|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
12-281 |
1.80e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.08 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 12 RLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDEARAgqlsehrKLEALQVALQEERQawikQEHQLKERLQALQEE 91
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRL-------ELEELELELEEAQA----EEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 92 GQAQLEREKGNSQREAQAAWE---TQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAVQLE 168
Cdd:COG1196 304 IARLEERRRELEERLEELEEElaeLEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 169 QRVTERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQELAAQLAQfKVEMADREERQQQVAQDYELRLAREQARVRDLK 248
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA-LAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260 270
....*....|....*....|....*....|...
gi 1907081119 249 SGNQQLEEQRAELVERLQAMLQAHWEEANQLLS 281
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-312 |
3.30e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.84 E-value: 3.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 2 EALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQawikQEHQL 81
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE----RRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 82 KERLQALQEEGQAQLEREKGNSQREAQAawetQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRiqmES 161
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEEL----EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA---EE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 162 ELAVQLEQRVTERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQELAAQLAQFKVEMADREERQQQvaqdyELRLAREQ 241
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL-----EEEEEALL 462
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081119 242 ARVRDLKSGNQQLEEQRAELVERLQAMLQAHWEEANQLLSTTLLPPNPQAPLAEPSSPGpLEPEKGERRTW 312
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG-LAGAVAVLIGV 532
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-284 |
7.57e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.60 E-value: 7.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 1 MEALSREQEGARLQQREKEA----LEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQawik 76
Cdd:COG1196 248 LEELEAELEELEAELAELEAeleeLRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE---- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 77 QEHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMS--LVQARYES 154
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRaaAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 155 QRIQMESELAVQLEQRVTERLAEAQEnsLRQAASLRDHHRKQLQELSGQHQQELAAQLAQFKVEMADREERQQQVAQDYE 234
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEA--LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1907081119 235 LRLAREQARVRDLKsgnqqLEEQRAELVERLQAMLQAHWEEANQLLSTTL 284
Cdd:COG1196 482 LLEELAEAAARLLL-----LLEAEADYEGFLEGVKAALLLAGLRGLAGAV 526
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-267 |
6.83e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.52 E-value: 6.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 2 EALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQL 81
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 82 KERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQ------TEVRRLEGDLDTVRRERDALQLEMSLVQARYESQ 155
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLErlerleEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 156 RIQMESELAVQLEQRVTERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQELAAQLAQFKVEMADREERQQQVAQ--DY 233
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgvEA 534
|
250 260 270
....*....|....*....|....*....|....
gi 1907081119 234 ELRLAREQARVRDLKSGNQQLEEQRAELVERLQA 267
Cdd:COG1196 535 AYEAALEAALAAALQNIVVEDDEVAAAAIEYLKA 568
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
24-285 |
5.39e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.44 E-value: 5.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 24 ERQALTLRLEVEQ-QQCRTLQEERDEARAG-QLSEHRKLEALQVALQEErqawIKQEHQLKERLQALQEEGQAQLEREKG 101
Cdd:COG1196 199 ERQLEPLERQAEKaERYRELKEELKELEAElLLLKLRELEAELEELEAE----LEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 102 NSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDAL-----QLEMSLVQARYESQRIQMESELAVQLEQRVTERLA 176
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELeerleELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 177 EAQENSLRQAASLRDHHRKQLQELSG--QHQQELAAQLAQfKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQL 254
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEEleELAEELLEALRA-AAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
250 260 270
....*....|....*....|....*....|.
gi 1907081119 255 EEQRAELVERLQAMLQAHWEEANQLLSTTLL 285
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-284 |
1.71e-14 |
|
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: 77.02 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 3 ALSREQEGARLQQrEKEALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAwIKQEHQLK 82
Cdd:TIGR02168 672 ILERRREIEELEE-KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-VEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 83 ERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESE 162
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 163 L--AVQLEQRVTERLAEAQENSLRQAASlrDHHRKQLQELSGQHQQELAAQLAQFKVEMADREERqqqvaqdyELRLARE 240
Cdd:TIGR02168 830 ErrIAATERRLEDLEEQIEELSEDIESL--AAEIEELEELIEELESELEALLNERASLEEALALL--------RSELEEL 899
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907081119 241 QARVRDLKSGNQQLEEQRAELVERLQAMlQAHWEEANQLLSTTL 284
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQL-ELRLEGLEVRIDNLQ 942
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-279 |
1.50e-13 |
|
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: 73.94 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 1 MEALSREQEGARLQQREKEALEE-ERQALTLRLEVEQQQCRTLQEERDEARagqlSEHRKLEALQVALQEERQAWIKQEH 79
Cdd:TIGR02168 202 LKSLERQAEKAERYKELKAELRElELALLVLRLEELREELEELQEELKEAE----EELEELTAELQELEEKLEELRLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 80 QLKERLQALQEEGQAQLEREKGNSQREAqaawETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQM 159
Cdd:TIGR02168 278 ELEEEIEELQKELYALANEISRLEQQKQ----ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 160 ESELAVQleqrvtERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQE--LAAQLAQFKVEMADREERQQQVAQDYE-LR 236
Cdd:TIGR02168 354 ESLEAEL------EELEAELEELESRLEELEEQLETLRSKVAQLELQIasLNNEIERLEARLERLEDRRERLQQEIEeLL 427
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907081119 237 LAREQARVRDLKSGNQQLEEQRAELVERLQAMLQAHWEEANQL 279
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
15-267 |
2.02e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 70.33 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 15 QREKEALEEERQALTLRLEVEQQQCRTLQEERDEARAgQLSEHRKLEALQvALQEERQAWIKQEHQLKERLQALQEEGQ- 93
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQE-RREALQRLAEYS-WDEIDVASAEREIAELEAELERLDASSDd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 94 -AQLEREKGNSQREAQAAwetQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYES-QRIQMESELAVQLEQRV 171
Cdd:COG4913 687 lAALEEQLEELEAELEEL---EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLRALLEERFAAALGDAV 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 172 TERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQELAAQLAQFKVEMADREERQQQVAQDYELRLAREQARVRDLKsgN 251
Cdd:COG4913 764 ERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGLPEYEERFKELL--N 841
|
250
....*....|....*.
gi 1907081119 252 QQLEEQRAELVERLQA 267
Cdd:COG4913 842 ENSIEFVADLLSKLRR 857
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
44-270 |
1.25e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.55 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 44 EERD-EARAGQLSEH-RKLEALQVALQEERQawikQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQ 121
Cdd:COG4913 219 EEPDtFEAADALVEHfDDLERAHEALEDARE----QIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 122 TEVRRLEGDLDTVRRERDALQLEMSLVQARYEsqriqmesELAVQLEQRVTERLA--EAQENSLRQAASLRDHHRKQLQE 199
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELD--------ELEAQIRGNGGDRLEqlEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081119 200 LSGQHQQELAAQLAQFkvemADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQAMLQ 270
Cdd:COG4913 367 LLAALGLPLPASAEEF----AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-268 |
1.58e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 2 EALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQL 81
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 82 KERLQALQEEGQAQ------LEREKGNSQREAQAAWETQQQfalLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQ 155
Cdd:TIGR02168 788 EAQIEQLKEELKALrealdeLRAELTLLNEEAANLRERLES---LERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 156 RIQ---MESELAVQLEQR-VTERLAEAQENSLRQAASLRDHHRKQLQELSGQHqQELAAQLAQFKVEMA----DREERQQ 227
Cdd:TIGR02168 865 EELieeLESELEALLNERaSLEEALALLRSELEELSEELRELESKRSELRREL-EELREKLAQLELRLEglevRIDNLQE 943
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1907081119 228 QVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQAM 268
Cdd:TIGR02168 944 RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2-225 |
7.57e-09 |
|
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: 57.85 E-value: 7.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 2 EALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDEARagqlsehRKLEALQVALQEERQAWIKQEHQL 81
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE-------AELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 82 KERLQALQEEGQAQLEREKGNSQREAQAAWetqqQFALLQTEVRRLEGDLDTVRRERDALQlemsLVQARYESQRIQMES 161
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAVR----RLQYLKYLAPARREQAEELRADLAELA----ALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081119 162 ELAVQLEQRVT-ERLAEAQENSLRQAASLRDHHRKQLQELSGQhQQELAAQLAQFKVEMADREER 225
Cdd:COG4942 179 LLAELEEERAAlEALKAERQKLLARLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-264 |
7.67e-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: 58.93 E-value: 7.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 2 EALSREQEGARLQ----QREKEALEEERQALTLRLEVEQQQCRTLQEERD--EARAGQlSEHRKLEALQVALQEERQAW- 74
Cdd:TIGR02169 733 EKLKERLEELEEDlsslEQEIENVKSELKELEARIEELEEDLHKLEEALNdlEARLSH-SRIPEIQAELSKLEEEVSRIe 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 75 ---------IKQEHQLKERLQALQEEGQAQLE--REKGNSQREAQAAW-----ETQQQFALLQTEVRRLEGDLDTVRRER 138
Cdd:TIGR02169 812 arlreieqkLNRLTLEKEYLEKEIQELQEQRIdlKEQIKSIEKEIENLngkkeELEEELEELEAALRDLESRLGDLKKER 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 139 DALQLEMSLVQARYESQRIQMEselavQLEQRVtERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQE-LAAQLAQFKV 217
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIE-----KKRKRL-SELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEdVQAELQRVEE 965
