|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
68-376 |
2.58e-127 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 370.40 E-value: 2.58e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 68 SERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAK---EPTKLADVYQAELRELRLRLDQLTANSARLEVERDNL 144
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkgaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 145 AQDLATVRQKLQDETNLRLEAENNLAAYRQEADEATLARLDLERKIESLEEEIRFLRKIHEEEVRELQEQLARQQVHVEL 224
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 225 DVA-KPDLTAALKEIRTQYEAMASSNMHEAEEWYRSKFADLTDAAARNAELLRQAKHEANDYRRQLQSLTCDLESLRGTN 303
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 121135 304 ESLERQMREQEERHVREAASYQEALARLEEEGQSLKDEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEENR 376
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
85-375 |
4.32e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 4.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 85 EKVRFLEQQNKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERDNLAQDLATVRQKLQDETNLRLE 164
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 165 AENNLAAYRQEADEATLARLDLERKIESLEEEIRFLRKIHEEEVRELQEQLARQQVHVELDVAKPDLTAALKEIRTQYEA 244
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 245 MASSNMHEAEEWYRSKFADLTDAAARNAELLRQAKHEANDYRRQLQsltcdLESLRGTNESLERQMREQEERHVREAASY 324
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER-----LEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 121135 325 QEALARLEEEGQSLKDEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEEN 375
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
90-377 |
5.50e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 5.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 90 LEQQnKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERDNLAQDLATVRQKLQDETNLRLEAENNL 169
Cdd:COG1196 205 LERQ-AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 170 AAYRQEADEATLARLDLERKIESLEEEIRFLRKIHEEEVRELQEQLARQQvhvELDVAKPDLTAALKEIRTQYEAMASSN 249
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE---ELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 250 MHEAEEwyrskfadLTDAAARNAELLRQAKHEANDYRRQLQSLTcDLESLRGTNESLERQMREQEERHVREAASYQEALA 329
Cdd:COG1196 361 AEAEEA--------LLEAEAELAEAEEELEELAEELLEALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 121135 330 RLEEEGQSLKDEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEENRI 377
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
85-378 |
4.93e-10 |
|
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: 61.61 E-value: 4.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 85 EKVRFLEQQNKALAAELNQLRakeptKLADVYQAELRELRLRLDQLTANSARLEVERDNLAQDLATVRQKLQDETNLRLE 164
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELR-----KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 165 AENNLAAYRQEADEATLARLDLERKIESLEEEIRFLR---KIHEEEVRELQEQLARQQVHV------------ELDVAKP 229
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKeelKALREALDELRAELTLLNEEAanlrerleslerRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 230 DLTAALKEIRTQYEAMASSNmHEAEEwYRSKFADLTDAAARNAELLRQAKHEANDYRRQLQSLTCDLESLRGTNESLERQ 309
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLA-AEIEE-LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 121135 310 MREQEERHvreaASYQEALARLEEEGQSLKDEMArhlQEYQDLLNVKLALDIEIATYRKLLEGEENRIT 378
Cdd:TIGR02168 917 LEELREKL----AQLELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
63-362 |
6.69e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 6.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 63 KETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKLADVYQA---------ELRELRLRLDQLTAN 133
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELlaelarleqDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 134 SARLEVERDNLAQDLATVRQKLQDETNLRLEAENNLAAYRQEADEATLARLDLERKIESLEEEIRFLRKIHEEEVRELQE 213
