLAAKEAKLRDLEDS 140
Cdd:COG3524 176 EDAVRFAEEEVERAE-ERLRDARE-----------ALLAFRNRNGILDpeataeALLQLIATLEGQLAELEAELAALRSY 243
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2244985380 141 L---ARERDTSRRLLAEKEREMAEMRARM---------QQQLDEYQEL-LDIKLALDM 185
Cdd:COG3524 244 LspnSPQVRQLRRRIAALEKQIAAERARLtgasggdslASLLAEYERLeLEREFAEKA 301
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
36-175 |
2.17e-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: 43.59 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 36 HETRLVEIDNGKQREfeSRLADALQELRAQHEDQVEQykkELEKTY-----SAKLDNARQSAERNSnLVGAAHEELQQSR 110
Cdd:pfam09731 227 HLDNVEEKVEKAQSL--AKLVDQYKELVASERIVFQQ---ELVSIFpdiipVLKEDNLLSNDDLNS-LIAHAHREIDQLS 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2244985380 111 IRIDSLSAQLSQ-LQKQLAAKEAKLRDLEDSLARE-----RDTSRRLLAEKEREMAEMRARMQQQLDEYQE 175
Cdd:pfam09731 301 KKLAELKKREEKhIERALEKQKEELDKLAEELSARleevrAADEAQLRLEFEREREEIRESYEEKLRTELE 371
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
6-180 |
2.49e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 6 DAENRLQTMKEELDFQKNIYSEELRETkrrhetrlveIDNGKQREFESRLADALQELraqhedqvEQYKKELEkTYSAKL 85
Cdd:PRK11281 91 QAPAKLRQAQAELEALKDDNDEETRET----------LSTLSLRQLESRLAQTLDQL--------QNAQNDLA-EYNSQL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 86 DNARQSAERNSNLVGAAHEELQQSRIRIDSLSA--------QLSQLQKQLAAKEAKLrDLEDSLARERDTSRRLLAEKER 157
Cdd:PRK11281 152 VSLQTQPERAQAALYANSQRLQQIRNLLKGGKVggkalrpsQRVLLQAEQALLNAQN-DLQRKSLEGNTQLQDLLQKQRD 230
|
170 180
....*....|....*....|...
gi 2244985380 158 EMAEMRARMQQQLDEYQELLDIK 180
Cdd:PRK11281 231 YLTARIQRLEHQLQLLQEAINSK 253
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
8-165 |
3.83e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 8 ENRLQTMKEELDFQKNIYsEELRETKRRHETRLVEID-NGKQREFESRLaDALQELRAQHEDQVEQYKKELEKtYSAKLD 86
Cdd:COG1340 122 EWRQQTEVLSPEEEKELV-EKIKELEKELEKAKKALEkNEKLKELRAEL-KELRKEAEEIHKKIKELAEEAQE-LHEEMI 198
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2244985380 87 NARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKqlaakeaKLRDLEDSLARERDTSRRLLAEKEREMAEMRAR 165
Cdd:COG1340 199 ELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK-------ELRELRKELKKLRKKQRALKREKEKEELEEKAE 270
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
55-163 |
4.40e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 55 LADALQELRAQhEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQS---RIRIDSLSAQLSQLQKQLAAKE 131
Cdd:PRK09039 79 LQDSVANLRAS-LSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSaraLAQVELLNQQIAALRRQLAALE 157
|
90 100 110
....*....|....*....|....*....|....*....
gi 2244985380 132 AKLRDLE----DSLARERDTSRRL---LAEKEREMAEMR 163
Cdd:PRK09039 158 AALDASEkrdrESQAKIADLGRRLnvaLAQRVQELNRYR 196
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
37-195 |
4.45e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 37 ETRLVEIDNgKQREFESRLADALQELRA---QHEDQVEQYKKELEKTYSA--KLDNARQSAERNSNLVGAAHEELQQSRI 111
Cdd:PRK03918 555 KKKLAELEK-KLDELEEELAELLKELEElgfESVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFE 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 112 RIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTsrrllaEKEREMAEMRARMQQ---QLDEYQELLDIKLALDMEIH 188
Cdd:PRK03918 634 ELAETEKRLEELRKELEELEKKYSEEEYEELREEYL------ELSRELAGLRAELEElekRREEIKKTLEKLKEELEERE 707
|
....*..
