|
Name |
Accession |
Description |
Interval |
E-value |
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
47-411 |
4.61e-109 |
|
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.
Pssm-ID: 462869 [Multi-domain] Cd Length: 303 Bit Score: 325.50 E-value: 4.61e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 47 DIRMRELERQQREpshhhsfdrkwgeihkwledseraryshrsghrrpylgvedtlslrslgshrLDEKSDKQYAENYT- 125
Cdd:pfam09738 17 EIRMRELERQQKE----------------------------------------------------VEENADRVFDMSSSs 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 126 --------RPSSRNSASATTPLSGNSSRRGSGDTSSLIDPDTSLSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVD 197
Cdd:pfam09738 45 gadtasgsPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISNAQLDNEKSNLMYQVD 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 198 TLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEalekqkehiaclrnerdvlreela 277
Cdd:pfam09738 125 LLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIE------------------------ 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 278 dlrqtvttaeKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEGPLDVRLRKLAGEKDELLSQIRKLKLQLE 357
Cdd:pfam09738 181 ----------KHGLVIVPDENTNGEEENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLE 250
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1720432708 358 EERQ-KCSRNDGMSGDLAGLQNGSDLqfIEMQRDANRQISEYKFKLSKAEQDIAT 411
Cdd:pfam09738 251 EEKSkRNSTRSSQSPDGFGLENGSHV--IEVQREANKQISDYKFKLQKAEQEITT 303
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
161-461 |
7.10e-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: 58.53 E-value: 7.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 161 LSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQhkmDE 240
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE---EE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 241 LKEGLRQRDELIEALEKQKEHIACLRNERDVLREELADLRQTVTTAEkhglviipdstpNGDVHHEPVVGAITAVSQEAA 320
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR------------ERLESLERRIAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 321 QVLESAGEgpldvRLRKLAGEKDELLSQIRKLKLQLEE-ERQKCSRNDGMSGDLAGLQN-GSDLQFIEMQR-DANRQISE 397
Cdd:TIGR02168 845 EQIEELSE-----DIESLAAEIEELEELIEELESELEAlLNERASLEEALALLRSELEElSEELRELESKRsELRRELEE 919
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720432708 398 YKFKLSKAEQDIATLEQSISRLEGQVL-RYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEM 461
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
199-486 |
4.01e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 199 LKDVIEEQEEQM---------AEFYRENEEKSKELERQkhmcsVLQHKMDELKEGLRQRDELIEALEKQKEHiacLRNER 269
Cdd:COG1196 191 LEDILGELERQLeplerqaekAERYRELKEELKELEAE-----LLLLKLRELEAELEELEAELEELEAELEE---LEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 270 DVLREELADLRQTVTTAEKhglviipdstpngdvhhepvvgAITAVSQEAAQVLESAGEgpLDVRLRKLAGEKDELLSQI 349
Cdd:COG1196 263 AELEAELEELRLELEELEL----------------------ELEEAQAEEYELLAELAR--LEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 350 RKLKLQLEEERQKcsrndgmsgdlaglqngsdlqfiemQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTA 429
Cdd:COG1196 319 EELEEELAELEEE-------------------------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720432708 430 AENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 486
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
154-461 |
7.88e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 7.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 154 LIDPDTSLSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSV 233
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 234 LQHKMDELKEGLRQ----RDELIEALEKQKEHIACLRNERDVLREELADLRQTVTTAEKHglviIPDSTPNGDVHHEPVV 309
Cdd:TIGR02168 801 LREALDELRAELTLlneeAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE----IEELEELIEELESELE 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 310 GA--ITAVSQEAAQVLESAGEGpLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSrndGMSGDLAGLQNGSDLQFIEM 387
Cdd:TIGR02168 877 ALlnERASLEEALALLRSELEE-LSEELRELESKRSELRRELEELREKLAQLELRLE---GLEVRIDNLQERLSEEYSLT 952
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720432708 388 QRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEM 461
Cdd:TIGR02168 953 LEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
230-485 |
9.93e-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: 50.92 E-value: 9.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 230 MCSVLQHKMDELKEGLRQRDELIEALEKQKEHIACLRNERDVLREELADLRQTVTTAEKhglviipdstpngdvhhepvv 309
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR--------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 310 gAITAVSQEAAQvlesagegpLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNdGMSGDLAGLQNGSDLQFIEMQR 389
Cdd:COG4942 70 -RIRALEQELAA---------LEAELAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFLDAVRRL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 390 DANRQISEYKfklskaEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLA 469
Cdd:COG4942 139 QYLKYLAPAR------REQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
|
250
....*....|....*.
