|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
104-416 |
9.57e-141 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 405.46 E-value: 9.57e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 104 NEKITMQNLNDRLASYLDKVRALEEANADLEVKIHDWYQKQTPtSPECDYSQYFKTIEELRDKIMATTIDNSRVILEIDN 183
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGA-EPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 184 ARLAADDFRLKYENELALRQGVEADINGLRRVLDELTLARTDLEMQIEGLNEELAYLKKNHEEEMKEFSSQLA-GQVNVE 262
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 263 MDAAPGVDLTRVLAEMREQYEAMAEKNRRDVEAWFFSKTEELNKEVASNTEMIQTSKTEITDLRRTMQELEIELQSQLSM 342
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519473574 343 KAGLENSLAETECRYATQLQQIQGLIGGLEAQLSELRCEMEAQNQEYKMLLDIKTRLEQEIATYRSLLEGQDAK 416
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
122-420 |
3.85e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 122 KVRALEEANADLEVKIHDWYQKQTptSPECDYSQYFKTIEELRDKIMATTIDNSRVILEIDNARLAADDFRLKYENELAL 201
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELE--ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 202 RQGVEADINGLRRVLDELTLARTDLEMQIEGLNEELAYLKKNHEEEMKEFSsqlagqvnvemdaapgvdLTRVLAEMREQ 281
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT------------------LLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 282 YEAMAEKNRRDVEAWFfsktEELNKEVASNTEMIQTSKTEITDLRRTMQELEIELQSQLSMKAGLENSLAETECRYATQL 361
Cdd:TIGR02168 825 RLESLERRIAATERRL----EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519473574 362 QQIQGL---IGGLEAQLSELRCEMEA-QNQEYKMLLDIKTRLEQEIATYRSLLEGQDAKMAGI 420
Cdd:TIGR02168 901 EELRELeskRSELRRELEELREKLAQlELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKI 963
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
180-385 |
1.61e-06 |
|
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: 50.15 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 180 EIDNARLAADDFRLKYENELALRQGVEADINGLRRVLDELTLARTDLEMQIEGLNEELAYLKKNHEEEMKEFSSQLA--- 256
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRaly 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 257 --GQVNVEMDAAPGVDLTRvLAEMREQYEAMAEKNRRDVEAWffsktEELNKEVASNTEMIQTSKTEITDLRRTMQELEI 334
Cdd:COG4942 115 rlGRQPPLALLLSPEDFLD-AVRRLQYLKYLAPARREQAEEL-----RADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1519473574 335 ELQSQLSMKAGLENSLAETECRYATQLQQIQGLIGGLEAQLSELRCEMEAQ 385
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
186-425 |
7.83e-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: 44.75 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 186 LAADDFRLKYENELalrQGVEADINGLRRVLDELTLARTDLEMQIEGLNEELAYLKK---NHEEEMKEFSSQLAgQVNVE 262
Cdd:COG4942 16 AAQADAAAEAEAEL---EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEAELA-ELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 263 MDAapgvdLTRVLAEMREQYEAM---AEKNRRDVEAWFFSKTEELNKEVASNT---EMIQTSKTEITDLRRTMQELEIEL 336
Cdd:COG4942 92 IAE-----LRAELEAQKEELAELlraLYRLGRQPPLALLLSPEDFLDAVRRLQylkYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 337 QSQLSMKAGLENSLAETEcryaTQLQQIQGLIGGLEAQLSELRCEMEAQNQEYKmlldiktRLEQEIATYRSLLEGQDAK 416
Cdd:COG4942 167 AELEAERAELEALLAELE----EERAALEALKAERQKLLARLEKELAELAAELA-------ELQQEAEELEALIARLEAE 235
|
....*....
gi 1519473574 417 MAGIAIREA 425
Cdd:COG4942 236 AAAAAERTP 244
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
194-425 |
8.19e-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: 8.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 194 KYENELALRQGVEADINGLRRVLDELTLARTDLEMQIEGLNEEL----AYLKKNHEEEMKEFSSQLA---GQV------- 259
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLeelnKKIKDLGEEEQLRVKEKIGeleAEIaslersi 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 260 ---NVEMDAAPG------VDLTRVLAEMREQYEAMAE------------KNRRDVEAWFFSKTEELNKEVASNTEMIQTS 318
Cdd:TIGR02169 311 aekERELEDAEErlakleAEIDKLLAEIEELEREIEEerkrrdklteeyAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 319 KTEITDLRRTMQELEIELQSQLSMKAGLENSLAETEcryaTQLQQIQGLIGGLEAQLSELRCEMEAQNQEYKMLLDIKTR 398
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
250 260 270
....*....|....*....|....*....|.