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1907081119 218 EMADREERQQQVAQDYElrlaREQARVRDLKSGNQQLEEQRAELVER 264
Cdd:TIGR02169 966 EIRALEPVNMLAIQEYE----EVLKRLDELKEKRAKLEEERKAILER 1008
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
7-316 |
1.36e-08 |
|
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: 57.83 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 7 EQEGARLQQREKEALEEERQALTLRLEveqQQCRTLQEERDEARAGQLSEHRKLEALQValqeERQawiKQEHQLKERLQ 86
Cdd:pfam17380 330 DRQAAIYAEQERMAMERERELERIRQE---ERKRELERIRQEEIAMEISRMRELERLQM----ERQ---QKNERVRQELE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 87 ALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDldtvrRERdalqlEMSLVQARYESQRIQMEsELAVQ 166
Cdd:pfam17380 400 AARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEE-----RAR-----EMERVRLEEQERQQQVE-RLRQQ 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 167 LEQRVTERLAEAQENSLRQAAslRDHHRKQLQELSGQHQQELAAQLAQFKVEMADREERQQQVAQDYELRLAREQARVRD 246
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRA--EEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQ 546
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081119 247 LKSGNQQLEEQRAELVE---RLQAMlqahwEEANQLLSTTLLPPNPQAPLAEPSSPGPLEPEKGERRTWAMPP 316
Cdd:pfam17380 547 EMEERRRIQEQMRKATEersRLEAM-----EREREMMRQIVESEKARAEYEATTPITTIKPIYRPRISEYQPP 614
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-278 |
5.84e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 2 EALSREQEGARLQQREKEALEEERQALTLRLEVEQQ----QCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQ 77
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKkkadEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK 1553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 78 EHQLKERLQALQEEGQAQLEREKGNSQREAQAAwetqqqfalLQTEVRRLEGDLDTVRRERdalqlEMSLVQARY-ESQR 156
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA---------KKAEEARIEEVMKLYEEEK-----KMKAEEAKKaEEAK 1619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 157 IQMESELAVQLEQRVTERLAEAQENSLRQAASLRdhhrkQLQELSGQHQQELA--AQLAQFKVEMADREERQQQVAQDYE 234
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK-----KAEEENKIKAAEEAkkAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907081119 235 LRLAREQARVRDLKSGNQQlEEQRAELVERLQAMLQAHWEEANQ 278
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAE-EKKKAEELKKAEEENKIKAEEAKK 1737
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
58-267 |
6.89e-08 |
|
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: 54.77 E-value: 6.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 58 RKLEALQVALQEERQAWIKQEHQLKERLQALQeegqaQLEREKGNSQREAQaawETQQQFALLQTEVRRLEGDLDTVRRE 137
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLA-----ALERRIAALARRIR---ALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 138 RDALQLEMS-LVQARYESQRIQ-----MESELAVQLEQRVT--ERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQ--E 207
Cdd:COG4942 99 LEAQKEELAeLLRALYRLGRQPplallLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAEleA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 208 LAAQLAQFKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQA 267
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
9-287 |
1.11e-07 |
|
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: 55.23 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 9 EGARLQQREK--EALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEAlqvALQEERQAWIKQEHQLKERLQ 86
Cdd:pfam12128 242 EFTKLQQEFNtlESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDD---QWKEKRDELNGELSAADAAVA 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 87 ALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEvrrlegdLDTVRRERDALQLEMSLVQARYESQRIQMESELAVQ 166
Cdd:pfam12128 319 KDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSE-------LENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRD 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 167 LEqRVTERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQ----------ELAAQLAQFKVEMAD----REERQQQVAQD 232
Cdd:pfam12128 392 IA-GIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAgklefneeeyRLKSRLGELKLRLNQatatPELLLQLENFD 470
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081119 233 YELRLAREQ-----ARVRDLKSGNQQLEEQRAELVERLQAMLQAHWEEANQL--LSTTLLPP 287
Cdd:pfam12128 471 ERIERAREEqeaanAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALdeLELQLFPQ 532
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2-271 |
3.92e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.44 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 2 EALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEER----DEARAGQLSEHRKLEALQVALQEERQAWIKQ 77
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEElkllAKEEEELKSELLKLERRKVDDEEKLKESEKE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 78 EHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQaryESQRI 157
Cdd:pfam02463 323 KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE---EELEL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 158 QMESELAVQLEQRVTERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQELAAQLAQFKVEMADREERQQQVAQDYELRL 237
Cdd:pfam02463 400 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479
|
250 260 270
....*....|....*....|....*....|....*
gi 1907081119 238 -AREQARVRDLKSGNQQLEEQRAELVERLQAMLQA 271
Cdd:pfam02463 480 vKLQEQLELLLSRQKLEERSQKESKARSGLKVLLA 514
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
10-275 |
4.09e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.44 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 10 GARLQQREKEALEEERQA-------LTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLK 82
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEEtenlaelIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 83 ERLQALQEEGQAQLEREKGNS----QREAQAAWETQQQ-------------FALLQTEVRRLEGDLDTVRRERDALQLEM 145
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEeklaQVLKENKEEEKEKklqeeelkllakeEEELKSELLKLERRKVDDEEKLKESEKEK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 146 SLVQARYESQRIQMESELAVQLEQRVTERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQELAAQLAQFKVEMADREER 225
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907081119 226 QQQV-AQDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQAMLQAHWEE 275
Cdd:pfam02463 404 EKEAqLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELE 454
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
4-279 |
5.90e-07 |
|
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: 52.65 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 4 LSREQEGARLQ---QREKEALEEerqaLTLRLEVEQQQCRTLQEERDEARA-------------GQLSEH-RKLEALQ-- 64
Cdd:COG3096 336 LNLVQTALRQQekiERYQEDLEE----LTERLEEQEEVVEEAAEQLAEAEArleaaeeevdslkSQLADYqQALDVQQtr 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 65 -VALQEERQAWIKQEHQL----------KERLQALQEEGQAQLEREKGNSQREAQAAwETQQQFALLQTEVRRLEGDLDT 133
Cdd:COG3096 412 aIQYQQAVQALEKARALCglpdltpenaEDYLAAFRAKEQQATEEVLELEQKLSVAD-AARRQFEKAYELVCKIAGEVER 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 134 VRRERDALQLemslvQARYESQRIQMESELAVQLEQRVTERLAEAQENSLRQAASLRDHHRKQLqelsgQHQQELAAQLA 213
Cdd:COG3096 491 SQAWQTAREL-----LRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQL-----DAAEELEELLA 560
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081119 214 QFKvemADREERQQQVAQDYELRLAREQARvrdlksgnQQLEEQRAELVERLQAMLQAHwEEANQL 279
Cdd:COG3096 561 ELE---AQLEELEEQAAEAVEQRSELRQQL--------EQLRARIKELAARAPAWLAAQ-DALERL 614
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
65-271 |
6.07e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 65 VALQEERQAWIKQEHQLKERLQALQEEgQAQLEREKGNSQREAQAAwetQQQFALLQTEVRRLEGDLDTVRRERDALQLE 144
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKE-LAALKKEEKALLKQLAAL---ERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 145 MSLVQARYESQRIQMESELAV--QLEQRVTERLAEAQENSLRQAASLR------DHHRKQLQELSGQHQ--QELAAQLAQ 214
Cdd:COG4942 92 IAELRAELEAQKEELAELLRAlyRLGRQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAelAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 215 FKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAEL---VERLQAMLQA 271
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELqqeAEELEALIAR 231
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
108-279 |
6.90e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 6.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 108 QAAWETQQQFALLQtEVRRLEGDLDTVRRERDALQLEMSLVQAryesQRIQMESELAVQLEQRVTERLAEAQEnSLRQAA 187
Cdd:COG4913 242 EALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRL----WFAQRRLELLEAELEELRAELARLEA-ELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 188 SLRDHHRKQLQELSGQHQQELAAQLAQFKVEMADREERQQQVAQdyelRLAREQARVRDLKSGNQQLEEQRAELVERLQA 267
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERER----RRARLEALLAALGLPLPASAEEFAALRAEAAA 391
|
170
....*....|..
gi 1907081119 268 MLQAHWEEANQL 279
Cdd:COG4913 392 LLEALEEELEAL 403
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
22-268 |
7.22e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 7.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 22 EEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKERLQALQEEGQAQLEREKG 101
Cdd:COG1196 534 AAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 102 NSQREAQAAWETQQQFALLQTEVRRLEGdLDTVRRERDALQLEMSLVQARYESQRIQMESELAVQLEQRVTERLAEAQEN 181
Cdd:COG1196 614 RYYVLGDTLLGRTLVAARLEAALRRAVT-LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 182 SLRQAASLRDHHRKQLQELSGQHQQELAAQLAQFKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAEL 261
Cdd:COG1196 693 LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL 772
|
....*..
gi 1907081119 262 VERLQAM 268
Cdd:COG1196 773 EREIEAL 779
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
6-189 |
8.04e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 6 REQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDEARAgQLSEHRKLEALQVALQEERQAWIKQEhQLKERL 85
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE-ELEKLEKLLQLLPLYQELEALEAELA-ELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 86 QALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMEsELAV 165
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE-ELEE 227
|
170 180
....*....|....*....|....
gi 1907081119 166 QLEQRVTERLAEAQENSLRQAASL 189
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARLL 251
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-165 |
9.55e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 2 EALSREQEGARLQQREKEALEEERQALTL--------RLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQA 73
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAqirgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 74 WIKQEHQLKERLQALQEEGQAQlerekgnsqreaqaawetQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYE 153
Cdd:COG4913 382 FAALRAEAAALLEALEEELEAL------------------EEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
170
....*....|..