gi 1720432708 470 KRLEKMKANRTALLAQ 485
Cdd:COG4942 213 AELAELQQEAEELEAL 228
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
161-462 |
2.17e-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: 50.45 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 161 LSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFyrenEEKSKELERqkhmcSVLQHKMDE 240
Cdd:TIGR02169 725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL----EEALNDLEA-----RLSHSRIPE 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 241 LKEGLRQRDELIEALEKQKEHIACLRNERDVLREELADLRQTvttaekhgLVIIPDSTPNGDVHHEPVVGAITAVSQEAA 320
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE--------LQEQRIDLKEQIKSIEKEIENLNGKKEELE 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 321 QVLE--SAGEGPLDVRLRKLAGEKDELLSQIRKLKL---QLEEERQKcsRNDGMSGDLAGLQNGSD-LQFIEMQRDANRQ 394
Cdd:TIGR02169 868 EELEelEAALRDLESRLGDLKKERDELEAQLRELERkieELEAQIEK--KRKRLSELKAKLEALEEeLSEIEDPKGEDEE 945
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720432708 395 ISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEME 462
Cdd:TIGR02169 946 IPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
160-462 |
5.01e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 160 SLSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDvieeqeeQMAEFYRENEEKSKELERQKHMCSVLQHKMD 239
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL-------EVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 240 ELKEGLRQRDELIEALEKQKEHiacLRNERDVLREELADLRQTVTTAEKhglviipdstpngdvHHEPVVGAITAvSQEA 319
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEE---LESKLDELAEELAELEEKLEELKE---------------ELESLEAELEE-LEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 320 AQVLESAGEGpLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRndgmsgdlaglQNGSDLQFIEMQRDANRQISEYK 399
Cdd:TIGR02168 367 LEELESRLEE-LEEQLETLRSKVAQLELQIASLNNEIERLEARLER-----------LEDRRERLQQEIEELLKKLEEAE 434
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720432708 400 FKLSKAEqdIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEME 462
Cdd:TIGR02168 435 LKELQAE--LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
199-485 |
6.59e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 6.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 199 LKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLR----QRDELIEALEKQKEHIACLRNERDVLRE 274
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGeiekEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 275 ELADLRQTVTTAEKhglviipdstpngdvhhepVVGAITAVSQEAAQVLESAGEGPLDVRLRKLAGEKDELLSQIRKLKL 354
Cdd:TIGR02169 752 EIENVKSELKELEA-------------------RIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 355 QLEEERQKCSRNDgmsgdlaglqngSDLQFIEMQR-DANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENA 433
Cdd:TIGR02169 813 RLREIEQKLNRLT------------LEKEYLEKEIqELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1720432708 434 EKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 485
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
195-433 |
2.66e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 195 QVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEALEKQkehIACLRNERDVLRE 274
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE---IAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 275 ELADLRQTVTTAEKHG--LVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEgpldvRLRKLAGEKDELLSQIRKL 352
Cdd:COG4942 105 ELAELLRALYRLGRQPplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-----ELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 353 KLQLEEERQKcsrndgmsgdLAGLQNGSDlqfiEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAEN 432
Cdd:COG4942 180 LAELEEERAA----------LEALKAERQ----KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
.
gi 1720432708 433 A 433
Cdd:COG4942 246 A 246
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
239-477 |
5.46e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 239 DELKEGLRQRDELIEALEKQKEHIACLRNERDvLREELADLRQTVTTAEKHGLviipdstpngdvhhepvvGAITAVSQE 318
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEPIRE-LAERYAAARERLAELEYLRA------------------ALRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 319 AAQVLESAGEGpLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGmsGDLAGLQNgsDLQFIEMQRD-ANRQISE 397
Cdd:COG4913 289 RLELLEAELEE-LRAELARLEAELERLEARLDALREELDELEAQIRGNGG--DRLEQLER--EIERLERELEeRERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 398 YKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKI----EDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLE 473
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEAleeaLAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
....