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 214 QLARQQvhveldvakpDLTAALKEIRTQYEAMASSNMHEAEEwyrskFADLTDAAARNAELLRQAKHEANDYRRQLQSLT 293
Cdd:COG1196 398 LAAQLE----------ELEEAEEALLERLERLEEELEELEEA-----LAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 121135 294 CDLESLRGTNESLERQMREQEERHVREAASYQEALARLEEEGQSLKDEMARHLQEYQDLLNVKLALDIE 362
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIG 531
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
86-375 |
1.27e-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: 60.46 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 86 KVRFLEQQNKAlAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERDNLAQDLATVRQKLQDETNLRLEA 165
Cdd:TIGR02168 201 QLKSLERQAEK-AERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 166 ENNLAAYRQEADEATLARLDLERKIESLEEEIRFLRKiHEEEVRELQEQLARQQVHVELDVAkpDLTAALKEIRTQYEAM 245
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLER-QLEELEAQLEELESKLDELAEELA--ELEEKLEELKEELESL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 246 ASSN------MHEAEEWYRSKFADLTDAAARNAELLRQAKHEAND---YRRQLQSLTCDLESLRGTNESLERQMREQE-- 314
Cdd:TIGR02168 357 EAELeeleaeLEELESRLEELEEQLETLRSKVAQLELQIASLNNEierLEARLERLEDRRERLQQEIEELLKKLEEAElk 436
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 121135 315 ------ERHVREAASYQEALARLEEEGQSLKDEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEEN 375
Cdd:TIGR02168 437 elqaelEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
68-314 |
1.63e-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: 60.07 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 68 SERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAK--EPTKLADVYQAEL--------------RELRLRLDQLT 131
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEvsELEEEIEELQKELyalaneisrleqqkQILRERLANLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 132 ANSARLEVERDNLAQDLATVRQKLQDETNLRLEAENNLAAYRQEADEATLARLDLERKIESLEEEIRFLRKiheeEVREL 211
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS----KVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 212 QEQLARQQVHVE-LDVAKPDLTAALK----EIRTQYEAMASSNMHEAEEWYRSKFADLTDAAARNAEL---LRQAKHEAN 283
Cdd:TIGR02168 392 ELQIASLNNEIErLEARLERLEDRRErlqqEIEELLKKLEEAELKELQAELEELEEELEELQEELERLeeaLEELREELE 471
|
250 260 270
....*....|....*....|....*....|.
gi 121135 284 DYRRQLQSLTCDLESLRGTNESLERQMREQE 314
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
117-348 |
1.57e-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: 56.31 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 117 QAELRELRLRLDQLTANSARLEVERDNLAQDLATVRQKLQDETNLRLEAENNLAAyrqeadeatlarldLERKIESLEEE 196
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA--------------LEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 197 IRFLRKIHEEEVRELQEQLARQQVHVELDvakpdltaALKEIRTQYEAMASSNMHEAEEWYRSKFADLTDAAARNAELLR 276
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQP--------PLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 121135 277 QAKHEANDYRRQLQSLTCDLESLRGTNESLERQMREQEERHVREAASYQEALARLEEEGQSLKDEMARHLQE 348
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| Filament_head |
pfam04732 |
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ... |
4-66 |
4.27e-08 |
|
Intermediate filament head (DNA binding) region; This family represents the N-terminal head region of intermediate filaments. Intermediate filament heads bind DNA. Vimentin heads are able to alter nuclear architecture and chromatin distribution, and the liberation of heads by HIV-1 protease liberates may play an important role in HIV-1 associated cytopathogenesis and carcinogenesis. Phosphorylation of the head region can affect filament stability. The head has been shown to interaction with the rod domain of the same protein.