gi 1907081119 154 SQRIQMESELAV 165
Cdd:COG4913 444 ALRDALAEALGL 455
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
15-279 |
1.12e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 15 QREKEALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEhrklEALQVALQEERQAWIKQEHQLKERLQALQEEGQA 94
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD----DADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 95 ---QLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQME-----SELAVQ 166
Cdd:PRK02224 340 hneEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGnaedfLEELRE 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 167 LEQRVTERLAEAQ------ENSLRQAASLRDH--------------HRKQLQELSGQhQQELAAQLAQFKVEMADREERQ 226
Cdd:PRK02224 420 ERDELREREAELEatlrtaRERVEEAEALLEAgkcpecgqpvegspHVETIEEDRER-VEELEAELEDLEEEVEEVEERL 498
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1907081119 227 QQVAQDYElrLAREQARVRDLKSGNQQLEEQRAELVERLQAMLQAHWEEANQL 279
Cdd:PRK02224 499 ERAEDLVE--AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAEL 549
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
4-279 |
1.43e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 4 LSREQEGARLQQREKEAlEEERQALTLRLEvEQQQCRTL-QEERDEARA-------------GQLSEH-RKLEALQV-AL 67
Cdd:PRK04863 337 LNLVQTALRQQEKIERY-QADLEELEERLE-EQNEVVEEaDEQQEENEAraeaaeeevdelkSQLADYqQALDVQQTrAI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 68 Q--------EERQAWIKQEHQLKERLQALQEEGQAQLE------REKGNSQREAQAAwetQQQFALLQTEVRRLEGDLDT 133
Cdd:PRK04863 415 QyqqavqalERAKQLCGLPDLTADNAEDWLEEFQAKEQeateelLSLEQKLSVAQAA---HSQFEQAYQLVRKIAGEVSR 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 134 VRRERDALQLEmslvqARYESQRIQmeselAVQLEQRvterlaEAQENSLRQAASLRDHHRKQLQELSGQHQQEL--AAQ 211
Cdd:PRK04863 492 SEAWDVARELL-----RRLREQRHL-----AEQLQQL------RMRLSELEQRLRQQQRAERLLAEFCKRLGKNLddEDE 555
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081119 212 LAQFKVEM-ADREERQQQVAQDYELRLAREQARvrdlksgnQQLEEQRAELVERLQAMLQAHwEEANQL 279
Cdd:PRK04863 556 LEQLQEELeARLESLSESVSEARERRMALRQQL--------EQLQARIQRLAARAPAWLAAQ-DALARL 615
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
64-267 |
1.52e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 64 QVALQEERQAWIKQEhqLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQL 143
Cdd:TIGR02169 181 EVEENIERLDLIIDE--KRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 144 EMSLVQARYESQRIQMEsELAVQLEQRVTERLAEAQENSLRQAASLRDHHRKqlQELSGQHQQELAAQLAQFKVEMadre 223
Cdd:TIGR02169 259 EISELEKRLEEIEQLLE-ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERS--IAEKERELEDAEERLAKLEAEI---- 331
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907081119 224 ERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQA 267
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1-279 |
1.76e-06 |
|
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: 51.38 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 1 MEALSREQEGARLQQREKEALEEERQALT------------LRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQ 68
Cdd:pfam12128 339 IETAAADQEQLPSWQSELENLEERLKALTgkhqdvtakynrRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 69 EERQAWIKQEHQLKERLQALQEEGQAQLEREKGNsQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLV 148
Cdd:pfam12128 419 ALESELREQLEAGKLEFNEEEYRLKSRLGELKLR-LNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQA 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 149 QARYESQRIQMESELAVQLEQRvtERLAEAQENSLRQAASLRDHHRKQLQELSgQHQQELA--AQLAQFKVEMADREERQ 226
Cdd:pfam12128 498 RKRRDQASEALRQASRRLEERQ--SALDELELQLFPQAGTLLHFLRKEAPDWE-QSIGKVIspELLHRTDLDPEVWDGSV 574
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1907081119 227 QQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQAMLQAHWEEANQL 279
Cdd:pfam12128 575 GGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQL 627
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
12-279 |
1.79e-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: 51.21 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 12 RLQQREKEA---LEEERQALT----LRLEVEQQQcRTLQEERDEARagqlsehrKLEALQVALQE-ERQAWIKQEHQLKE 83
Cdd:TIGR02168 169 KYKERRKETerkLERTRENLDrledILNELERQL-KSLERQAEKAE--------RYKELKAELRElELALLVLRLEELRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 84 RLQALQEEGQaqlerekgnsqreaqaawETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMEsel 163
Cdd:TIGR02168 240 ELEELQEELK------------------EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS--- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 164 avQLEQRVtERLAEAQENSLRQAASLRDhhrkQLQELsGQHQQELAAQLAQfkveMADREERQQQVAQDYELRLAREQAR 243
Cdd:TIGR02168 299 --RLEQQK-QILRERLANLERQLEELEA----QLEEL-ESKLDELAEELAE----LEEKLEELKEELESLEAELEELEAE 366
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907081119 244 VRDLKSGNQQLEEQRAELVERLQAMLQAHWEEANQL 279
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
19-268 |
2.62e-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: 50.56 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 19 EALEEERQAL---TLRLEVEQQQCRTlQEERD-EARAGQLSEHRKLEALQValqeeRQAWIKQEHQLKERLQALQEEGQA 94
Cdd:pfam01576 702 EELEDELQATedaKLRLEVNMQALKA-QFERDlQARDEQGEEKRRQLVKQV-----RELEAELEDERKQRAQAVAAKKKL 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 95 QLEREKGNSQREA--QAAWETQQQFALLQTEVRRLEGDLDTVRRERDALqlemsLVQAR--------YESQRIQMESELA 164
Cdd:pfam01576 776 ELDLKELEAQIDAanKGREEAVKQLKKLQAQMKDLQRELEEARASRDEI-----LAQSKesekklknLEAELLQLQEDLA 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 165 V---QLEQRVTER--LAEAQENSLRQAASLRDHHRkQLQELSGQHQQELaaQLAQFKVEM-ADREERQQQVAQDYELRLA 238
Cdd:pfam01576 851 AserARRQAQQERdeLADEIASGASGKSALQDEKR-RLEARIAQLEEEL--EEEQSNTELlNDRLRKSTLQVEQLTTELA 927
|
250 260 270
....*....|....*....|....*....|
gi 1907081119 239 REQARVRDLKSGNQQLEEQRAELVERLQAM 268
Cdd:pfam01576 928 AERSTSQKSESARQQLERQNKELKAKLQEM 957
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
69-302 |
6.25e-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: 6.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 69 EERQAWIKQE-HQLKERLQALQEEGQAQLEREKGNSqreaqaaweTQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSL 147
Cdd:COG3206 174 RKALEFLEEQlPELRKELEEAEAALEEFRQKNGLVD---------LSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 148 VQARYESQRIQMESELAVQLEQRVTERLAEAQENSLRQAASLRDHH------RKQLQELSGQHQQELAAQLAQFKVEMAD 221
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdvialRAQIAALRAQLQQEAQRILASLEAELEA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 222 REERQQQVAQdyelRLAREQARVRDLKSGNQQLE--EQRAELVERLQAMLQAHWEEANqlLSTTLLPPN------PQAPL 293
Cdd:COG3206 325 LQAREASLQA----QLAQLEARLAELPELEAELRrlEREVEVARELYESLLQRLEEAR--LAEALTVGNvrvidpAVVPL 398
|
....*....
gi 1907081119 294 aEPSSPGPL 302
Cdd:COG3206 399 -KPVSPKKL 406
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1-225 |
7.70e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 1 MEALSREQEGARLQQREKEALEEERQALTLRLEVE--QQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQE 78
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAALRLWFAQRRLEllEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 79 HQLKERLQALQEEGQAQLEREKGNSQREAQAAW-------ETQQQFALLQTEVRRLegdLDTVRRERDALQlemslvQAR 151
Cdd:COG4913 337 GDRLEQLEREIERLERELEERERRRARLEALLAalglplpASAEEFAALRAEAAAL---LEALEEELEALE------EAL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 152 YEsqriqmeselAVQLEQRVTERLAEAQE--NSLRQAASLRDHH----RKQLQELSGQHQQEL--AAQLaqfkVEMADRE 223
Cdd:COG4913 408 AE----------AEAALRDLRRELRELEAeiASLERRKSNIPARllalRDALAEALGLDEAELpfVGEL----IEVRPEE 473
|
..
gi 1907081119 224 ER 225
Cdd:COG4913 474 ER 475
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1-167 |
1.17e-05 |
|
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: 48.58 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 1 MEALSREQEGARlqQREKEALEEERQALTLR-----LEVEQQQCRTLQEERD----------EARAGQLSEHRKLEALQV 65
Cdd:pfam17380 422 MEQIRAEQEEAR--QREVRRLEEERAREMERvrleeQERQQQVERLRQQEEErkrkklelekEKRDRKRAEEQRRKILEK 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 66 ALQEERQAWIKQ-------EHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRLEgdldtvrrer 138
Cdd:pfam17380 500 ELEERKQAMIEEerkrkllEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE---------- 569
|
170 180
....*....|....*....|....*....
gi 1907081119 139 dALQLEMSLVQARYESQRIQMESELAVQL 167
Cdd:pfam17380 570 -AMEREREMMRQIVESEKARAEYEATTPI 597
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
70-311 |
1.49e-05 |
|
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: 48.20 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 70 ERQAWIKQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQfALLQTEVRRLEGDLDtvrRERDALQLEmslvQ 149
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQ-AAIYAEQERMAMERE---RELERIRQE----E 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 150 ARYESQRIQMEsELAVQLEQ-RVTERLA-EAQENSLRQAASLRDHHRKQLQElsGQHQQELAAQLAQFKVEMADREERQQ 227
Cdd:pfam17380 358 RKRELERIRQE-EIAMEISRmRELERLQmERQQKNERVRQELEAARKVKILE--EERQRKIQQQKVEMEQIRAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 228 QVAQDYELRLAREQARVR-DLKSGNQQLEEQRAELVERLQAML--------QAHWEEANQLLSTTLLPPNPQAPLAEPSS 298
Cdd:pfam17380 435 REVRRLEEERAREMERVRlEEQERQQQVERLRQQEEERKRKKLelekekrdRKRAEEQRRKILEKELEERKQAMIEEERK 514
|
250
....*....|...