gi 1720432708 474 KMKA 477
Cdd:COG4913 444 ALRD 447
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
195-477 |
9.14e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 9.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 195 QVDTLKDVIEEQEEQMAEFYRENEEKSK----ELERQKHMCSVLQHKMDELKEGLRQRDELIEALEKQKEHIACLRNERD 270
Cdd:TIGR02169 185 NIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 271 VLREELADLRQTVTT--AEKHGLVIIPDSTPNGDVHHE--PVVGAITAVSQEAAQvlesagegpLDVRLRKLAGEKDELL 346
Cdd:TIGR02169 265 KRLEEIEQLLEELNKkiKDLGEEEQLRVKEKIGELEAEiaSLERSIAEKERELED---------AEERLAKLEAEIDKLL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 347 SQIRKLKLQLEEERQkcsRNDGMSGDLAGLQNGSDLQFIEMQ------RDANRQISEYKFKLSKAEQDIATLEQSISRLE 420
Cdd:TIGR02169 336 AEIEELEREIEEERK---RRDKLTEEYAELKEELEDLRAELEevdkefAETRDELKDYREKLEKLKREINELKRELDRLQ 412
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720432708 421 GQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKA 477
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
185-450 |
1.31e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 185 LDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKElerqkHMCSVLQHKM--DELKEGLRqrdELIEALEKQKEHI 262
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDE-----LVEEAKTIKAeiEELTDELL---NLVMDIEDPSAAL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 263 ACLRNERDVLREELADLRQTVTTAEKHGlvIIPDSTpngdvhhepvvgaitavsqeaaQVLESAGEgpldvRLRKLAGEK 342
Cdd:PHA02562 258 NKLNTAAAKIKSKIEQFQKVIKMYEKGG--VCPTCT----------------------QQISEGPD-----RITKIKDKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 343 DELLSQIRKLKLQLEEERQKCSrndgmsgdlaglqngsdlQFIEMQR---DANRQISEYKFKLSKAEQDIATLEQSISRL 419
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEEIMD------------------EFNEQSKkllELKNKISTNKQSLITLVDKAKKVKAAIEEL 370
|
250 260 270
....*....|....*....|....*....|.
gi 1720432708 420 EGQVLRYKTAAENAEKIEDELKAERRKLQRE 450
Cdd:PHA02562 371 QAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
161-459 |
1.78e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 161 LSELRESLSEVEEKYKKA-----MVSNAQLDNEK--------NNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQ 227
Cdd:PRK04863 316 LAELNEAESDLEQDYQAAsdhlnLVQTALRQQEKieryqadlEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDEL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 228 KHMCSVLQHKMDELKEGLRQRDELIEALEKQK--------------EHIACLRNERDVLREELADLRQTVTTAEkhglvi 293
Cdd:PRK04863 396 KSQLADYQQALDVQQTRAIQYQQAVQALERAKqlcglpdltadnaeDWLEEFQAKEQEATEELLSLEQKLSVAQ------ 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 294 ipdstpngdvhhepvvgaitAVSQEAAQVLESagegpldvrLRKLAGEKD--ELLSQIRKLKLQLEEERQKCSRNDGMSG 371
Cdd:PRK04863 470 --------------------AAHSQFEQAYQL---------VRKIAGEVSrsEAWDVARELLRRLREQRHLAEQLQQLRM 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 372 DLAGLQngsdlQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENA-------EKIEDELKAER 444
Cdd:PRK04863 521 RLSELE-----QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEArerrmalRQQLEQLQARI 595
|
330
....*....|....*...