Pssm-ID: 461414 [Multi-domain] Cd Length: 83 Bit Score: 50.08 E-value: 4.27e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 121135 4 RRI---TSAARRSY-VSSGEMMV--------GGLAPGRRLGPGTRLSLARMPPPLPT-RVDFSLAGALNAGFKETR 66
Cdd:pfam04732 7 RRMfgdSSSSRPSYsSSSGSRSVssrsysrsSSSSPSSSSRRSSRSSSRSSYPSLAAdSLDFSLADALNQEFKATR 82
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
54-273 |
9.65e-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: 53.61 E-value: 9.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 54 LAGALNAGFKETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAK--EPTKLADVYQAELRELRLRLDQLT 131
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiaALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 132 ANSARLEVERDNLAQDLATV-----RQKLQDETNLRLEAENNLAAYRQEA--DEATLARLDLERKIESLEEEIRFLRKIH 204
Cdd:COG4942 90 KEIAELRAELEAQKEELAELlralyRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 121135 205 EEEVRELQEQLARQQV-HVELDVAKPDLTAALKEIRTQYEAMAS--SNMHEAEEWYRSKFADLTDAAARNAE 273
Cdd:COG4942 170 EAERAELEALLAELEEeRAALEALKAERQKLLARLEKELAELAAelAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
63-344 |
2.86e-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: 49.68 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 63 KETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLtansarlEVERD 142
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREI-------EQKLN 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 143 NLAQDLATVRQKLQDETNLRLEAENNLAAYRQEADEatlarldLERKIESLEEEIrflrKIHEEEVRELQEQLArqqvhv 222
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN-------LNGKKEELEEEL----EELEAALRDLESRLG------ 885
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 223 eldvakpDLTAALKEIRTQYEAMaSSNMHEAEEWYRSKFADLTDAAARNAELLRQAKHEANDYRRQLQSLTC--DLESLR 300
Cdd:TIGR02169 886 -------DLKKERDELEAQLREL-ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEelSLEDVQ 957
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 121135 301 GTNESLERQMR----------EQEERHVREAASYQEALARLEEEGQSLKDEMAR 344
Cdd:TIGR02169 958 AELQRVEEEIRalepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
114-354 |
8.72e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 8.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 114 DVYQAELRELRLRLDQLTANSARLEVERDNLaQDLATVRQKLQDETnlrlEAENNLAAYRQEADEATLARLDLER---KI 190
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDAL-QERREALQRLAEYS----WDEIDVASAEREIAELEAELERLDAssdDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 191 ESLEEEIRFLRKIHEEEVRELQEQLARQQvhvELDVAKPDLTAALKEIRTQYEAMASsnmheaeewyRSKFADLTDAAAR 270
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIG---RLEKELEQAEEELDELQDRLEAAED----------LARLELRALLEER 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 271 NAELLRQAKheANDYRRQLQSltcDLESLRGTNESLERQMREQEERHVRE--------------AASYQEALARLEEEGq 336
Cdd:COG4913 755 FAAALGDAV--ERELRENLEE---RIDALRARLNRAEEELERAMRAFNREwpaetadldadlesLPEYLALLDRLEEDG- 828
|
250
....*....|....*...
gi 121135 337 slkdeMARHLQEYQDLLN 354
Cdd:COG4913 829 -----LPEYEERFKELLN 841
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
62-259 |
1.13e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 62 FKETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQL--RAKEPTKLADVYQAELRELRLRLDQLTANSARLEV 139
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLeeQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 140 ERDNLAQDLATVRQKLQDETNLRLEAENNLAAYRQEADEATLARLDLERKIESLEEEIRFLRKIHEEEVRELQEQLARQQ 219
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALE 960
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 121135 220 VHVELDVAKpdLTAALKEIRTQYEAMASSNMhEAEEWYRS 259
Cdd:TIGR02168 961 NKIEDDEEE--ARRRLKRLENKIKELGPVNL-AAIEEYEE 997
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
70-308 |
1.41e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 70 RAEMMELNDRFASY--IEKVRFLEQQNKALAAELNQLRAKeptkLADVYQA--ELRELRLRLDQLTANSARLEVERDNLA 145
Cdd:COG4913 637 EAELDALQERREALqrLAEYSWDEIDVASAEREIAELEAE----LERLDASsdDLAALEEQLEELEAELEELEEELDELK 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 146 QDLATVRQKLQDETNLRLEAENNLAAYRQEADEATLARLDLERKIESLEEEIRFLRKIHEEEVRELQEQLARQQVHVEL- 224
Cdd:COG4913 713 GEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERa 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 225 --------DVAKPDLTAALKEIRtQYEAM----ASSNMHEAEEwyrsKFADLTDAAARN--AELLRQAKHEANDYRRQLQ 290
Cdd:COG4913 793 mrafnrewPAETADLDADLESLP-EYLALldrlEEDGLPEYEE----RFKELLNENSIEfvADLLSKLRRAIREIKERID 867
|
250
....*....|....*...