gi 1907081119 299 PGPLEPEKGERRT 311
Cdd:pfam17380 515 RKLLEKEMEERQK 527
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-264 |
1.71e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 2 EALSREQEGARLQQREKEALEEERQALTLRLEVEQ-QQCRTLQEERDEARAG-----QLSEHRKLEALQVALQEERQAwi 75
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEkKKADEAKKKAEEAKKAdeakkKAEEAKKAEEAKKKAEEAKKA-- 1472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 76 kQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSlvQARYESQ 155
Cdd:PTZ00121 1473 -DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA--EEKKKAD 1549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 156 RIQMESELAVQLEQRVTERLAEAQEN---SLRQAASLRDHHRKQLQELSGQHQQELA--------AQLAQFKVEMADREE 224
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDknmALRKAEEAKKAEEARIEEVMKLYEEEKKmkaeeakkAEEAKIKAEELKKAE 1629
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1907081119 225 RQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVER 264
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
111-279 |
1.87e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 111 WETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYES-QRIQMESELAVQLEQ------RVTERLAEAQENS- 182
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlQRLAEYSWDEIDVASaereiaELEAELERLDASSd 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 183 -LRQAASLRDHHRKQLQELSGQhQQELAAQLAQFKVEMADREERQQQVAQDYELRLAREQARVR---DLKSGNQQLEEQR 258
Cdd:COG4913 686 dLAALEEQLEELEAELEELEEE-LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRallEERFAAALGDAVE 764
|
170 180
....*....|....*....|.
gi 1907081119 259 AELVERLQAMLQAHWEEANQL 279
Cdd:COG4913 765 RELRENLEERIDALRARLNRA 785
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1-270 |
2.28e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.49 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 1 MEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQ-----EERDEARAGQLSEHRKLEAlQVALQEER---- 71
Cdd:PRK10246 557 TKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQpwldaQEEHERQLRLLSQRHELQG-QIAAHNQQiiqy 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 72 -QAWIKQEHQLKERLQALQEEGQAQLEREKGNSQREAQAA-WETQQ-QFALLQTEVRRLEGDLDTVRRERDA-------- 140
Cdd:PRK10246 636 qQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQsWQQRQnELTALQNRIQQLTPLLETLPQSDDLphseetva 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 141 --------------------LQLEMSLVQARYESQRIQMESELAVQLEQRVTERLA----EAQENSLRQAASLRDHHRKQ 196
Cdd:PRK10246 716 ldnwrqvheqclslhsqlqtLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLAalldEETLTQLEQLKQNLENQRQQ 795
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081119 197 LQELSGQHQQELAAQLAQ---FKVEMADREERQQQVAQ-DYELRL-AREQARVRdlksgnQQLeEQRAELVERLQAMLQ 270
Cdd:PRK10246 796 AQTLVTQTAQALAQHQQHrpdGLDLTVTVEQIQQELAQlAQQLREnTTRQGEIR------QQL-KQDADNRQQQQALMQ 867
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
77-320 |
2.96e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 77 QEHQLKERLQALQEEgQAQLEREKGNSQREAQAAwetqqqfallQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQR 156
Cdd:COG3883 17 QIQAKQKELSELQAE-LEAAQAELDALQAELEEL----------NEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 157 IQMESELAVQLEQRVT----ERLAEAQENS--LRQAASLR---DHHRKQLQElsgqhQQELAAQLAQFKVEMADREERQQ 227
Cdd:COG3883 86 EELGERARALYRSGGSvsylDVLLGSESFSdfLDRLSALSkiaDADADLLEE-----LKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 228 QVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQAMLQAHWEEANQLLSTTLLPPNPQAPLAEPSSPGPLEPEKG 307
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
250
....*....|...
gi 1907081119 308 ERRTWAMPPMAVA 320
Cdd:COG3883 241 AAAASAAGAGAAG 253
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
13-272 |
3.43e-05 |
|
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: 47.14 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 13 LQQREKEALEEE-RQALTLRLEVEQQQCRTLQEERD--EARAGQLSEHR--KLEALQVaLQEERQAwikQEHQLKERLQA 87
Cdd:pfam12128 665 EKDKKNKALAERkDSANERLNSLEAQLKQLDKKHQAwlEEQKEQKREARteKQAYWQV-VEGALDA---QLALLKAAIAA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 88 LQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAvQL 167
Cdd:pfam12128 741 RRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLS-NI 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 168 EQRVTE---RLAEAQENSLRQAASL---RDHHRKQLQELSGQHQ--QELAAQLAQFKVEmadreerqqQVAQDYELRLAR 239
Cdd:pfam12128 820 ERAISElqqQLARLIADTKLRRAKLemeRKASEKQQVRLSENLRglRCEMSKLATLKED---------ANSEQAQGSIGE 890
|
250 260 270
....*....|....*....|....*....|...
gi 1907081119 240 EQARVRDLKSGNQQLEEQRAELVERLQAMLQAH 272
Cdd:pfam12128 891 RLAQLEDLKLKRDYLSESVKKYVEHFKNVIADH 923
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-284 |
5.85e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 1 MEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEH-RKLEALQVALQEERQAWIKQEH 79
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLaEELEELQQRLAELEEELEEAQE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 80 QLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTV------------------RRERDAL 141
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIagvlflvlgllallflllAREKASL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 142 QLEMSLVQARYESQRIQMESEL----AVQLEQRVTERLAEAQENSLRQAASLRDHHRKQLQELS-GQHQQELAAQLAQFK 216
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEellaALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQlEELEQEIAALLAEAG 380
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081119 217 VEmaDREERQQQVAQDYELRlaREQARVRDLKsgnQQLEEQRAELVERLQAMLQAHWEEANQLLSTTL 284
Cdd:COG4717 381 VE--DEEELRAALEQAEEYQ--ELKEELEELE---EQLEELLGELEELLEALDEEELEEELEELEEEL 441
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
47-281 |
6.39e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.12 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 47 DEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQ---QQFALLQTE 123
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLlylDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 124 VRRLEGDLDTVRRERDALQLEMSLVQ---ARYESQRIQMESELAVQLEQRVTERLAEAQENSLRQAASLRDHHRKQLQEL 200
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEeklAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 201 SGQHQQELAAQLAQFKVEMADRE-ERQQQVAQDYELRLAREQARVRDLKsgNQQLEEQRAELVERLQAMLQAHWEEANQL 279
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEkELKELEIKREAEEEEEEELEKLQEK--LEQLEEELLAKKKLESERLSSAAKLKEEE 396
|
..
gi 1907081119 280 LS 281
Cdd:pfam02463 397 LE 398
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
7-278 |
7.69e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.29 E-value: 7.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 7 EQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKERLQ 86
Cdd:pfam13868 50 EEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 87 ALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTE-VRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAV 165
Cdd:pfam13868 130 EEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAErEEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 166 ----QLEQRVTERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQELAAQLAQFKVEMADREERQQQVAQDYELRLAREQ 241
Cdd:pfam13868 210 lyqeEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRL 289
|
250 260 270
....*....|....*....|....*....|....*..
gi 1907081119 242 ARVRDLKSGNQQLEEQRAELVERLQAMLQAHWEEANQ 278
Cdd:pfam13868 290 EHRRELEKQIEEREEQRAAEREEELEEGERLREEEAE 326
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-132 |
8.35e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 8.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 2 EALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQL 81
Cdd:COG1196 647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1907081119 82 KERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDLD 132
Cdd:COG1196 727 EEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
4-281 |
9.48e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 9.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 4 LSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKE 83
Cdd:pfam01576 168 LAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 84 RLQALQEEGQAQLEREKGNSQREAQAAwETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRiqmesEL 163
Cdd:pfam01576 248 ALARLEEETAQKNNALKKIRELEAQIS-ELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQ-----EL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 164 AVQLEQRVTErLAEAQENSLR----QAASLRDHHRKQLQELSGQHQQELAAQLAQFKVEMADREERQ---------QQVA 230
Cdd:pfam01576 322 RSKREQEVTE-LKKALEEETRsheaQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAelqaelrtlQQAK 400
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907081119 231 QDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQAmLQAHWEEANQLLS 281
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSK-LQSELESVSSLLN 450
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
85-267 |
1.20e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 85 LQALQEEgQAQLEREKG----NSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQME 160
Cdd:COG4717 48 LERLEKE-ADELFKPQGrkpeLNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 161 SELAVQLEQRVTERLAEAQE--NSLRQAASLRDHHRKQLQELSGQH---QQELAAQLAQFKVEMADREERQQQVAQDYEL 235
Cdd:COG4717 127 LLPLYQELEALEAELAELPErlEELEERLEELRELEEELEELEAELaelQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190
....*....|....*....|....*....|..