gi 2244985380 189 AYRKLLE 195
Cdd:PRK03918 708 KAKKELE 714
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
116-177 |
5.86e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.87 E-value: 5.86e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2244985380 116 LSAQLSQLQKQLAAKEAKLRDLEDSLARERDT-SRRLLAEKEREMAEMRARMQQQLDEYQELL 177
Cdd:smart00935 23 LEKEFKKRQAELEKLEKELQKLKEKLQKDAATlSEAAREKKEKELQKKVQEFQRKQQKLQQDL 85
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
52-188 |
7.24e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 52 ESRLADALQELRAQH--EDQVEQYKKELEKTYSAKLD----NARQSAERNSNLVGAAheELQQSRIRIDSLSAQLSQLQK 125
Cdd:COG3096 518 RAQLAELEQRLRQQQnaERLLEEFCQRIGQQLDAAEEleelLAELEAQLEELEEQAA--EAVEQRSELRQQLEQLRARIK 595
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 126 QLAAKEAKLRDLEDSLARERDTSRRLLAEKeremAEMRARMQQQLD-------EYQELLDIKLALDMEIH 188
Cdd:COG3096 596 ELAARAPAWLAAQDALERLREQSGEALADS----QEVTAAMQQLLErereatvERDELAARKQALESQIE 661
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
54-203 |
7.43e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 54 RLADALQELRAQHEdQVEQYKKELEKtYSAKLDNARQsAERNSNLVGAAHEELQQSRIRIDSLSAQ---LSQLQKQLAAK 130
Cdd:COG4717 92 ELQEELEELEEELE-ELEAELEELRE-ELEKLEKLLQ-LLPLYQELEALEAELAELPERLEELEERleeLRELEEELEEL 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2244985380 131 EAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDiklALDMEIHAYRKLLEGEEERLRL 203
Cdd:COG4717 169 EAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE---EAQEELEELEEELEQLENELEA 238
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
116-177 |
7.92e-04 |
|
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: 39.87 E-value: 7.92e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2244985380 116 LSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELL 177
Cdd:pfam03938 24 LEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQEL 85
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
105-201 |
8.28e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 105 ELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLAR---ERDTSRRLLAEKEREMAEMRARM---QQQLD------E 172
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAaktELEDLEKEIKRLELEIEEVEARIkkyEEQLGnvrnnkE 90
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2244985380 173 YQELL--------------DIKLALDMEIHAYRKLLEGEEERL 201
Cdd:COG1579 91 YEALQkeieslkrrisdleDEILELMERIEELEEELAELEAEL 133
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
26-202 |
8.75e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 8.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 26 SEELRETKRRHETRLVEIDNGKQREfesRLADALQELRAqHEDQVEQYKKELEKTYS------------------AKLDN 87
Cdd:COG2433 312 KEDLSVEEKLHLAREYGYDNDHERD---ALAAALKAYDA-YKNKFERVEKKVPPDVDrdevkarvirglsieealEELIE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 88 ARQSAERNSNLVGAAHEElqqsrIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLlaekEREMAEMRARMQ 167
Cdd:COG2433 388 KELPEEEPEAEREKEHEE-----RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERL----ERELSEARSEER 458
|
170 180 190
....*....|....*....|....*....|....*
gi 2244985380 168 QQLDEYQELldikLALDMEIHAYRKLLEGEEERLR 202
Cdd:COG2433 459 REIRKDREI----SRLDREIERLERELEEERERIE 489
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
112-178 |
1.07e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 1.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2244985380 112 RIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKER------EMAEMRARMQQQLDEYQELLD 178
Cdd:PRK09039 54 ALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRlqallaELAGAGAAAEGRAGELAQELD 126
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
7-201 |
1.19e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 7 AENRLQTMKEELDFQKNIYSEELRETKrrhetrlvEIDNgKQREFESRLADALQELRaQHEDQVEQYKKELEKtysakld 86
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTE--------NIEE-LIKEKEKELEEVLREIN-EISSELPELREELEK------- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 87 narqsaernsnlVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRlLAEKEREMAEMRARM 166
Cdd:PRK03918 226 ------------LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKA 292
|
170 180 190
....*....|....*....|....*....|....*...