gi 121135 291 SLtcdleslrgtNESLER 308
Cdd:COG4913 868 PL----------NDSLKR 875
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
63-333 |
2.69e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 63 KETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRaKEPTKLadvyQAELRELRLRLDQLTANSARLEVERD 142
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS-KELTEL----EAEIEELEERLEEAEEELAEAEAEIE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 143 NLAQDLATVRQKLQDETNLRLEAENNLAAYRQEADEATLARLDLERKIESLEEEIRFLRKIHE---EEVRELQEQLARQQ 219
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEelsEDIESLAAEIEELE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 220 V--------HVELDVAKPDLTAALKEIRTQYEAM------ASSNMHEAEEWYRSKFADLTDAAARNAELLRQAKH----- 280
Cdd:TIGR02168 866 ElieeleseLEALLNERASLEEALALLRSELEELseelreLESKRSELRRELEELREKLAQLELRLEGLEVRIDNlqerl 945
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 121135 281 --------------------EANDYRRQLQSLTCDLESLRGTNESLERQMREQEERHV---REAASYQEALARLEE 333
Cdd:TIGR02168 946 seeysltleeaealenkiedDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDfltAQKEDLTEAKETLEE 1021
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
71-247 |
3.08e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 71 AEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERDNL------ 144
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELeaqirg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 145 --AQDLATVRQKLQDETNLRLEAENNLAAYRQEADEATLARLDLERKIESLEEEIRFLRKIHEEEVRELQEQLArqqvhv 222
Cdd:COG4913 335 ngGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA------ 408
|
170 180
....*....|....*....|....*
gi 121135 223 ELDVAKPDLTAALKEIRTQYEAMAS 247
Cdd:COG4913 409 EAEAALRDLRRELRELEAEIASLER 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
118-334 |
3.82e-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: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 118 AELRELRLRLDQLTAnsarlEVERDNLAQDLATVRQKLQDETNLRLEAENNLAAYRQEADEATLARLDLE-RKIESLEEE 196
Cdd:COG4913 272 AELEYLRAALRLWFA-----QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLERE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 197 IRFLrkihEEEVRELQEQLARQQVHVE-LDVAKPDLTAALKEIRTQYEAMAssnmheaeewyrskfADLTDAAARNAELL 275
Cdd:COG4913 347 IERL----ERELEERERRRARLEALLAaLGLPLPASAEEFAALRAEAAALL---------------EALEEELEALEEAL 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 121135 276 RQAKHEANDYRRQLQSLTCDLESLRGtneslerqmreqeeRHVREAASYQEALARLEEE 334
Cdd:COG4913 408 AEAEAALRDLRRELRELEAEIASLER--------------RKSNIPARLLALRDALAEA 452
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
117-344 |
5.63e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 117 QAELRELRLRLDQLTANSARLEVERDNLAQDLATVRQKLQDETNLRLEAENNLAAYRQEADEATLARLDLERKIESLEEE 196
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDR 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 197 IRFLR---KIHEEEVRELQEQLAR-----QQVHVELDVAKPDLTAALKEIRTQYEAMASsnMHEAEEWYRSKFADLTDAA 268
Cdd:PRK02224 330 LEECRvaaQAHNEEAESLREDADDleeraEELREEAAELESELEEAREAVEDRREEIEE--LEEEIEELRERFGDAPVDL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 269 ARNAELLRQAKHEANDYRRQLQSLTCDLESLRGTNESLERQMRE----------QEERHVREAASYQEALARLEEEGQSL 338
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEDRERVEELEAELEDL 487
|
....*.