gi 1907081119 236 RLAREQARVRDLKSGNQQLEEQRAELVERLQA 267
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
16-265 |
1.21e-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: 45.33 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 16 REK--EALEEERQALTLR---LEVEQQQCRTLQEERDEARAGQLS----------------EHRKLEALQVALQEERQAW 74
Cdd:COG3096 783 REKrlEELRAERDELAEQyakASFDVQKLQRLHQAFSQFVGGHLAvafapdpeaelaalrqRRSELERELAQHRAQEQQL 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 75 IKQEHQLKERLQALQE-EGQAQLEREKGNSQR------EAQAAWETQQQFALLQTEVRRLEGDLDTVRR---ERDALQLE 144
Cdd:COG3096 863 RQQLDQLKEQLQLLNKlLPQANLLADETLADRleelreELDAAQEAQAFIQQHGKALAQLEPLVAVLQSdpeQFEQLQAD 942
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 145 msLVQARYESQRIQMESELAVQLEQRVT--------ERLAEAQENS------LRQAASLRDHHRKQLQELSGQHQQELAA 210
Cdd:COG3096 943 --YLQAKEQQRRLKQQIFALSEVVQRRPhfsyedavGLLGENSDLNeklrarLEQAEEARREAREQLRQAQAQYSQYNQV 1020
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081119 211 -------------QLAQFKVEM--------ADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERL 265
Cdd:COG3096 1021 laslkssrdakqqTLQELEQELeelgvqadAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRL 1096
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2-124 |
1.51e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.69 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 2 EALSReqegARLQQREK-EALEEERQALTlRLEVEQQQCRTLQEERDEARAGQLSEhrKLEALQVALQEERQAWiKQEHQ 80
Cdd:COG0542 397 EAAAR----VRMEIDSKpEELDELERRLE-QLEIEKEALKKEQDEASFERLAELRD--ELAELEEELEALKARW-EAEKE 468
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1907081119 81 LKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEV 124
Cdd:COG0542 469 LIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEV 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-132 |
1.85e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 1 MEALSREQEGarlQQREKEALEEERQALTLRLEVEQQQCRTLQEERDEARAGQlsehRKLEALQVALQEERQAWIKQEHQ 80
Cdd:TIGR02168 854 IESLAAEIEE---LEELIEELESELEALLNERASLEEALALLRSELEELSEEL----RELESKRSELRRELEELREKLAQ 926
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081119 81 LKERLQALQEEGQAQLEREKGNSQREAQAAWETQQ----QFALLQTEVRRLEGDLD 132
Cdd:TIGR02168 927 LELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENkiedDEEEARRRLKRLENKIK 982
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
14-282 |
1.90e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 14 QQREKEALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEhRKLEALQVALQEERQawikQEHQLKERLQALQEEGQ 93
Cdd:TIGR00618 603 LSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKL-TALHALQLTLTQERV----REHALSIRVLPKELLAS 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 94 AQLEREKGNSQREAQAAWetQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRI---QMESELAVQLEQR 170
Cdd:TIGR00618 678 RQLALQKMQSEKEQLTYW--KEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDalnQSLKELMHQARTV 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 171 VTERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQELAAQLAQfkvEMADREERQQQVAQDYEL-RLAREQARVRDLKS 249
Cdd:TIGR00618 756 LKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTH---LLKTLEAEIGQEIPSDEDiLNLQCETLVQEEEQ 832
|
250 260 270
....*....|....*....|....*....|...
gi 1907081119 250 GNQQLEEQRAELVERLQamLQAHWEEANQLLST 282
Cdd:TIGR00618 833 FLSRLEEKSATLGEITH--QLLKYEECSKQLAQ 863
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2-269 |
1.93e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.09 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 2 EALSREQEGARLQQREKEALEEERQaltlrlEVEQQQCRTLQEERdeARAGQLSEHRKLEALQVALQEERQAWIKQEHQL 81
Cdd:pfam02029 81 EALERQKEFDPTIADEKESVAERKE------NNEEEENSSWEKEE--KRDSRLGRYKEEETEIREKEYQENKWSTEVRQA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 82 KERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRLegDLDTVRRERDALQLEMSLVQARYESQRIQMES 161
Cdd:pfam02029 153 EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFL--DQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 162 ELAVQLEQRVTERLaEAQENSLRQAASLRDHHRKQLQELSgQHQQELAAQLAQFKVEMADR----EERQQQVAQDYELRL 237
Cdd:pfam02029 231 SQSQEREEEAEVFL-EAEQKLEELRRRRQEKESEEFEKLR-QKQQEAELELEELKKKREERrkllEEEEQRRKQEEAERK 308
|
250 260 270
....*....|....*....|....*....|..
gi 1907081119 238 AREQARVRDLKsgnQQLEEQRAELVERLQAML 269
Cdd:pfam02029 309 LREEEEKRRMK---EEIERRRAEAAEKRQKLP 337
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2-158 |
2.00e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 2 EALSREQEGARLQQREKEALEEERQALTLRLEvEQQQCRTLQEERDEARAGQLSEHRKLEALQvalqEERQAWIKQEHQL 81
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALEAELAELPERLEELE----ERLEELRELEEEL 165
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081119 82 KERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQ 158
Cdd:COG4717 166 EELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
6-268 |
2.27e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 6 REQEGARLQQREKEALEEERQALTLRLEveqqqcRTLQEERDEARAGQLSEHRKLEALQVALQEERQAWIkQEHQLKERL 85
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAGRATFLPLDKI------RARAALAAALARGAIGAAVDLVASDLREADARYYVL-GDTLLGRTL 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 86 QALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAV 165
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 166 QLEQRVTERLAEAQENSLRQAASLRDHHRKQLQELsgQHQQELAAQLAQFKVEMADREERQQQVAQdYELRLAR------ 239
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELL--EEEELLEEEALEELPEPPDLEELERELER-LEREIEAlgpvnl 784
|
250 260 270
....*....|....*....|....*....|....*..
gi 1907081119 240 --------EQARVRDLKSGNQQLEEQRAELVERLQAM 268
Cdd:COG1196 785 laieeyeeLEERYDFLSEQREDLEEARETLEEAIEEI 821
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
74-284 |
2.76e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 74 WIKQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQ-LEMSLVQARY 152
Cdd:pfam12128 595 WAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQsEKDKKNKALA 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 153 ESQRiqmeselavQLEQRVTERLAEAQENSLRQAASLrDHHRKQLQELSGQHQQ-------ELAAQLAQFKVEMADREE- 224
Cdd:pfam12128 675 ERKD---------SANERLNSLEAQLKQLDKKHQAWL-EEQKEQKREARTEKQAywqvvegALDAQLALLKAAIAARRSg 744
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081119 225 ---RQQQVAQDY----------ELRLAREQARVRDLKSGNQQLEEQRAElVERLQAMLQAHWEEANQLLSTTL 284
Cdd:pfam12128 745 akaELKALETWYkrdlaslgvdPDVIAKLKREIRTLERKIERIAVRRQE-VLRYFDWYQETWLQRRPRLATQL 816
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
25-238 |
3.10e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 25 RQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKERLQALQEEgQAQLEREKgNSQ 104
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE-LEELREEL-EKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 105 REAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDAL-QLEMSLVQARYESQRIQMESELAVQLEQRVTERLAEAQENSL 183
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELrELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907081119 184 RQAASLRDHHRKQLQELSGQHQQeLAAQLAQFKVEMADREERQQQVAQDYELRLA 238
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEE-LEEELEQLENELEAAALEERLKEARLLLLIA 255
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-256 |
3.30e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 2 EALSREQEGARLQQREKEalEEERQALTLRLEVEQQ-------QCRTLQEERDEARAGQL--SEHRKLEALQVALQEERQ 72
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKA--EEDKNMALRKAEEAKKaeearieEVMKLYEEEKKMKAEEAkkAEEAKIKAEELKKAEEEK 1632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 73 AWIKQ-------EHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQfallQTEVRRLEGDLDtvRRERDALQLEm 145
Cdd:PTZ00121 1633 KKVEQlkkkeaeEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA----EEDEKKAAEALK--KEAEEAKKAE- 1705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 146 SLVQARYESQRIQMESELAVQLEQRVTERLAEAQENSLRQAASLR--DHHRKQLQELsgQHQQELAAQLAQFKVEMADRE 223
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKkdEEEKKKIAHL--KKEEEKKAEEIRKEKEAVIEE 1783
|
250 260 270
....*....|....*....|....*....|...
gi 1907081119 224 ErqqqVAQDYELRLAREQARVRDLKSGNQQLEE 256
Cdd:PTZ00121 1784 E----LDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
15-268 |
3.31e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.89 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 15 QREKEALEEERQALTLRL---EVEQQ----------QCRTLQEERDEARagQLSEhrKLEALQVALQEERqawiKQEHQL 81
Cdd:PRK10929 85 RQQLNNERDEPRSVPPNMstdALEQEilqvssqlleKSRQAQQEQDRAR--EISD--SLSQLPQQQTEAR----RQLNEI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 82 KERLQALQEEGQAqlerekgnsqreaqaawETQQQFALLQTEVRRLEGDLDtvrrerdalQLEMSLVQARYESQRIQMES 161
Cdd:PRK10929 157 ERRLQTLGTPNTP-----------------LAQAQLTALQAESAALKALVD---------ELELAQLSANNRQELARLRS 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 162 ELAVQLEQRVTERLAE--AQENSLRQ-AASLRDHHRKQLQELSG----------QHQQELAAQLAQFKVEMADREERQQQ 228
Cdd:PRK10929 211 ELAKKRSQQLDAYLQAlrNQLNSQRQrEAERALESTELLAEQSGdlpksivaqfKINRELSQALNQQAQRMDLIASQQRQ 290
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907081119 229 VA-QDYELRLA----REQARVrdLKSGNQQLEEQRAElVERLQAM 268
Cdd:PRK10929 291 AAsQTLQVRQAlntlREQSQW--LGVSNALGEALRAQ-VARLPEM 332
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
38-267 |
3.79e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 38 QCRTLQEERDEARAGQLSEHRKLEALQVALQE-ERQAWIKQEHQLKERLQAL-QEEGQAQLEREKGNSQREAQAAW---- 111
Cdd:PRK02224 160 QLGKLEEYRERASDARLGVERVLSDQRGSLDQlKAQIEEKEEKDLHERLNGLeSELAELDEEIERYEEQREQARETrdea 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 112 --------ETQQQFALLQTEVRRLEGDLDTVRRERDALqlemslvqaryeSQRIQMESELAVQLEQRVTERLAEAQENSL 183
Cdd:PRK02224 240 devleeheERREELETLEAEIEDLRETIAETEREREEL------------AEEVRDLRERLEELEEERDDLLAEAGLDDA 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 184 RQAASLrdhhrkqlqelsgQHQQELAAQlaqfKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVE 263
Cdd:PRK02224 308 DAEAVE-------------ARREELEDR----DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES 370
|
....