gi 1519473574 399 LEQEI----ATYRSLLEGQDAKMAGIAIREA 425
Cdd:TIGR02169 467 YEQELydlkEEYDRVEKELSKLQRELAEAEA 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
193-425 |
8.93e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 193 LKYENELALRQGVEADINGLRRVLDELTLARTDLEMQIEGLNEELAYLKKNHEEEMKEFSSQLAGQVNVEMDAAPGVDLT 272
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 273 RVLAEMREQYEAMAEKNRRDVEAwFFSKTEELNKEVASNTEMIQTSKTEITDLRRTMQELEIELQSQLSMKAGLENSLAE 352
Cdd:COG1196 312 RELEERLEELEEELAELEEELEE-LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519473574 353 TEcryaTQLQQIQGLIGGLEAQLSELRCEMEAQNQEYKMLLDIKTRLEQEIATYRSLLEGQDAKMAGIAIREA 425
Cdd:COG1196 391 AL----RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
194-425 |
1.20e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 194 KYENELAL--RQGVEADINGLRRVLDELTLARTDLEMQIEGLNEELAYLKKNHEEEMKEFSSQLAGQVNVEMDAAPGVDL 271
Cdd:COG1196 224 ELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 272 TRVLAEMREQYEAmaeknrrdveawffsKTEELNKEVASNTEMIQTSKTEITDLRRTMQELEIELQSQLSMKAGLENSLA 351
Cdd:COG1196 304 IARLEERRRELEE---------------RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519473574 352 ETEcryATQLQQIQGLIGGLEAQLSELRcEMEAQNQEYKMLLDIKTRLEQEIATYRSLLEGQDAKMAGIAIREA 425
Cdd:COG1196 369 EAE---AELAEAEEELEELAEELLEALR-AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
160-425 |
1.27e-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: 44.66 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 160 IEELRDKIMATTIDNSRVILEIDNARLAADDFRLKYENELALRQGVEADINGLRRVLDELTLARTDLEMQIEGLNEELAY 239
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 240 LKKnHEEEMKEFSSQLAGQVNVEMDAApgVDLTRVLAEMREQYEamaeknrrdveawffskteELNKEVASNTEMIQTSK 319
Cdd:TIGR02168 773 AEE-ELAEAEAEIEELEAQIEQLKEEL--KALREALDELRAELT-------------------LLNEEAANLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 320 TEITDLRRTMQELE---IELQSQLSMKAGLENSLAETECRYATQLQQIQGLIGGLEAQLSELRCEMEAQNQEYKMLLDIK 396
Cdd:TIGR02168 831 RRIAATERRLEDLEeqiEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
250 260
....*....|....*....|....*....
gi 1519473574 397 TRLEQEIATYRSLLEGQDAKMAGIAIREA 425
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEGLEVRID 939
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
148-425 |
1.43e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 148 SPECDYSQYFKTIEELRDKIMATTIDNSRVIlEI----DNARLAAddfrlKYENELA---LRQGVEADINGLRRVLDELT 220
Cdd:COG3206 108 DPLGEEASREAAIERLRKNLTVEPVKGSNVI-EIsytsPDPELAA-----AVANALAeayLEQNLELRREEARKALEFLE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 221 LARTDLEMQIEGLNEELAYLKKNH-----EEEMKEFSSQLAgQVNVEMdaapgVDLTRVLAEMREQYEAMAEKNRRDVEA 295
Cdd:COG3206 182 EQLPELRKELEEAEAALEEFRQKNglvdlSEEAKLLLQQLS-ELESQL-----AEARAELAEAEARLAALRAQLGSGPDA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 296 wffskteelnKEVASNTEMIQTSKTEITDLRRTMQELE----------IELQSQL-SMKAGLENSLAETECRYATQLQQI 364
Cdd:COG3206 256 ----------LPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIaALRAQLQQEAQRILASLEAELEAL 325
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519473574 365 QGLIGGLEAQLSELRCEMEAQNQEYKMLLdiktRLEQEIATYRSLLEGQDAKMAGIAIREA 425
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAELR----RLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
158-404 |
4.00e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 158 KTIEELRDKIMATTidnsrviLEIDNARLAADDFRLKYENELALRQGVEADINGLRRVLDELTLARTDLEMQIEGLNEEL 237
Cdd:COG1196 267 AELEELRLELEELE-------LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 238 AYLKKNHEEEMKEFSSQLAGQVNVEmdaapgVDLTRVLAEMREQYEAMAEKNRRDVEAwfFSKTEELNKEVASNTEMIQT 317
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAE------EALLEAEAELAEAEEELEELAEELLEA--LRAAAELAAQLEELEEAEEA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 318 SKTEITDLRRTMQELEIELQSQLSMKAGLENSLAETECRYATQLQQIQGLIGGLEAQLSELRCEMEAQNQEYKMLLDIKT 397
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
....*..