gi 1720432708 445 RKLQR---ELRTAQDKIE 459
Cdd:PRK04863 596 QRLAArapAWLAAQDALA 613
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
161-476 |
2.41e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 161 LSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDE 240
Cdd:TIGR04523 323 LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 241 LKEGLRQRDELIEALEKQKE----HIACLRNERDVLREELADLrqtvtTAEKHGLVIIPDStpngdvhhepvvgaitavs 316
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKEllekEIERLKETIIKNNSEIKDL-----TNQDSVKELIIKN------------------- 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 317 qeaaqvlesagegpLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAglQNGSDLQfiEMQRDANRQIS 396
Cdd:TIGR04523 459 --------------LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN--EEKKELE--EKVKDLTKKIS 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 397 EYKFKLSKAEQDIATLEQSISRLEgqvlryktaaENAEKIEDELKaeRRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMK 476
Cdd:TIGR04523 521 SLKEKIEKLESEKKEKESKISDLE----------DELNKDDFELK--KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQ 588
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
156-462 |
3.35e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 156 DPDTSLSELRESLSEVEEKykkamvsnaQLDNEKNNLIYQVDTLKDVIEEQEEQmaefyRENEEKSKElerqkhmcsVLQ 235
Cdd:PRK02224 184 DQRGSLDQLKAQIEEKEEK---------DLHERLNGLESELAELDEEIERYEEQ-----REQARETRD---------EAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 236 HKMDELKEGLRQRDELIEALEKQKEHIACLRNERDVLREELADLRQTVTTAEKhglviipdstpngdvhhepvvgAITAV 315
Cdd:PRK02224 241 EVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEE----------------------ERDDL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 316 SQEAAqvLESAGEGPLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAGlqNGSDLQfiEMQRDANRQI 395
Cdd:PRK02224 299 LAEAG--LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE--RAEELR--EEAAELESEL 372
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720432708 396 SEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAER-------RKLQRELRTAQDKIEEME 462
Cdd:PRK02224 373 EEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERdelrereAELEATLRTARERVEEAE 446
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
319-486 |
5.27e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 319 AAQVLESAGEG--PLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRndgMSGDLAGLQnGSDLQFIEMQRDANRQIS 396
Cdd:TIGR02168 230 LVLRLEELREEleELQEELKEAEEELEELTAELQELEEKLEELRLEVSE---LEEEIEELQ-KELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 397 EYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMK 476
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170
....*....|
gi 1720432708 477 ANRTALLAQQ 486
Cdd:TIGR02168 386 SKVAQLELQI 395
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
331-485 |
1.86e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 331 LDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAglqngSDLQFIEMQ-RDANRQISEYKFKLSKA---- 405
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE-----KEIKRLELEiEEVEARIKKYEEQLGNVrnnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 406 -----EQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEmtnSHLAKRLEKMKANRT 480
Cdd:COG1579 90 eyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL---AELEAELEELEAERE 166
|
....*
gi 1720432708 481 ALLAQ 485
Cdd:COG1579 167 ELAAK 171
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
245-454 |
1.92e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 245 LRQRDELIEALEKQKEHIACLRNERDVLREELADLRQtvttaekhglviipdstpngdvhhepvvgAITAVSQEAAQVLE 324
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-----------------------------ELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 325 SAGEGPLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSK 404
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720432708 405 AEQDIATLEQSISRLEGQVLRYKTAAENAEKiEDELKAERRKLQRELRTA 454
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLL 252
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
389-477 |
2.09e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 389 RDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELkaerRKLQRELRTAQDKIEEMEMTNSHL 468
Cdd:COG2433 416 RRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREI----SRLDREIERLERELEEERERIEEL 491
|
....*....
gi 1720432708 469 AKRLEKMKA 477
Cdd:COG2433 492 KRKLERLKE 500
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
206-461 |
2.74e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 206 QEEQMAEFYRENEEKSKELERQkhmcsvlqhkMDELKEGLRQRDELIEALeKQKEHIACLRNERDVLREELADLRQTVTT 285
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQ----------LPELRKELEEAEAALEEF-RQKNGLVDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 286 AEkhglviipdstpngdvhhepvvGAITAVSQEAAQVLESAGEGPLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSR 365
Cdd:COG3206 231 AR----------------------AELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTP 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 366 NDgmsgdlaglqngSDLQFIEMQRDANRQI--SEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELkae 443
Cdd:COG3206 289 NH------------PDVIALRAQIAALRAQlqQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL--- 353
|
250
....*....|....*...
