|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
76-385 |
2.54e-117 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 344.98 E-value: 2.54e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 76 NGKLAMQNLNDRLANYLEKVRSLEQSNSRLEAQIKQWYETNAPSTIRDYSSYYAQIKELQNQVKDAQVQNAQCVLRIDNA 155
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 156 KLAAEDFRLKFETERGMRIAVEADLQGLSKVYDNLTLQKTDLEIQIEELNKDLALLKKEHQEEVEVLRRQLG-NNVNVEV 234
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 235 DAAPGLNLGEIMNEMRQRYEVLAQKNLQEAKEQFERQSQTLQQQVTVNTEELKGFEVQVTELRRTYQNLEIELQSHLSMK 314
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21592285 315 ESLERNLEDVKARYASQLAAIQEMLSSLEAQLMQIRSDTERQNQEHNILLDIKTRLEQEIATYRRLLEGED 385
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEE 311
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
129-376 |
1.81e-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: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 129 AQIKELQNQVKDAQVQNAQCVLRIDNAKLAAEDFRLKFETERGMRIAVEADLQGLSKVYDNLTLQKTDLEIQIEELNKDL 208
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 209 A---LLKKEHQEEVEVLRRQLGN-NVNVEVDAAPGLNLGEIMNEMRQRYEVLAQK--NLQEAKEQFERQSQTLQQQVTVN 282
Cdd:TIGR02168 771 EeaeEELAEAEAEIEELEAQIEQlKEELKALREALDELRAELTLLNEEAANLRERleSLERRIAATERRLEDLEEQIEEL 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 283 TEELKGFEVQVTELRRTYQNLEIELQSHLSMKESLERNLEDVKARYASQLAAIQEMlsslEAQLMQIRSDTERQNQEHNI 362
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL----ESKRSELRRELEELREKLAQ 926
|
250
....*....|....
gi 21592285 363 LLDIKTRLEQEIAT 376
Cdd:TIGR02168 927 LELRLEGLEVRIDN 940
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-414 |
5.93e-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: 5.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 158 AAEDFRLKFETERGMRIAVEA-DLQGLSKVYDNLTLQKTDLEIQIEELNKDLALLkkehQEEVEVLRRQLgNNVNVEVDA 236
Cdd:TIGR02168 211 KAERYKELKAELRELELALLVlRLEELREELEELQEELKEAEEELEELTAELQEL----EEKLEELRLEV-SELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 237 APG--LNLGEIMNEMRQRYEVLAQK--NLQEAKEQFERQSQTLQQQVTVNTEELKGFEVQVTELRRTYQNLEIELQSHLS 312
Cdd:TIGR02168 286 LQKelYALANEISRLEQQKQILRERlaNLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 313 MKESLERNLEDVKA---RYASQLAAIQEMLSSLEAQLMQIRSDTERQNQEHNILLDIKTRLEQEIATYRRLLEGEDIKTT 389
Cdd:TIGR02168 366 ELEELESRLEELEEqleTLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445
|
250 260
....*....|....*....|....*
gi 21592285 390 EYQLSTLEMKDIKKTRKIKTVVEEV 414
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREEL 470
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
129-413 |
3.54e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 129 AQIKELQNQVKDA-----------QVQNAQCVLRIDNAKLAAEDFRLKFETERGMRIAVEADLQGLSKVYDNLTLQKTDL 197
Cdd:COG1196 200 RQLEPLERQAEKAeryrelkeelkELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 198 EIQIEELNKDLALLKKEHQEEVEVLRRQlgnnvnvevdaapglnlgeimNEMRQRYEVLAQKnLQEAKEQFERQSQTLQQ 277
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARL---------------------EERRRELEERLEE-LEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 278 QVTVNTEELKGFEVQVTELRRTYQNLEIELQSHLSMKESLERNLEDVKARYASQLAAIQEMLSSLEAQLMQIRSDTERQN 357
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 21592285 358 QEHNILLDIKTRLEQEIATYRRLLEGEDIKTTEYQLSTLEMKDIKKTRKIKTVVEE 413
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
123-382 |
3.98e-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: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 123 DYSSYYAQIKELQNQVKDAQVQNAQCVLRIDNAKLAAEDFRLKFEtergmriAVEADLQGLSKVYDNLTLQKTDLEIQIE 202
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS-------ELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 203 ELNKDLALLKKEhQEEVEVLRRQLGNNVNvevdaapglNLGEIMNEMRQRYEVLAQ---------KNLQEAKEQFERQSQ 273