gi 1519473574 398 RLEQEIA 404
Cdd:COG1196 492 RLLLLLE 498
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
105-419 |
6.19e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 105 EKITMQN----LNDRLASYLDKVRALEEANADL-------EVKIHDWYQKQTP------TSPECD-----YSQYFKTIEE 162
Cdd:pfam15921 487 KKMTLESsertVSDLTASLQEKERAIEATNAEItklrsrvDLKLQELQHLKNEgdhlrnVQTECEalklqMAEKDKVIEI 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 163 LRDKIM--------------ATTIDNSRVILEIDNARLAADDFRLkyenelaLRQGVEADINGLRRVLDELTLARTDLem 228
Cdd:pfam15921 567 LRQQIEnmtqlvgqhgrtagAMQVEKAQLEKEINDRRLELQEFKI-------LKDKKDAKIRELEARVSDLELEKVKL-- 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 229 qIEGLNEELAYLKknheeEMKEFSSQLAGQVNVEMDAapgvdltrvLAEMREQYEAMAEKnrrdveawFFSKTEELNKEV 308
Cdd:pfam15921 638 -VNAGSERLRAVK-----DIKQERDQLLNEVKTSRNE---------LNSLSEDYEVLKRN--------FRNKSEEMETTT 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 309 ASNTEMIQTSKTEITDLRRTMQELEIELQSQLSMKAGLENslaetecryatQLQQIQGLIGGLEAQLSELRCEMEAQNQE 388
Cdd:pfam15921 695 NKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQK-----------QITAKRGQIDALQSKIQFLEEAMTNANKE 763
|
330 340 350
....*....|....*....|....*....|.
gi 1519473574 389 YKMLLDIKTRLEQEIATYRSllegQDAKMAG 419
Cdd:pfam15921 764 KHFLKEEKNKLSQELSTVAT----EKNKMAG 790
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
206-419 |
1.81e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 206 EADINGLRRVLDELTLARTDLEMQIEGLNEELAYLKknheEEMKEFSSQLAgQVNVEMDAApGVDLTRVLAEMREQYEAM 285
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELN----EEYNELQAELE-ALQAEIDKL-QAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 286 AE------KNRRDVEAW-----------FFSKTEELNKEVASNTEMIQTSKTEITDLRRTMQELEIELQSQLSMKAGLEN 348
Cdd:COG3883 89 GEraralyRSGGSVSYLdvllgsesfsdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519473574 349 SLAETEcryaTQLQQIQGLIGGLEAQLSELRCEMEAQNQEYKMLLDIKTRLEQEIATYRSLLEGQDAKMAG 419
Cdd:COG3883 169 AKAELE----AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
299-415 |
2.88e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 299 SKTEELNKEVASNTEMIQTSKTEITDLRRTMQELEIELQSQLSMKAgLENSLAETEcryaTQLQQIQGLIGGLEAQLSEL 378
Cdd:PRK11281 80 EETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSLRQ-LESRLAQTL----DQLQNAQNDLAEYNSQLVSL 154
|
90 100 110
....*....|....*....|....*....|....*...