gi 2244985380 167 QQQL---DEYQELLDIKLALDMEIHAYRKLLEGEEERL 201
Cdd:PRK03918 293 EEYIklsEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
10-201 |
1.29e-03 |
|
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: 41.59 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 10 RLQTMKEELDFQKNIySEELRETKRRHETRLVEIDNGKQREFESRLADALQELraqheDQVEQYKKELEKTYSAKLDNAR 89
Cdd:TIGR02169 202 RLRREREKAERYQAL-LKEKREYEGYELLKEKEALERQKEAIERQLASLEEEL-----EKLTEEISELEKRLEEIEQLLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 90 QSAERNSNLVGaahEELQQSRIRIDSLSAQLSQL----------QKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREM 159
Cdd:TIGR02169 276 ELNKKIKDLGE---EEQLRVKEKIGELEAEIASLersiaekereLEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR 352
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2244985380 160 AEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERL 201
Cdd:TIGR02169 353 DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
27-168 |
1.32e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 27 EELRETKRRHETRLVEIdNGKQREFESRLAD--ALQELRAQHEDQVEQYKKELEKTYS--AKLDNARQSAERNSNLVGAA 102
Cdd:PRK03918 224 EKLEKEVKELEELKEEI-EELEKELESLEGSkrKLEEKIRELEERIEELKKEIEELEEkvKELKELKEKAEEYIKLSEFY 302
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2244985380 103 HEELQQSR---IRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRL--LAEKEREMAEMRARMQQ 168
Cdd:PRK03918 303 EEYLDELReieKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLeeLEERHELYEEAKAKKEE 373
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
6-178 |
1.45e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 39.55 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 6 DAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEkTYSAKL 85
Cdd:pfam01442 4 DSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLE-PYTEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 86 -DNARQSAERNSNLVGAAHEELQQS-RIRIDSLSAQLSQLQKQLAAK-EAKLRDLEDSLARERDTSRRLLAEKERemaEM 162
Cdd:pfam01442 83 rKRLNADAEELQEKLAPYGEELRERlEQNVDALRARLAPYAEELRQKlAERLEELKESLAPYAEEVQAQLSQRLQ---EL 159
|
170
....*....|....*.
gi 2244985380 163 RARMQQQLDEYQELLD 178
Cdd:pfam01442 160 REKLEPQAEDLREKLD 175
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
30-201 |
1.60e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 30 RETKRRHETRLVEIDNGKQREfeSRLADALQELRAQHedQVEQYKKELEKTYSAKLDNA---RQSAERNSNLVGAAHEEL 106
Cdd:PRK04863 499 RELLRRLREQRHLAEQLQQLR--MRLSELEQRLRQQQ--RAERLLAEFCKRLGKNLDDEdelEQLQEELEARLESLSESV 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 107 QQSRIRIDSLSAQLSQLQ---KQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEmrarMQQQLDEYQELldiKLAL 183
Cdd:PRK04863 575 SEARERRMALRQQLEQLQariQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEY----MQQLLEREREL---TVER 647
|
170
....*....|....*...