gi 1907081119 264 RLQA 267
Cdd:PRK02224 371 ELEE 374
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
84-275 |
3.98e-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: 42.22 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 84 RLQALQEEgQAQLEREKGNSQREAQAAwetQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARyesqriqmesel 163
Cdd:COG1579 11 DLQELDSE-LDRLEHRLKELPAELAEL---EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR------------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 164 avqlEQRVTERLAEAQENslRQAASLR---DHHRKQLQELSgQHQQELAAQLAQFKVEMADREERQQQVAQDYELRLARE 240
Cdd:COG1579 75 ----IKKYEEQLGNVRNN--KEYEALQkeiESLKRRISDLE-DEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
170 180 190
....*....|....*....|....*....|....*
gi 1907081119 241 QARVRDLKSGNQQLEEQRAELVERLQAMLQAHWEE 275
Cdd:COG1579 148 DEELAELEAELEELEAEREELAAKIPPELLALYER 182
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
6-217 |
4.96e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 6 REQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKERL 85
Cdd:TIGR00618 659 RVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARE 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 86 QALQE-EGQAQLEREKGNSQREAQAAWETQQQFALLQT--EVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESE 162
Cdd:TIGR00618 739 DALNQsLKELMHQARTVLKARTEAHFNNNEEVTAALQTgaELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDI 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907081119 163 LAVQLEQRVTERlaEAQENSLRQAASLRDHHRKQLQELSGQHQQELAAQLAQFKV 217
Cdd:TIGR00618 819 LNLQCETLVQEE--EQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKI 871
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
12-214 |
5.11e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 12 RLQQREKEALEEERQALtlrlEVEQQQCRTLQEERDEARAgqlsehrKLEALQVALQEerqawIKQEHQLKERLQALQE- 90
Cdd:COG4717 67 ELNLKELKELEEELKEA----EEKEEEYAELQEELEELEE-------ELEELEAELEE-----LREELEKLEKLLQLLPl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 91 -EGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAVQLEQ 169
Cdd:COG4717 131 yQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907081119 170 RvTERLAEAQENslrqaaslRDHHRKQLQELSGQHQ-QELAAQLAQ 214
Cdd:COG4717 211 L-EEELEEAQEE--------LEELEEELEQLENELEaAALEERLKE 247
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
4-255 |
5.34e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.25 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 4 LSREQEGARLQQREKEALEEERQALT------LRLEVEQ--QQCRTLQEERDEARAGQLSEHRKLEALQVALQE--ERQA 73
Cdd:PRK10246 249 LTRLDELQQEASRRQQALQQALAAEEkaqpqlAALSLAQpaRQLRPHWERIQEQSAALAHTRQQIEEVNTRLQStmALRA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 74 WIKQ--EHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQ-QQFALLQTEVRRLEGDLDTVRRERDAL-QLEMSLVq 149
Cdd:PRK10246 329 RIRHhaAKQSAELQAQQQSLNTWLAEHDRFRQWNNELAGWRAQfSQQTSDREQLRQWQQQLTHAEQKLNALpAITLTLT- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 150 aryesqriqmESELAVQLEQRVTERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQELAAQLAQFKVEMADREERQQQV 229
Cdd:PRK10246 408 ----------ADEVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQL 477
|
250 260
....*....|....*....|....*.
gi 1907081119 230 AQDYElrLAREQARVRDLKSGNQQLE 255
Cdd:PRK10246 478 ADVKT--ICEQEARIKDLEAQRAQLQ 501
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2-282 |
5.85e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 2 EALSREQEGARLQQREKEALEEERQAltlrLEVEQQQCRTLQEERDEARAGQlsehRKLEALQVALQEerqawikQEHQL 81
Cdd:PRK04863 300 RQLAAEQYRLVEMARELAELNEAESD----LEQDYQAASDHLNLVQTALRQQ----EKIERYQADLEE-------LEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 82 KERLQALQE--EGQAQLEREKGNSQREA----------QAAWETQQQFAL-LQTEVRRLEgdldTVRRERDALQLEMSLV 148
Cdd:PRK04863 365 EEQNEVVEEadEQQEENEARAEAAEEEVdelksqladyQQALDVQQTRAIqYQQAVQALE----RAKQLCGLPDLTADNA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 149 QARYESQRIQMES--ELAVQLEQRVteRLAEAQENSLRQAASL---------RDHHRKQLQELSGQH--QQELAAQLAQF 215
Cdd:PRK04863 441 EDWLEEFQAKEQEatEELLSLEQKL--SVAQAAHSQFEQAYQLvrkiagevsRSEAWDVARELLRRLreQRHLAEQLQQL 518
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081119 216 KVEMAD--REERQQQVAQdyelRLAREQARVrdlksgnQQLEEQRAELVERLQAMLQAHWEEANQLLST 282
Cdd:PRK04863 519 RMRLSEleQRLRQQQRAE----RLLAEFCKR-------LGKNLDDEDELEQLQEELEARLESLSESVSE 576
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
285-479 |
6.55e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 285 LPPNPQAPLAEPSSPGPLEPEKGERRTWAMPPmavalkpvlqqsREVKGDVPGAPSVlcSTSPDLSLLLGPPfqnQNSFQ 364
Cdd:PHA03247 2617 LPPDTHAPDPPPPSPSPAANEPDPHPPPTVPP------------PERPRDDPAPGRV--SRPRRARRLGRAA---QASSP 2679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 365 PLEPKPDVTPPTAGPfsaLEAFTDDHRAERPfPEEDPGSDGDAR-LPPASQLEGLKNFLQQLLETAPQSNGNPSADLLLP 443
Cdd:PHA03247 2680 PQRPRRRAARPTVGS---LTSLADPPPPPPT-PEPAPHALVSATpLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPA 2755
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907081119 444 KAGSRAVSSWEEAPQVPRLPPPVHKTKVPLAMASSL 479
Cdd:PHA03247 2756 RPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASL 2791
|
|
| FUSC |
pfam04632 |
Fusaric acid resistance protein family; This family includes a conserved region found in two ... |
118-272 |
7.52e-04 |
|
Fusaric acid resistance protein family; This family includes a conserved region found in two proteins associated with fusaric acid resistance, from Burkholderia cepacia and Klebsiella oxytoca. These proteins are likely to be membrane transporter proteins.
Pssm-ID: 428044 [Multi-domain] Cd Length: 655 Bit Score: 42.66 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 118 ALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAVQLEQRVTERLAeaqenslrQAASLRDHHRkQL 197
Cdd:pfam04632 174 AALAGAPGAEAFEAARLRLAADILALEALRSHAAFESPRGRARARALRRLLARMLALLP--------RLRSLARLLA-RL 244
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081119 198 QELSGQHQQELAAQLAqfkvEMADREERQQQVAQDYELRLAREQAR--VRDLKSGNQQLEEQRAELVERLQAMLQAH 272
Cdd:pfam04632 245 RTEGAGTVPELAALLD----ELAAWEAALAAEALQAALAALRARLRalRPALPLDFDTAAELLARLADLLAELAEAL 317
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
4-272 |
8.67e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 41.95 E-value: 8.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 4 LSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLeaLQVALQEERQAWIKQEHQLKE 83
Cdd:pfam15558 17 HKEEQRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKAR--LGREERRRADRREKQVIEKES 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 84 RLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRlegdldtVRRERDALQLEMSLVQARYESQRIQMESEL 163
Cdd:pfam15558 95 RWREQAEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQ-------ALREQNSLQLQERLEEACHKRQLKEREEQK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 164 AVQLEQRVTERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQELAAQLaqfkVEMADREERQQQVAQDYELRLAREQAR 243
Cdd:pfam15558 168 KVQENNLSELLNHQARKVLVDCQAKAEELLRRLSLEQSLQRSQENYEQL----VEERHRELREKAQKEEEQFQRAKWRAE 243
|
250 260
....*....|....*....|....*....
gi 1907081119 244 vrdlKSGNQQLEEQRAELVERLQAMLQAH 272
Cdd:pfam15558 244 ----EKEEERQEHKEALAELADRKIQQAR 268
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2-266 |
1.21e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 2 EALSREQEGARLQQREKEALEEeRQALTLRLEVEQQQCRTLQEErdEARAGQLSEHRKLEALQVALQEERQAWIKQEHQL 81
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEE-QLKKQQLLKQLRARIEELRAQ--EAVLEETQERINRARKAAPLAAHIKAVTQIEQQA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 82 KERLQALQEEgQAQLEREKGNSQREAQAAWETQQQFALLQTEVR---RLEGDLDTVRRERDALQLEMSLVQARYESQRIQ 158
Cdd:TIGR00618 310 QRIHTELQSK-MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSqeiHIRDAHEVATSIREISCQQHTLTQHIHTLQQQK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 159 MESELAVQLEQRVTERLAEAQENSLRQAASLRDhHRKQLQELSGQH--QQELAAQLAQFKVEMADREERQQQVAQDYELR 236
Cdd:TIGR00618 389 TTLTQKLQSLCKELDILQREQATIDTRTSAFRD-LQGQLAHAKKQQelQQRYAELCAAAITCTAQCEKLEKIHLQESAQS 467
|
250 260 270
....*....|....*....|....*....|
gi 1907081119 237 LAREQARVRDLKSGNQQLEEQRAELVERLQ 266
Cdd:TIGR00618 468 LKEREQQLQTKEQIHLQETRKKAVVLARLL 497
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2-169 |
1.62e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 2 EALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHR-KLEALQVALQEERQAWiKQEH- 79
Cdd:COG3206 213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRaQLAELEAELAELSARY-TPNHp 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 80 ---QLKERLQALQEEGQAQLEREKGNSQREAQAAwetQQQFALLQTEVRRLEGDLDT---VRRERDALQLEMSLVQARYE 153
Cdd:COG3206 292 dviALRAQIAALRAQLQQEAQRILASLEAELEAL---QAREASLQAQLAQLEARLAElpeLEAELRRLEREVEVARELYE 368
|
170
....*....|....*...