gi 1720432708 444 rRKLQRELRTAQDKIEEM 461
Cdd:COG3206 354 -RRLEREVEVARELYESL 370
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
184-486 |
2.83e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 184 QLDNEKNNLiyqvDTLKDVIEEQEEQM---------AEFYRENEEKSKELERqkhmcSVLQHKMDELKEGLRQRDELIEA 254
Cdd:TIGR02168 180 KLERTRENL----DRLEDILNELERQLkslerqaekAERYKELKAELRELEL-----ALLVLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 255 LEKQKEHIAclrNERDVLREELADLRqtvttaekhglviipdstpngDVHHEpvvgaitavsqeaaqvlesagegpLDVR 334
Cdd:TIGR02168 251 AEEELEELT---AELQELEEKLEELR---------------------LEVSE------------------------LEEE 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 335 LRKLAGEKDELLSQIRKLKLQLEEERQKcsrndgmsgdLAGLQNgsDLQFIEMQRDAN-RQISEYKFKLSKAEQDIATLE 413
Cdd:TIGR02168 283 IEELQKELYALANEISRLEQQKQILRER----------LANLER--QLEELEAQLEELeSKLDELAEELAELEEKLEELK 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 414 QSISRLEGQVLRYKTAAENAEKIEDEL-------KAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 486
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELeeqletlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
265-462 |
2.96e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 265 LRNERDVLREELADLRQTVTTAE--------KHGLViipdstpngdvhhepvvgaitAVSQEAAQVLESAGEgpLDVRLR 336
Cdd:COG3206 173 ARKALEFLEEQLPELRKELEEAEaaleefrqKNGLV---------------------DLSEEAKLLLQQLSE--LESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 337 KLAGEKDELLSQIRKLKLQLEEERQkcsrndgmsgDLAGLQNGSDLQFIEMQR-DANRQISEYKFKLSKAEQDIATLEQS 415
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPD----------ALPELLQSPVIQQLRAQLaELEAELAELSARYTPNHPDVIALRAQ 299
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720432708 416 ISRLEGQVlryktaAENAEKIEDELKAERRKLQRELRTAQDKIEEME 462
Cdd:COG3206 300 IAALRAQL------QQEAQRILASLEAELEALQAREASLQAQLAQLE 340
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
391-486 |
4.77e-03 |
|
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: 39.36 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 391 ANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAK 470
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90
....*....|....*.
gi 1720432708 471 RLEKMKAnrtaLLAQQ 486
Cdd:COG4942 98 ELEAQKE----ELAEL 109
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
161-474 |
6.53e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 161 LSELRESLSEVEEKYKkamvsnaQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQkhmcsvLQHKMDE 240
Cdd:COG4717 134 LEALEAELAELPERLE-------ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE------LQDLAEE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 241 LKEGLRQRDELIEALEKQKEHIACLRNERDVLREELADLRQTVTTAEKHGLVIIpdstpngdvhhepvVGAITAVSQEAA 320
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLI--------------AAALLALLGLGG 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 321 QVLESAGE---------GPLDVRLRKLAGEKDELLSQIRKLKLQLEEERqkcSRNDGMSGDLAGLQNGSDLQfIEMQRDA 391
Cdd:COG4717 267 SLLSLILTiagvlflvlGLLALLFLLLAREKASLGKEAEELQALPALEE---LEEEELEELLAALGLPPDLS-PEELLEL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 392 NRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIED--ELKAERRKLQRELRTAQDKIEEMEMTNSHLA 469
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAalEQAEEYQELKEELEELEEQLEELLGELEELL 422
|
....*
gi 1720432708 470 KRLEK 474
Cdd:COG4717 423 EALDE 427
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
391-460 |
6.68e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.66 E-value: 6.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 391 ANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEE 460
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
158-279 |
7.27e-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: 38.90 E-value: 7.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 158 DTSLSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQM-------AEFYRENEEKSKELERQKHM 230
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIenlngkkEELEEELEELEAALRDLESR 883
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1720432708 231 CSVLQHKMDELKEGLRQ----RDELIEALEKQKEHIACLRNERDVLREELADL 279
Cdd:TIGR02169 884 LGDLKKERDELEAQLRElerkIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
331-485 |
9.18e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 9.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432708 331 LDVRLRKLAGEKDELLSQIRKLKLQLEEERQkcsrndgmsgdlaglqngsdlqfiemQRDANRQISEYKFklskAEQDIA 410
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQE--------------------------RREALQRLAEYSW----DEIDVA 664
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720432708 411 TLEQSISRLEGQvlryKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 485
Cdd:COG4913 665 SAEREIAELEAE----LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
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