gi 2244985380 184 DmEIHAYRKLLEGEEERL 201
Cdd:PRK04863 648 D-ELAARKQALDEEIERL 664
|
|
| COG0610 |
COG0610 |
Type I site-specific restriction-modification system, R (restriction) subunit and related ... |
5-200 |
1.77e-03 |
|
Type I site-specific restriction-modification system, R (restriction) subunit and related helicases ... [Defense mechanisms];
Pssm-ID: 440375 [Multi-domain] Cd Length: 936 Bit Score: 41.01 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 5 VDAENRLQTMKEELDFQKNIYSEElretkrrhetrlVEIDNGKQREFESRLADALQELRAQHEDQVEQYK--KELEKTYS 82
Cdd:COG0610 674 TDPEEALEELKEALDELRALFPEG------------VDFSAFDPTEKLEALDEAVERFLGDEEARKEFKKlfKELSRLYN 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 83 AkldnARQSAErnsnLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAK--EAKLRDL-EDSLARERDTSRRLLAEKEREM 159
Cdd:COG0610 742 L----LSPDDE----FGDLELEKYRDDVSFYLALRAKLRKLGEKLDLKeyEEKIRQLlDEAIDLERKEIKPRIKQNPVQY 813
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2244985380 160 AEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEER 200
Cdd:COG0610 814 RKFSELLEEIIEEYNNGALDADEVLEELEELAKEVKEEEER 854
|
|
| LCD1 |
pfam09798 |
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. ... |
116-242 |
2.53e-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: 40.38 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 116 LSAQLSQLQKQLAAKEAKLRDLEDSLARerdtsrrllaEKEREMAEMRArmqqqldEYQELLDIKLALDMEIhayRKLle 195
Cdd:pfam09798 2 LRDKLELLQQEKEKELEKLKNSYEELKS----------SHEEELEKLKQ-------EVQKLEDEKKFLLNEL---RSL-- 59
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2244985380 196 geeerlrLSPSPTSQRSRGRASSHSSQtqgggSVTKKRKLESTESRS 242
Cdd:pfam09798 60 -------SATSPASSQSHETDTDDSSS-----VSLKKRKIEESTAES 94
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
71-239 |
3.12e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.04 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 71 EQYKKELEKTYSAKLDN------ARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARE 144
Cdd:PRK10929 26 KQITQELEQAKAAKTPAqaeiveALQSALNWLEERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 145 R------DTSRRLLaEKEREmaemrarMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSqrSRGRASS 218
Cdd:PRK10929 106 AleqeilQVSSQLL-EKSRQ-------AQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNT--PLAQAQL 175
|
170 180
....*....|....*....|.
gi 2244985380 219 HSSQTQgggSVTKKRKLESTE 239
Cdd:PRK10929 176 TALQAE---SAALKALVDELE 193
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
9-178 |
3.15e-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: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 9 NRLQTMKEELDFQKNIYSEE----------LRETKRRHETRLVEID--NGKQREFESRLADaLQELRAQHEDQVEQYKKE 76
Cdd:TIGR04523 162 NDLKKQKEELENELNLLEKEklniqknidkIKNKLLKLELLLSNLKkkIQKNKSLESQISE-LKKQNNQLKDNIEKKQQE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 77 LEKTySAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSlaRERDTSRRL---LA 153
Cdd:TIGR04523 241 INEK-TTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ--KEQDWNKELkseLK 317
|
170 180
....*....|....*....|....*
gi 2244985380 154 EKEREMAEmrarMQQQLDEYQELLD 178
Cdd:TIGR04523 318 NQEKKLEE----IQNQISQNNKIIS 338
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
115-200 |
4.04e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.18 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 115 SLSAQLSQLQKQLAAKEA---KLRDLEDSLARERDTSRRLLAEKEREMAEMR---ARMQQQLdeyqELLDIKL-ALDMEI 187
Cdd:PRK09039 78 DLQDSVANLRASLSAAEAersRLQALLAELAGAGAAAEGRAGELAQELDSEKqvsARALAQV----ELLNQQIaALRRQL 153
|
90
....*....|...
gi 2244985380 188 HAYRKLLEGEEER 200
Cdd:PRK09039 154 AALEAALDASEKR 166
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
35-195 |
4.42e-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: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 35 RHETRLVEIDNGKQREfesRLADALQELRAQHEDQveqykkELEKTYSAKLDNARqsaernsnlvgAAHEElQQSRIRID 114
Cdd:pfam05483 178 REETRQVYMDLNNNIE---KMILAFEELRVQAENA------RLEMHFKLKEDHEK-----------IQHLE-EEYKKEIN 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 115 SLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLL 194
Cdd:pfam05483 237 DKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALE 316
|
.