gi 121135 339 KDEMAR 344
Cdd:PRK02224 488 EEEVEE 493
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
116-371 |
8.91e-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: 8.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 116 YQAELRELRLRLDQLTANSARLEVERDNLAQDLATVRQKLQDETNLRLEAENNLAAYRQEADEATLARLDLERKIESLEE 195
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 196 EIrflrkihEEEVRELQEQLARqqvhveldvaKPDLTAALKEIRTQYEAMASSNMHEAEEWYRSKFADLTDAAARNAELL 275
Cdd:TIGR02169 752 EI-------ENVKSELKELEAR----------IEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 276 RQAKheandyrRQLQSLTCDLESLRGTNESLERQMREQEERHV-----------------REAASYQEALARLEEEGQSL 338
Cdd:TIGR02169 815 REIE-------QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKsiekeienlngkkeeleEELEELEAALRDLESRLGDL 887
|
250 260 270
....*....|....*....|....*....|...
gi 121135 339 KDEMARHLQEYQDLLNVKLALDIEIATYRKLLE 371
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
63-374 |
1.24e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 63 KETRASE-RAEMMELNDRFAsyieKVRFLEQQNKALAAELNQLRAkepTKLADVYQ----AELRELRLRLDQLTANSARL 137
Cdd:COG3096 783 REKRLEElRAERDELAEQYA----KASFDVQKLQRLHQAFSQFVG---GHLAVAFApdpeAELAALRQRRSELERELAQH 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 138 EVERDNLAQDLATVRQKLQDETnlRLEAENNLAAyrqeaDEATLARLD-LERKIESLEEEIRFLRKiHEEEVRELQEQLA 216
Cdd:COG3096 856 RAQEQQLRQQLDQLKEQLQLLN--KLLPQANLLA-----DETLADRLEeLREELDAAQEAQAFIQQ-HGKALAQLEPLVA 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 217 RQQV----HVELDVAKPDLTAALKEIRTQYEAM--------------------ASSNMHEAeewYRSKFADLTDAAARNA 272
Cdd:COG3096 928 VLQSdpeqFEQLQADYLQAKEQQRRLKQQIFALsevvqrrphfsyedavgllgENSDLNEK---LRARLEQAEEARREAR 1004
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 273 ELLRQAKHEANDYRRQLQSLTcdlESLRGTNESLERQMREQEERHVREAAsyqEALARLEEEGQSLKDEMARHLQEYQDL 352
Cdd:COG3096 1005 EQLRQAQAQYSQYNQVLASLK---SSRDAKQQTLQELEQELEELGVQADA---EAEERARIRRDELHEELSQNRSRRSQL 1078
|
330 340
....*....|....*....|..
gi 121135 353 LNVKLALDIEIATYRKLLEGEE 374
Cdd:COG3096 1079 EKQLTRCEAEMDSLQKRLRKAE 1100
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
134-247 |
3.65e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 134 SARLEVERDNLAQDLATVRQKLQdetnlRLEAEnnLAAYRQEADEATLARLD-LERKIESLEEEIRFLRKIHEEEVRELQ 212
Cdd:COG0542 399 AARVRMEIDSKPEELDELERRLE-----QLEIE--KEALKKEQDEASFERLAeLRDELAELEEELEALKARWEAEKELIE 471
|
90 100 110
....*....|....*....|....*....|....*
gi 121135 213 EQLARQQVHVELDVAKPDLTAALKEIRTQYEAMAS 247
Cdd:COG0542 472 EIQELKEELEQRYGKIPELEKELAELEEELAELAP 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
164-394 |
5.37e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 164 EAENNLAAYRQEADEATLARLDLERKIESLEEE----IRFLRKIHEEEVRELQEQLAR-QQVHVELDVAKPDLTAALKEI 238
Cdd:COG1196 176 EAERKLEATEENLERLEDILGELERQLEPLERQaekaERYRELKEELKELEAELLLLKlRELEAELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 239 RTQYEAMASSNMHEAEEwyRSKFADLTDAAARNAELLRQAKHEANDYRRQLQSLTCDLESLRGTNESLERQMREQEERHV 318
Cdd:COG1196 256 EELEAELAELEAELEEL--RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 121135 319 R---EAASYQEALARLEEEGQSLKDEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEENRITIPVQTFSNLQIRETSL 394
Cdd:COG1196 334 EleeELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
97-226 |