Cdd:TIGR02168 306 ILRERLANLERQ-LEELEAQLEELESKLD---------ELAEELAELEEKLEELKEelesleaelEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 274 TLQQQVTVNTEELKGFEVQVTELRRTYQNLEIELQSHLSMKESLERNLEDV-KARYASQLAAIQEMLSSLEAQLMQIRSD 352
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELlKKLEEAELKELQAELEELEEELEELQEE 455
|
250 260 270
....*....|....*....|....*....|
gi 21592285 353 TERQNQEHNILLDIKTRLEQEIATYRRLLE 382
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELA 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
78-324 |
1.68e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 78 KLAMQNLNDRLANYLEKVRSLEQSNSRLEAQIKQwyetnapstirdyssYYAQIKELQNQVKDAQVQNAQCVLRIDNAKL 157
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQI---------------LRERLANLERQLEELEAQLEELESKLDELAE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 158 AAEDFRLKFETERGMRIAVEADLQGLSKVYDNLTLQKTDLEIQIEELNKDLALLKKE---HQEEVEVLRRQLgNNVNVEV 234
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiasLNNEIERLEARL-ERLEDRR 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 235 DaapglNLGEIMNEMRQRYEVLAQKNLQEAKEQFERQSQTLQQQVTVNTEELKGFEVQVTELRRTYQNLEIELQSHLSMK 314
Cdd:TIGR02168 417 E-----RLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
250
....*....|
gi 21592285 315 ESLERNLEDV 324
Cdd:TIGR02168 492 DSLERLQENL 501
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
189-372 |
5.13e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 189 NLTLQKTDLEIQIEELNKDLALLKKEhQEEVEVLRRQLGNNVNVEVDAAPGLNLGEIMNEMRQRYEVLAQKnLQEAKEQF 268
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAEARAE-LAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAE-LAELSARY 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 269 ERQS---QTLQQQVTVNTEELKgfevqvTELRRTYQNLEIELQSHLSMKESLERNLEDVKARYASqlaaiqemLSSLEAQ 345
Cdd:COG3206 287 TPNHpdvIALRAQIAALRAQLQ------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAE--------LPELEAE 352
|
170 180
....*....|....*....|....*..
gi 21592285 346 LMQIRSDTERQNQEHNILLdikTRLEQ 372
Cdd:COG3206 353 LRRLEREVEVARELYESLL---QRLEE 376
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
121-355 |
1.29e-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: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 121 IRDYSSYYAQIKELQNQVKDAQVQNAQCV----LRIDNAKLAAEDFRLKFETERGMRIAVEADLQGLSKVYDNLTLQKTD 196
Cdd:COG4913 234 FDDLERAHEALEDAREQIELLEPIRELAEryaaARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 197 LEIQIEELNKDLALLKKEHQE----EVEVLRRQLgNNVNVEVDAApglnlgeimNEMRQRYEVLAQK---NLQEAKEQFE 269
Cdd:COG4913 314 LEARLDALREELDELEAQIRGnggdRLEQLEREI-ERLERELEER---------ERRRARLEALLAAlglPLPASAEEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 270 RQSQTLQQQVTVNTEELKGFEVQVTELRRTYQNLEIELQSHLSMKESLERNLEDVKARYASQLAAIQEMLSSLEAQ---- 345
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAElpfv 463
|
250
....*....|..
gi 21592285 346 --LMQIRSDTER 355
Cdd:COG4913 464 geLIEVRPEEER 475
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
179-418 |
2.54e-05 |
|
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: 46.55 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 179 DLQGLSKVYDNLTLQKTDLEIQIEELNKDLALLKKEHQEEVEVLRrQLGNNVNvevdaapglnlgeIMNEMRQRYEVLAQ 258
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK-NLESQIN-------------DLESKIQNQEKLNQ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 259 ------KNLQEAKEQFERQSQTLQQQVTVNTEELKGFEVQVTELRRTYQNLEielqshlSMKESLERNLEDVKARYasql 332
Cdd:TIGR04523 409 qkdeqiKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD-------NTRESLETQLKVLSRSI---- 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 333 aaiqemlSSLEAQLMQIRSDTERQNQEHNILLDIKTRLEQEIATYRR----LLEGED-----IKTTEYQLSTLEMKDIK- 402
Cdd:TIGR04523 478 -------NKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKkissLKEKIEkleseKKEKESKISDLEDELNKd 550
|
250
....*....|....*.