gi 2244985380 195 E 195
Cdd:pfam05483 317 E 317
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
64-137 |
6.30e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.66 E-value: 6.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2244985380 64 AQHEDQVEQYKKELEKTySAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDL 137
Cdd:COG3883 19 QAKQKELSELQAELEAA-QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
37-181 |
6.42e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.17 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 37 ETRLVEIDNGKQREFESRLADALQELRaQHEDQVEQYKK---ELEKTYSAKLDNARQSAERNSNL-----VGAA------ 102
Cdd:PRK04863 983 NSDLNEKLRQRLEQAEQERTRAREQLR-QAQAQLAQYNQvlaSLKSSYDAKRQMLQELKQELQDLgvpadSGAEerarar 1061
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 103 ----HEELQQSRIRIDSLSAQLS-------QLQKQLAAKEAKLRDLEDS-------------LARERDTSRRLLAekeRE 158
Cdd:PRK04863 1062 rdelHARLSANRSRRNQLEKQLTfceaemdNLTKKLRKLERDYHEMREQvvnakagwcavlrLVKDNGVERRLHR---RE 1138
|
170 180
....*....|....*....|...
gi 2244985380 159 MAEMRArmqqqlDEYQELLDIKL 181
Cdd:PRK04863 1139 LAYLSA------DELRSMSDKAL 1155
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1-267 |
7.51e-03 |
|
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: 38.95 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 1 MLRRVDAENRLQTMKEELDFQKNIYSEELR---ETKR-----RHETRLVEIDNGKQREFESRLAD--ALQELRAQHEDQV 70
Cdd:pfam17380 312 VERRRKLEEAEKARQAEMDRQAAIYAEQERmamEREReleriRQEERKRELERIRQEEIAMEISRmrELERLQMERQQKN 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 71 EQYKKELEKTYSAKLdnarQSAERnsnlvgaaHEELQQSRIRIDSLSAQlsqlqkQLAAKEAKLRDLEDSLARERDTSRR 150
Cdd:pfam17380 392 ERVRQELEAARKVKI----LEEER--------QRKIQQQKVEMEQIRAE------QEEARQREVRRLEEERAREMERVRL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 151 LLAEKEREMAEMRA----RMQQQLDEYQELLDIKLA-------LDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRASSH 219
Cdd:pfam17380 454 EEQERQQQVERLRQqeeeRKRKKLELEKEKRDRKRAeeqrrkiLEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE 533
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2244985380 220 SSQTqgggSVTKKRKLESTESRSSFSQHAR--TSGRVAVEEVDEEGKFVR 267
Cdd:pfam17380 534 RRRE----AEEERRKQQEMEERRRIQEQMRkaTEERSRLEAMEREREMMR 579
|
|
| PRK10920 |
PRK10920 |
putative uroporphyrinogen III C-methyltransferase; Provisional |
98-166 |
7.76e-03 |
|
putative uroporphyrinogen III C-methyltransferase; Provisional
Pssm-ID: 236795 Cd Length: 390 Bit Score: 38.54 E-value: 7.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2244985380 98 LVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARM 166
Cdd:PRK10920 54 LYYHGKQQAQNQTATNDALANQLTALQKAQESQKQELEGILKQQAKALDQANRQQAALAKQLDELQQKV 122
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
67-138 |
7.90e-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: 38.39 E-value: 7.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2244985380 67 EDQVEQYKKELEKTYsAKLDNARQSAERNSNLVG---AAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLE 138
Cdd:COG0845 60 QAALAQAQAQLAAAQ-AQLELAKAELERYKALLKkgaVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTT 133
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
9-186 |
7.92e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 9 NRLQTMKEELDFQKNIYSE--ELRETKRRHETRLVEIDNgKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLD 86
Cdd:COG4717 71 KELKELEEELKEAEEKEEEyaELQEELEELEEELEELEA-ELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 87 NARQsaernsnlvgaAHEELQQSRIRIDSLSAQLSQLQKQLAAKE-----AKLRDLEDsLARERDTSRRLLAEKEREMAE 161