gi 1907081119 154 S--QRIQmESELAVQLEQ 169
Cdd:COG3206 369 SllQRLE-EARLAEALTV 385
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2-264 |
1.62e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 2 EALSREQEGARLQQREKEALEEERqaltlRLEVEQQQCRTLQEERDEARA---GQLSEHRK-----------LEALQVAL 67
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAA-----ELESELEEAREAVEDRREEIEeleEEIEELRErfgdapvdlgnAEDFLEEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 68 QEERQAWIKQEHQLKERLQALQ---EEGQAQLEREK----GNSQRE---AQAAWETQQQFALLQTEVRRLEGDLDTVRRE 137
Cdd:PRK02224 418 REERDELREREAELEATLRTARervEEAEALLEAGKcpecGQPVEGsphVETIEEDRERVEELEAELEDLEEEVEEVEER 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 138 RDALQlemSLVQARYESQRIQMESELavqLEQRVTERLAEAQENSLRqAASLRDhhRKQLQELSGQHQQELAAQLAQ--- 214
Cdd:PRK02224 498 LERAE---DLVEAEDRIERLEERRED---LEELIAERRETIEEKRER-AEELRE--RAAELEAEAEEKREAAAEAEEeae 568
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1907081119 215 -FKVEMADREERQQQVAQDYEL--RLAREQARVRDLKSGNQQLEEQRAELVER 264
Cdd:PRK02224 569 eAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEIERLREKREALAEL 621
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
29-219 |
1.73e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.19 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 29 TLRLEVEQQQcRTLQEERDEArAGQLSEHRKLEALQVALQEERQAWikqEHQLKERLQALQEE-GQAQLEREKGNsqrEA 107
Cdd:COG1842 27 MLDQAIRDME-EDLVEARQAL-AQVIANQKRLERQLEELEAEAEKW---EEKARLALEKGREDlAREALERKAEL---EA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 108 QAAwETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQ---------MESELAV----QLEQRVTER 174
Cdd:COG1842 99 QAE-ALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQekvnealsgIDSDDATsaleRMEEKIEEM 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907081119 175 LAEAQE-NSLRQAASLRDhhrkQLQELSGQHqqELAAQLAQFKVEM 219
Cdd:COG1842 178 EARAEAaAELAAGDSLDD----ELAELEADS--EVEDELAALKAKM 217
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
120-266 |
1.77e-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: 40.87 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 120 LQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRI-QMESELAVQLEQRVTERLAEAQenslRQAASLRD--HHRKQ 196
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAIsRQDYDGATAQLRAAQAAVKAAQ----AQLAQAQIdlARRRV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 197 LQELSGQHQQELAAQLAQFKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQ 266
Cdd:pfam00529 132 LAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELK 201
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
281-496 |
2.64e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 281 STTLLPPNPQAPLAEPSSPGPLEPEKgERRTWAMPPMAVALKPVLQQSrevkgdvpgAPSVLCSTSPDLSLLLGPPFQNQ 360
Cdd:PHA03247 2825 AGPLPPPTSAQPTAPPPPPGPPPPSL-PLGGSVAPGGDVRRRPPSRSP---------AAKPAAPARPPVRRLARPAVSRS 2894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 361 NSFQPLEPKPDVTPPTAGPFSALEAFTDDHRAERPFPEEDPGSDGDARLPPasqleglknflqqllETAPQSNGNPSADL 440
Cdd:PHA03247 2895 TESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAP---------------TTDPAGAGEPSGAV 2959
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081119 441 LLPKAGsrAVSSWEEAPQVPRLPPPVHKTKVPLAMASSLfRVHGLPSTNLQGSGLS 496
Cdd:PHA03247 2960 PQPWLG--ALVPGRVAVPRFRVPQPAPSREAPASSTPPL-TGHSLSRVSSWASSLA 3012
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-180 |
3.17e-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: 40.82 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 2 EALSREQEGARLQQR----EKEALEEERQALTLRLEVEQQQCRTLQEERDEARAgqlsehrKLEALQVALQEER---QAW 74
Cdd:TIGR02169 311 AEKERELEDAEERLAkleaEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE-------ELEDLRAELEEVDkefAET 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 75 IKQEHQLKERLQALQEEgqaqLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYES 154
Cdd:TIGR02169 384 RDELKDYREKLEKLKRE----INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
|
170 180 190
....*....|....*....|....*....|.
gi 1907081119 155 QRIQMESE----LAVQLE-QRVTERLAEAQE 180
Cdd:TIGR02169 460 LAADLSKYeqelYDLKEEyDRVEKELSKLQR 490
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
11-90 |
3.60e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 11 ARLQQREKEALEEERQALTLRLEVE------QQQCRTLQEERDEARAGQLSEHR------KLEALQV-----ALQEERQA 73
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEklkeelEEKKEKLQEEEDKLLEEAEKEAQqaikeaKKEADEIikelrQLQKGGYA 602
|
90
....*....|....*..
gi 1907081119 74 WIKqEHQLKERLQALQE 90
Cdd:PRK00409 603 SVK-AHELIEARKRLNK 618
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
4-224 |
4.51e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 4 LSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDEaragqLSEHRKLEALQVALQEERQawIKQEHQLKE 83
Cdd:TIGR00606 328 LEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQS-----LATRLELDGFERGPFSERQ--IKNFHTLVI 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 84 RLQALQEEGQAQLEREKGNSQREAQAAwetqqqfallQTEVR-RLEGDLDTVRRERDALQLEMS-LVQARYESQRIQMES 161
Cdd:TIGR00606 401 ERQEDEAKTAAQLCADLQSKERLKQEQ----------ADEIRdEKKGLGRTIELKKEILEKKQEeLKFVIKELQQLEGSS 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081119 162 ELAVQLEQRVTERLAE---AQENSLRQAASLRDHHRKQLQELSGQHQQELAAQLAQFKVEMADREE 224
Cdd:TIGR00606 471 DRILELDQELRKAERElskAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQ 536
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
12-153 |
4.55e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 38.37 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 12 RLQQREkEALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEhrkLEALQVALQEERQAWIKQEHQLKERLQALQEE 91
Cdd:pfam08614 11 RLLDRT-ALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQS---LEQLLAQLREELAELYRSRGELAQRLVDLNEE 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081119 92 GQAQLEREKGNSQREAQAawetQQQFALLQTEVRRLEGDL-------DTVRRERDALQLEMSLVQARYE 153
Cdd:pfam08614 87 LQELEKKLREDERRLAAL----EAERAQLEEKLKDREEELrekrklnQDLQDELVALQLQLNMAEEKLR 151
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
8-282 |
4.76e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 40.12 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 8 QEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQ------EERQAWIK----Q 77
Cdd:pfam07111 344 QEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKfvvnamSSTQIWLEttmtR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 78 EHQLKERLQALQEEGQAQLERE---KGNSQREAQAAwETQQQFALLQTEVRRLEGD----LDTVRRERD----ALQLEMS 146
Cdd:pfam07111 424 VEQAVARIPSLSNRLSYAVRKVhtiKGLMARKVALA-QLRQESCPPPPPAPPVDADlsleLEQLREERNrldaELQLSAH 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 147 LVQARYESQRIQME------SELAVQLE---QRVTERLA----------EAQENSLRQAASLRDHHRKQlQELSGQHQQE 207
Cdd:pfam07111 503 LIQQEVGRAREQGEaerqqlSEVAQQLEqelQRAQESLAsvgqqlevarQGQQESTEEAASLRQELTQQ-QEIYGQALQE 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 208 LAAQL-AQFKVEMADREERQQQVAQDYE---LRLAREQARVRDLKSGNQQL----EEQRAELVERLQAMLQAHWEEANQL 279
Cdd:pfam07111 582 KVAEVeTRLREQLSDTKRRLNEARREQAkavVSLRQIQHRATQEKERNQELrrlqDEARKEEGQRLARRVQELERDKNLM 661
|
...
gi 1907081119 280 LST 282
Cdd:pfam07111 662 LAT 664
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
6-258 |
4.81e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 6 REQEGARLQQREKEAlEEERQALTLRLEVEQQQCRTLQEERDEARAGQ----LSEHRKLEALQVALQEERQAWIKQEHQL 81
Cdd:PTZ00121 1200 RKAEAARKAEEERKA-EEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEeernNEEIRKFEEARMAHFARRQAAIKAEEAR 1278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 82 K-ERLQALQEEGQAQlEREKGNSQREAQAAWETQQQfallQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQME 160
Cdd:PTZ00121 1279 KaDELKKAEEKKKAD-EAKKAEEKKKADEAKKKAEE----AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 161 selAVQLEQRVTERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQELAAQLAQFKVEMADREERQQQVAQDYElRLARE 240
Cdd:PTZ00121 1354 ---AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK-KKAEE 1429
|
250
....*....|....*...
gi 1907081119 241 QARVRDLKsgnQQLEEQR 258
Cdd:PTZ00121 1430 KKKADEAK---KKAEEAK 1444
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
58-173 |
5.04e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.06 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 58 RKLEALQVALQEERQAWIK-QEHQLKERLQALQEEgQAQLEREkgnsQREAQAAWETQQQfalLQTEVRRLEGDLDTVRR 136
Cdd:COG0542 414 DELERRLEQLEIEKEALKKeQDEASFERLAELRDE-LAELEEE----LEALKARWEAEKE---LIEEIQELKEELEQRYG 485
|
90 100 110
....*....|....*....|....*....|....*..
gi 1907081119 137 ERDALQLEMSLVQARyesqriqmESELAVQLEQRVTE 173
Cdd:COG0542 486 KIPELEKELAELEEE--------LAELAPLLREEVTE 514
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1-107 |
5.06e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 1 MEALSREQEgARLQQRE---KEALEEERQALTLRLEVEQQQCRTLQEERdearagQLSEH-RKLEALQVALQEERQAWIK 76
Cdd:PRK12704 49 KEAEAIKKE-ALLEAKEeihKLRNEFEKELRERRNELQKLEKRLLQKEE------NLDRKlELLEKREEELEKKEKELEQ 121
|
90 100 110
....*....|....*....|....*....|....