gi 21592285 403 KTRKIKTVVEEVVDGK 418
Cdd:TIGR04523 551 DFELKKENLEKEIDEK 566
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
201-431 |
5.96e-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: 42.36 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 201 IEELNKDLALLKKEHQEevevlRRQLGNNVNVEVDAAPGlNLGEIMNEMRQRYEVLAQknLQEAKEQFERQSQTLQQQVT 280
Cdd:TIGR02169 683 LEGLKRELSSLQSELRR-----IENRLDELSQELSDASR-KIGEIEKEIEQLEQEEEK--LKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 281 VNTEELKGFEVQVTELRRTYQNLEIEL--------QSHLSMKESLERNLEDVKARYASQLAAIQEMLSSLEAQLMQIRSD 352
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALndlearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 353 TERQNQEHNILLDIKTRLEQEIATYRRLLEG--EDIKTTEYQLSTLEMKDIKKTRKIKTVVEEvvdGKVVSSEVKEIEES 430
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEEleEELEELEAALRDLESRLGDLKKERDELEAQ---LRELERKIEELEAQ 911
|
.
gi 21592285 431 V 431
Cdd:TIGR02169 912 I 912
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
129-388 |
6.89e-04 |
|
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: 41.67 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 129 AQIKELQNQVKDAQVQnaqcvlrIDNAKLAAEDFRLKFETERGMRIAVEADLQGLSKVYDNLTLQKTDLEIQIEELNKDL 208
Cdd:COG4942 20 DAAAEAEAELEQLQQE-------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 209 ALLKKEHQEEVEVLRRQLGNNvnvevdaapglnlgeimnEMRQRYEVLAQKNLQEAKEQFERQSQTLQQQVTVNTEELKG 288
Cdd:COG4942 93 AELRAELEAQKEELAELLRAL------------------YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 289 FEVQVTELRRTYQNLEIE---LQSHLSMKESLERNLEDVKARYASQLAAIQEMLSSLEAQLMQIRSDTERqnqehniLLD 365
Cdd:COG4942 155 LRADLAELAALRAELEAEraeLEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE-------LEA 227
|
250 260
....*....|....*....|...
gi 21592285 366 IKTRLEQEIATYRRLLEGEDIKT 388
Cdd:COG4942 228 LIARLEAEAAAAAERTPAAGFAA 250
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
175-359 |
1.60e-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: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 175 AVEADLQGLskvydnLTLQKTDLEI-QIEELNKDLALLKKEHQEEVEVLRRQLgNNVNVEVDAApglnlgeimNEMRQRY 253
Cdd:COG1579 1 AMPEDLRAL------LDLQELDSELdRLEHRLKELPAELAELEDELAALEARL-EAAKTELEDL---------EKEIKRL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 254 EvlaqKNLQEAKEQFERqSQTLQQQVTvNTEELKGFEVQVTELRRTYQNLEIELQSHLSMKESLERNLEDVKARYASQLA 333
Cdd:COG1579 65 E----LEIEEVEARIKK-YEEQLGNVR-NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138
|
170 180
....*....|....*....|....*.
gi 21592285 334 AIQEMLSSLEAQLMQIRSDTERQNQE 359
Cdd:COG1579 139 ELEEKKAELDEELAELEAELEELEAE 164
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
82-378 |
1.89e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 82 QNLNDRLANYLEKVRSLEQSNSRLEAQIKQWYETNAPSTIRDYSSYYAQIKELQNQVKDAQVQNAQCVLRIDNAKLAAED 161
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 162 FRLKFETERGMRIAVEAD--------------------------LQGLSKVYDNLTLQKTDLEIQIEELNkDLALLKKEH 215
Cdd:COG4717 239 AALEERLKEARLLLLIAAallallglggsllsliltiagvlflvLGLLALLFLLLAREKASLGKEAEELQ-ALPALEELE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 216 QEEVEVLRRQLGNNVNVEVDAApgLNLGEIMNEMRQRYEVLAQKNLQEAKEQFERQSQTLQQQVTVNTEE-----LKGFE 290
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEEL--LELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEelraaLEQAE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 291 vQVTELRRTYQNLEIELQSHLS---------MKESLERNLEDVKAR---YASQLAAIQEMLSSLEAQLMQIRSDTE--RQ 356
Cdd:COG4717 396 -EYQELKEELEELEEQLEELLGeleellealDEEELEEELEELEEEleeLEEELEELREELAELEAELEQLEEDGElaEL 474
|
330 340
....*....|....*....|..