Cdd:COG4717 150 ELEE-----------RLEELRELEEELEELEAELAELQEELEELLeqlslATEEELQD-LAEELEELQQRLAELEEELEE 217
|
170 180
....*....|....*....|....*
gi 2244985380 162 MRARMQQQLDEYQELLDIKLALDME 186
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALE 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3-201 |
8.08e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 3 RRVDAENRLQTMKEELDFQKNIYSE--ELRETKRRHETRLVEIDNGKQREfesrladalQELRAQHE--DQVEQYKKELE 78
Cdd:PRK03918 443 RELTEEHRKELLEEYTAELKRIEKElkEIEEKERKLRKELRELEKVLKKE---------SELIKLKElaEQLKELEEKLK 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 79 KTYSAKLdnarqsaERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQ---KQLAAKEAKLRDLEDSLARERDTSRRLLAEK 155
Cdd:PRK03918 514 KYNLEEL-------EKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelkKKLAELEKKLDELEEELAELLKELEELGFES 586
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2244985380 156 EREMAEMRARMQQQLDEYQELLDIKlaldMEIHAYRKLLEGEEERL 201
Cdd:PRK03918 587 VEELEERLKELEPFYNEYLELKDAE----KELEREEKELKKLEEEL 628
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
67-224 |
8.32e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 38.17 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 67 EDQVEQYKKELektysAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARerd 146
Cdd:pfam00529 57 QAALDSAEAQL-----AKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 147 tsRRLLAEK----EREMAEMRARMQQQLDEY----QELLDIKLALDMEIHAYRKLLEGEEERLRLSPSpTSQRSRGRASS 218
Cdd:pfam00529 129 --RRVLAPIggisRESLVTAGALVAQAQANLlatvAQLDQIYVQITQSAAENQAEVRSELSGAQLQIA-EAEAELKLAKL 205
|
....*.
gi 2244985380 219 HSSQTQ 224
Cdd:pfam00529 206 DLERTE 211
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
11-154 |
8.70e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 38.07 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 11 LQTMKEELDFQKNIYSEELRETKRrHETRLVEIdNGKQREFESRLADALQELRaQHEDQVEQYKKELEKTYSAKLDNARQ 90
Cdd:smart00787 142 LEGLKEGLDENLEGLKEDYKLLMK-ELELLNSI-KPKLRDRKDALEEELRQLK-QLEDELEDCDPTELDRAKEKLKKLLQ 218
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2244985380 91 SAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEaklRDLEDSLARERDTSRRLLAE 154
Cdd:smart00787 219 EIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAE---KKLEQCRGFTFKEIEKLKEQ 279
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
47-130 |
9.68e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 36.26 E-value: 9.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 47 KQREFESRLADA---LQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERnsnLVGAAHEELQQSRIR-IDSLSAQLSQ 122
Cdd:cd06503 45 AKEEAEELLAEYeekLAEARAEAQEIIEEARKEAEKIKEEILAEAKEEAER---ILEQAKAEIEQEKEKaLAELRKEVAD 121
|
....*...
gi 2244985380 123 LQKQLAAK 130
Cdd:cd06503 122 LAVEAAEK 129
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
59-202 |
9.71e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.22 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985380 59 LQELRAQHEDQVEQYKKELEKTYSAKLDNARqsaERNSNLVGAAHEELQQSRiridslsAQLSQLQKQLAAKEAKLRDLE 138
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKEALLEAK---EEIHKLRNEFEKELRERR-------NELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2244985380 139 DSLARER---DTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEiHAYRKLLEGEEERLR 202
Cdd:PRK12704 103 ELLEKREeelEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE-EAKEILLEKVEEEAR 168
|
|
| |