6.59e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 97 LAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERDNLAQDLATvrqklQDETNLRLEAEnnLAAYRQEA 176
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEE-----KDERIERLERE--LSEARSEE 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 121135 177 DEatlaRLDLERKIESLEEEIRFLRKIHEEE---VRELQEQLARQQVHVELDV 226
Cdd:COG2433 458 RR----EIRKDREISRLDREIERLERELEEErerIEELKRKLERLKELWKLEH 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
70-260 |
7.17e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 70 RAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAkeptkLADVYQAELRELRLRLDQLTANSARLEVERDNLAQDLA 149
Cdd:TIGR02169 293 KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA-----EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 150 TVRQKLQDETNLRLEAENNLAAYRQEADeatlarlDLERKIESLEEEIRFL---RKIHEEEVRELQEQLAR-QQVHVELD 225
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDELKDYREKLE-------KLKREINELKRELDRLqeeLQRLSEELADLNAAIAGiEAKINELE 440
|
170 180 190
....*....|....*....|....*....|....*
gi 121135 226 VAKPDLTAALKEIRTQYEAMASSNMHEAEEWYRSK 260
Cdd:TIGR02169 441 EEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK 475
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
118-339 |
1.55e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 118 AELRELRLRLDQLTANSARLEVERDNLAQdLATVRQKLQDETNLRLEAEnnlaayRQEADEATLARLDLERKIESLEEEI 197
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIEL-LEPIRELAERYAAARERLA------ELEYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 198 RFLRkiheEEVRELQEQLARQQVHVEldvakpDLTAALKEIRTQYEAMASSNMHEAE---EWYRSKFADLTDAAARNAEL 274
Cdd:COG4913 298 EELR----AELARLEAELERLEARLD------ALREELDELEAQIRGNGGDRLEQLEreiERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 121135 275 LRQAKHEANDYRRQLQSLTCDLESLRGTNESLERQMREQEERHVREAASYQEALARLEEEGQSLK 339
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
67-307 |
1.95e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 67 ASERAemmeLNDRFASYIEKVRFLEQQNkalaAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEV-ERDNLA 145
Cdd:pfam15921 493 SSERT----VSDLTASLQEKERAIEATN----AEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMaEKDKVI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 146 QDLatvRQKLQDETnlRLEAENNLAAYRQEADEATLARLDLERKIESleEEIRFLRKIHEEEVRELQEQLARQQVH-VEL 224
Cdd:pfam15921 565 EIL---RQQIENMT--QLVGQHGRTAGAMQVEKAQLEKEINDRRLEL--QEFKILKDKKDAKIRELEARVSDLELEkVKL 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 225 DVAKPDLTAALKEIRTQYEAMassnMHEAEEwYRSKFADLTDAAARNAELLRQAKHE----ANDYRRQLQSLTCDLESLR 300
Cdd:pfam15921 638 VNAGSERLRAVKDIKQERDQL----LNEVKT-SRNELNSLSEDYEVLKRNFRNKSEEmettTNKLKMQLKSAQSELEQTR 712
|
....*..
gi 121135 301 GTNESLE 307
Cdd:pfam15921 713 NTLKSME 719
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
64-241 |
3.35e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.12 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 64 ETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKLADVYQ--AELRELRLRLDQLTANSARLEVER 141
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKElrEEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 142 DNLAQDLATVRQKlqdetnlrleaennLAAYRQEADEATLARLD---LERKIESLEEEI--RFLRKIHE----EEVRELQ 212
Cdd:COG1340 81 DELNEKLNELREE--------------LDELRKELAELNKAGGSidkLRKEIERLEWRQqtEVLSPEEEkelvEKIKELE 146
|
170 180
....*....|....*....|....*....