gi 1519473574 379 RCEME-AQNQEYKMLldikTRLeQEIatyRSLLEGQDA 415
Cdd:PRK11281 155 QTQPErAQAALYANS----QRL-QQI---RNLLKGGKV 184
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
160-411 |
5.68e-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: 39.27 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 160 IEELRDKIMATTIDNSRVILEIDNARLAADDFRLKYENELALRQGVEADINGLRRVLDELTLARTDLEMQIEGLNEELAY 239
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 240 LKKNHEEemkefssqlagqvnvemdaapgvdltrvLAEMREQYEAMAEKNRRDVEAWFfSKTEELNKEVASNTEMIQTSK 319
Cdd:TIGR02168 314 LERQLEE----------------------------LEAQLEELESKLDELAEELAELE-EKLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 320 TEITDLRRTMQELEIELQSQLSMKAGLENSLAETE---CRYATQLQQIQGLIGGLEAQLSELRCEM-EAQNQEYKMLLDi 395
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNneiERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELE- 443
|
250
....*....|....*.
gi 1519473574 396 ktRLEQEIATYRSLLE 411
Cdd:TIGR02168 444 --ELEEELEELQEELE 457
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
177-405 |
6.98e-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: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 177 VILEIDNARLAADDFRL-KYENELALRQGVeadINGLRRVLDELTLARTDLEMQIEGLNEELAYLKKNHEEEMKEFSS-- 253
Cdd:TIGR02169 625 VVEDIEAARRLMGKYRMvTLEGELFEKSGA---MTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRie 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 254 QLAGQVNVEMDaapgvDLTRVLAEMREQYEAMAEKNRRDVEawffskteelnkEVASNTEMIQTSKTEITDLRRTMQELE 333
Cdd:TIGR02169 702 NRLDELSQELS-----DASRKIGEIEKEIEQLEQEEEKLKE------------RLEELEEDLSSLEQEIENVKSELKELE 764
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519473574 334 IELQSQLSMKAGLENSLAETECRYA-TQLQQIQGLIGGLEAQLSELRCEMEAQNQEYKMLLDIKTRLEQEIAT 405
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARLShSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
200-411 |
7.65e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 38.72 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 200 ALRQGVEADINGLRRVLDELTLARTDLEMQIEGLNEELAYLKKNHEEEMKEFSsqlagqvnvemdaapgvDLTRVLAEMR 279
Cdd:pfam07888 52 AANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYK-----------------ELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 280 EQYEAMAEKNRRDVeawffSKTEELNKEVASNTEMIQTSKTEITDLRRTMQELEIELQSQLSMKAGLENSLAETE---CR 356
Cdd:pfam07888 115 EEKDALLAQRAAHE-----ARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEeelRS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1519473574 357 YATQLQQIQGLIGGLEAQLSELRCEMEAQNQEYKMLLDIKTRLEQEIATYRSLLE 411
Cdd:pfam07888 190 LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQE 244
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
104-333 |
8.22e-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: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 104 NEKITMQNLNDRLASYLDKVRALEEANADLEVKIHDwyqkqtptspecdysQYFKTIEELRDKIMATTIDNSRVILEIDn 183
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSH---------------SRIPEIQAELSKLEEEVSRIEARLREIE- 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 184 ARLAADDFRLKYEnelalrqgvEADINGLRRVLDELTLARTDLEMQIEGLNEELAYLK---KNHEEEMKEFSSQLAgqvn 260
Cdd:TIGR02169 819 QKLNRLTLEKEYL---------EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEeelEELEAALRDLESRLG---- 885
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519473574 261 vemdaapgvDLTRVLAEMREQYEAMaEKNRRDVEAwffsKTEELNKEVASNTEMIQTSKTEITDLRRTMQELE 333
Cdd:TIGR02169 886 ---------DLKKERDELEAQLREL-ERKIEELEA----QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
203-385 |
9.61e-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: 37.60 E-value: 9.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 203 QGVEADINGLRRVLDELTLARTDLEMQIEGLNEELAYLKKNHEE---EMKEFSSQLAgqvnvemdaapgvDLTRVLAEMR 279
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDlekEIKRLELEIE-------------EVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519473574 280 EQyeAMAEKNRRDVEAwffskteeLNKEVASNTEMIQTSKTEITDLRRTMQELEIELQSQLSMKAGLENSLAETECRYAT 359
Cdd:COG1579 80 EQ--LGNVRNNKEYEA--------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
170 180
....*....|....*....|....*.
gi 1519473574 360 QLQQIQGLIGGLEAQLSELRCEMEAQ 385
Cdd:COG1579 150 ELAELEAELEELEAEREELAAKIPPE 175
|
|
| |