gi 1907081119 77 QEHQLKER---LQALQEEGQAQLEREKGNSQREA 107
Cdd:PRK12704 122 KQQELEKKeeeLEELIEEQLQELERISGLTAEEA 155
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
7-185 |
5.56e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 7 EQEGARLQQREKE-ALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQehQLKERL 85
Cdd:COG3206 195 EAALEEFRQKNGLvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQ--QLRAQL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 86 QALQEEgQAQLEREKGNSQREAQAAwetQQQFALLQTEVR-RLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELA 164
Cdd:COG3206 273 AELEAE-LAELSARYTPNHPDVIAL---RAQIAALRAQLQqEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE 348
|
170 180
....*....|....*....|.
gi 1907081119 165 VQLEQRVTERLAEAQENSLRQ 185
Cdd:COG3206 349 LEAELRRLEREVEVARELYES 369
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2-276 |
5.95e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 2 EALSREQEGARLQQrEKEALEEERQALTLRLEVEQQQCRTLQEERDEARA--GQLSEHR-KLEALQVALQEERQAWIKQE 78
Cdd:PRK02224 350 DADDLEERAEELRE-EAAELESELEEAREAVEDRREEIEELEEEIEELRErfGDAPVDLgNAEDFLEELREERDELRERE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 79 HQLKERLQALQ---EEGQAQLEREK----GNSQRE---AQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQlemSLV 148
Cdd:PRK02224 429 AELEATLRTARervEEAEALLEAGKcpecGQPVEGsphVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE---DLV 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 149 QARYESQRIQMESELavqLEQRVTERLAEAQENSLRqAASLRD------------HHRKQLQELSGQHQQELAAQLAQFK 216
Cdd:PRK02224 506 EAEDRIERLEERRED---LEELIAERRETIEEKRER-AEELREraaeleaeaeekREAAAEAEEEAEEAREEVAELNSKL 581
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081119 217 VEMADREERQQQVA------QDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQAMLQAHWEEA 276
Cdd:PRK02224 582 AELKERIESLERIRtllaaiADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEAR 647
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
114-284 |
6.42e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 39.31 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 114 QQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQmESELAVQLEQRVTERLAEAQENSLRQAASLrDHH 193
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQ-EARREREELQREEERLVQKEEQLDARAEKL-DNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 194 RKQLQELSgqhqQELAAQLAQFKVEMADREERQQQVAQdyelrLAREQARVRDLKSGNQQLEEQRAELVERLQAMLQAHW 273
Cdd:PRK12705 104 ENQLEERE----KALSARELELEELEKQLDNELYRVAG-----LTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEA 174
|
170
....*....|..
gi 1907081119 274 E-EANQLLSTTL 284
Cdd:PRK12705 175 ErKAQNILAQAM 186
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1-116 |
6.70e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 39.13 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 1 MEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAwIKQEHQ 80
Cdd:pfam13868 158 LEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKK-ARQRQE 236
|
90 100 110
....*....|....*....|....*....|....*.
gi 1907081119 81 LKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQ 116
Cdd:pfam13868 237 LQQAREEQIELKERRLAEEAEREEEEFERMLRKQAE 272
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
15-267 |
7.32e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.39 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 15 QREKEALEEERQALTLRLEVEQQQCrtlqEERDEARAGQLSEHRKLEALQVALQ---EERQAWIKQEHQLKERLQALQEE 91
Cdd:pfam01576 32 EKKHQQLCEEKNALQEQLQAETELC----AEAEEMRARLAARKQELEEILHELEsrlEEEEERSQQLQNEKKKMQQHIQD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 92 GQAQLEREKGNSQReaqaaweTQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARY---------ESQRIQMESE 162
Cdd:pfam01576 108 LEEQLDEEEAARQK-------LQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERIseftsnlaeEEEKAKSLSK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 163 LAVQLEQRVTErLAEAQENSLRQAASLRDHHRKQLQELSGQHQQ--ELAAQLAQFKVEMADREERqqqvAQDYELRLARE 240
Cdd:pfam01576 181 LKNKHEAMISD-LEERLKKEEKGRQELEKAKRKLEGESTDLQEQiaELQAQIAELRAQLAKKEEE----LQAALARLEEE 255
|
250 260
....*....|....*....|....*..
gi 1907081119 241 QARVRDLKSGNQQLEEQRAELVERLQA 267
Cdd:pfam01576 256 TAQKNNALKKIRELEAQISELQEDLES 282
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
47-214 |
8.02e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.55 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 47 DEARAgQLSEHRKLEAlqvalQEERQAWIKQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRR 126
Cdd:COG3096 495 QTARE-LLRRYRSQQA-----LAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEE 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 127 LEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAVQ-----LEQRVTERLAEAQE-NSLRQAASLRDHHRKQLQEL 200
Cdd:COG3096 569 LEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQdalerLREQSGEALADSQEvTAAMQQLLEREREATVERDE 648
|
170
....*....|....
gi 1907081119 201 SGQHQQELAAQLAQ 214
Cdd:COG3096 649 LAARKQALESQIER 662
|
|
| bZIP_Maf_small |
cd14717 |
Basic leucine zipper (bZIP) domain of small musculoaponeurotic fibrosarcoma (Maf) proteins: a ... |
80-142 |
8.40e-03 |
|
Basic leucine zipper (bZIP) domain of small musculoaponeurotic fibrosarcoma (Maf) proteins: a DNA-binding and dimerization domain; Maf proteins are Basic leucine zipper (bZIP) transcription factors that may participate in the activator protein-1 (AP-1) complex, which is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. Maf proteins fall into two groups: small and large. The small Mafs (MafF, MafK, and MafG) do not contain a transactivation domain but do harbor the anxillary DNA-binding domain and a C-terminal bZIP domain. They form dimers with cap'n'collar (CNC) proteins that harbor transactivation domains, and they act either as activators or repressors depending on their dimerization partner. CNC transcription factors include NFE2 (nuclear factor, erythroid-derived 2) and similar proteins NFE2L1 (NFE2-like 1), NFE2L2, and NFE2L3, as well as BACH1 and BACH2. Small Mafs play roles in stress response and detoxification pathways. They also regulate the expression of betaA-globin and other genes activated during erythropoiesis. They have been implicated in various diseases such as diabetes, neurological diseases, thrombocytopenia and cancer. Triple deletion of the three small Mafs is embryonically lethal. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.
Pssm-ID: 269865 [Multi-domain] Cd Length: 70 Bit Score: 35.42 E-value: 8.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081119 80 QLKERLQALQEEGQAQLEREKGNSQREaqaawETQQQFALLQTEVRRLEGDLDTVRRERDALQ 142
Cdd:cd14717 6 RLKQRRRTLKNRGYAASCRIKRVTQKE-----ELEKQKAELQQEVEKLARENASMRLELDALR 63
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
58-279 |
8.46e-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: 39.03 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 58 RKLEALQVALQEERQAWIKQEHQ-LKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFA---LLQTEVRRLEGDLDT 133
Cdd:pfam10174 48 RKEEAARISVLKEQYRVTQEENQhLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFStpeLTEENFRRLQSEHER 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 134 VRRERDALQLEMSLVQARYESQRIQMESElavqlEQRVTERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQELAAQLA 213
Cdd:pfam10174 128 QAKELFLLRKTLEEMELRIETQKQTLGAR-----DESIKKLLEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLD 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081119 214 QFKVE-MADREE--RQQQVAQD------YELRLAREQARVRDLKSGNQQLEEQRAELVERLQAMLQAHWEEANQL 279
Cdd:pfam10174 203 QKEKEnIHLREElhRRNQLQPDpaktkaLQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQM 277
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
113-311 |
9.51e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.73 E-value: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 113 TQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESElavQLEQRVTERLAEAQENSLRQAASLRDH 192
Cdd:COG4372 22 TGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQA---RSELEQLEEELEELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 193 HRKQLQELSGQhQQELAAQLAQFKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQAMLQAH 272
Cdd:COG4372 99 AQEELESLQEE-AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907081119 273 WEEANQLLSTTLLPPNPQAPLAEPSSPGPLEPEKGERRT 311
Cdd:COG4372 178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPREL 216
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
14-280 |
9.59e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 38.36 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 14 QQREKEALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRK-----LEALQVALQEERQAWIKQEHQLKERLQAL 88
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQeleeqIEEREQKRQEEYEEKLQEREQMDEIVERI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 89 QEEGQAQLErEKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMEselavqlE 168
Cdd:pfam13868 111 QEEDQAEAE-EKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEE-------K 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 169 QRVTERLAEAQENSLRQAASLRDHHRKQLQE--LSGQHQQELAAQLAQFKVEMADREERQQQVAQDYELR---LAREQAR 243
Cdd:pfam13868 183 EREIARLRAQQEKAQDEKAERDELRAKLYQEeqERKERQKEREEAEKKARQRQELQQAREEQIELKERRLaeeAEREEEE 262
|
250 260 270
....*....|....*....|....*....|....*..
gi 1907081119 244 VRDLKSGNQQLEEQRAELVERLQAMLQAHWEEANQLL 280
Cdd:pfam13868 263 FERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQI 299
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1-248 |
9.76e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 38.36 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 1 MEALSREQEGARLQQREKEALEEERQALTLRLEVEQQ-------QCRTLQEERDEARAGQLSEHRKLEALQVALQEERQA 73
Cdd:pfam13868 91 EEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQlreeideFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 74 WIKQEHQLKERLQALQEEGQAQLEREKgNSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLvQARYE 153
Cdd:pfam13868 171 REAEREEIEEEKEREIARLRAQQEKAQ-DEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREE-QIELK 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081119 154 SQRIQMESELAVQLEQRVTERLAEAQENSLRQAAslrdhhrkQLQELSGQHQQELAAQLAQFKVEMADREERQQQVAQDY 233
Cdd:pfam13868 249 ERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAE--------KRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERL 320
|
250
....*....|....*
gi 1907081119 234 ELRLAREQARVRDLK 248
Cdd:pfam13868 321 REEEAERRERIEEER 335
|
|
| |