gi 121135 213 EQLARQQVHVELDVAKPDLTAALKEIRTQ 241
Cdd:COG1340 147 KELEKAKKALEKNEKLKELRAELKELRKE 175
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
116-270 |
5.03e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 38.94 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 116 YQAELRELRLRLDQLTANSARLEVERDNLAQDLATVRQKLQDETNLRLEAENNLAAYRQEADEATLARLDLER-----KI 190
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARrrvlaPI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 191 -----ESLEEEIRfLRKIHEEEVRELQEQLARQQVHVELDVAkpDLTAALKEIRTQYEAMASsnmhEAEEWYRSKFADLT 265
Cdd:pfam00529 136 ggisrESLVTAGA-LVAQAQANLLATVAQLDQIYVQITQSAA--ENQAEVRSELSGAQLQIA----EAEAELKLAKLDLE 208
|
....*
gi 121135 266 DAAAR 270
Cdd:pfam00529 209 RTEIR 213
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
111-371 |
5.42e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.23 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 111 KLADVYQAELRELRLrlDQLTANSARLEVERDNLAQDLATVRQKLQDetnlrLEAENNLAAYRQEADEATLARLDLERKI 190
Cdd:COG3206 156 ALAEAYLEQNLELRR--EEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAKLLLQQLSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 191 ESLEEEIRFLrkihEEEVRELQEQLARQQVHVELDVAKP---DLTAALKEIRTQYEAMASSnmheaeewYRSKFADLTDA 267
Cdd:COG3206 229 AEARAELAEA----EARLAALRAQLGSGPDALPELLQSPviqQLRAQLAELEAELAELSAR--------YTPNHPDVIAL 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 268 AARNAELLRQAKHEAndyRRQLQSLTCDLESLRGTNESLERQMREQEERhVREAASYQEALARLEEEgqslkdemarhlq 347
Cdd:COG3206 297 RAQIAALRAQLQQEA---QRILASLEAELEALQAREASLQAQLAQLEAR-LAELPELEAELRRLERE------------- 359
|
250 260
....*....|....*....|....
gi 121135 348 eyqdllnvklaLDIEIATYRKLLE 371
Cdd:COG3206 360 -----------VEVARELYESLLQ 372
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
64-217 |
7.37e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 38.76 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 64 ETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERDN 143
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE 704
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 121135 144 LAQDLATVRQKLQDETNLRLEAENNLAAYRQEADEATLARLDLERKIESLEEEIRFLRKIHEEEVRELQEQLAR 217
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
85-282 |
7.84e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 38.52 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 85 EKVRFLEQQNKALAAELNQLRAKEPT------KLADVyQAELRELRLRLDQLTANSARLE----VERDNLAQDL-ATVRQ 153
Cdd:PRK11637 58 AKEKSVRQQQQQRASLLAQLKKQEEAisqasrKLRET-QNTLNQLNKQIDELNASIAKLEqqqaAQERLLAAQLdAAFRQ 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 154 K--------LQDETNLRLEAENNLAAYRQEADEATLArlDLERKIESLEEEIRFLRKIHEEEVRELQEQLARQQvhvELD 225
Cdd:PRK11637 137 GehtglqliLSGEESQRGERILAYFGYLNQARQETIA--ELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQ---KLE 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 121135 226 VAKPD-------LTAALKEIRTQYeamasSNMHEAEEWYRSKFADLTDAA-------ARNAELLRQAKHEA 282
Cdd:PRK11637 212 QARNErkktltgLESSLQKDQQQL-----SELRANESRLRDSIARAEREAkaraereAREAARVRDKQKQA 277
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-377 |
9.58e-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: 38.50 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 162 RLEAENNLAAYRQEADEATLARLDLERKIESLEEEIRFLRKIHE--EEVRELQEQLARQQVHvELDVAKPDLTAALKEIR 239
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKElkAELRELELALLVLRLE-ELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121135 240 TQYEAmASSNMHEAEEwyrsKFADLTDAAARNAELLRQAKHEANDYRRQLQSLTCDLESLRGTNESLERQMREQEERHVR 319
Cdd:TIGR02168 253 EELEE-LTAELQELEE----KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 121135 320 EAAS---YQEALARLEEEGQSLKDEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEENRI 377
Cdd:TIGR02168 328 LESKldeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
|
| |