gi 21592285 357 NQEHNILLDIKTRLEQEIATYR 378
Cdd:COG4717 475 LQELEELKAELRELAEEWAALK 496
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
82-343 |
3.20e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 82 QNLNDRLANYLEKVRSLEQSNSRLEAQIKQWYET--NAPSTIRDYSSYYAQIKELQNQVKDAQVQNAQCVLRIDNAKLAA 159
Cdd:PRK02224 202 KDLHERLNGLESELAELDEEIERYEEQREQARETrdEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 160 EDFRLKFET--ERGMRIAVEADLQGLSKvyDNLTLQKTDLEIQIEELNKDL---ALLKKEHQEEVEVLRRqlgnnvnvev 234
Cdd:PRK02224 282 RDLRERLEEleEERDDLLAEAGLDDADA--EAVEARREELEDRDEELRDRLeecRVAAQAHNEEAESLRE---------- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 235 DAApglNLGEIMNEMRQRYEVLaQKNLQEAKEQFERQSQTLqqqvtvntEELkgfEVQVTELRRTYQNLEIELQSHLSMK 314
Cdd:PRK02224 350 DAD---DLEERAEELREEAAEL-ESELEEAREAVEDRREEI--------EEL---EEEIEELRERFGDAPVDLGNAEDFL 414
|
250 260
....*....|....*....|....*....
gi 21592285 315 ESLERNLEDVKARYASQLAAIQEMLSSLE 343
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVE 443
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
250-397 |
3.52e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 250 RQRYeVLAQKNlQEAKEQFERQSQTLQQQVTVNTEELKGFEVQ---VTELRRTYQNLEiELQSHLSMKESLERNLEDVKA 326
Cdd:COG4913 599 RSRY-VLGFDN-RAKLAALEAELAELEEELAEAEERLEALEAEldaLQERREALQRLA-EYSWDEIDVASAEREIAELEA 675
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21592285 327 RYA------SQLAAIQEMLSSLEAQLMQIRSDTERQNQEHNILLDIKTRLEQEIATYRRLLEGEDIKTTEYQLSTLE 397
Cdd:COG4913 676 ELErldassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
123-374 |
3.79e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.82 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 123 DYSSYYAQIKELQNQVKDAQVQnaqcvlrIDNAKLAAEDFRLKFETERgmriaveADLQGLSKVYDNLTLQKTD------ 196
Cdd:pfam12128 612 ALQSAREKQAAAEEQLVQANGE-------LEKASREETFARTALKNAR-------LDLRRLFDEKQSEKDKKNKalaerk 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 197 --LEIQIEELNKDLALLKKEHQEEVEVLRRQLGNNVNV------EVDAAPGLNLGEIMNEMRQRYEVLAQKnLQEAKEQF 268
Cdd:pfam12128 678 dsANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEkqaywqVVEGALDAQLALLKAAIAARRSGAKAE-LKALETWY 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 269 ERQSQTLQqqvtVNTEELKGFEVQVTELRRTYQNLEIELQSHLSMKESLERNLEDVKARYASQLAAIQEMLSSLEAQLMQ 348
Cdd:pfam12128 757 KRDLASLG----VDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLAR 832
|
250 260
....*....|....*....|....*.
gi 21592285 349 IRSDTERQNQEHNILLDIKTRLEQEI 374
Cdd:pfam12128 833 LIADTKLRRAKLEMERKASEKQQVRL 858
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
201-346 |
7.18e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 37.24 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 201 IEELNKDLALLKKEHQEEVEVLRRQLGNNVNvEVDAApglnLGEIMNEMRQRYEVLAQknlqEAKEQFERQSQTLQQQVT 280
Cdd:pfam01442 28 VDRLEKETEALRERLQKDLEEVRAKLEPYLE-ELQAK----LGQNVEELRQRLEPYTE----ELRKRLNADAEELQEKLA 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21592285 281 VNTEELKGfevqvtelrRTYQNLEiELQSHL-----SMKESLERNLEDVKARYASQLAAIQEMLSSLEAQL 346
Cdd:pfam01442 99 PYGEELRE---------RLEQNVD-ALRARLapyaeELRQKLAERLEELKESLAPYAEEVQAQLSQRLQEL 159
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
247-364 |
8.44e-03 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 37.44 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 247 NEMRQRYEVLAQKNLQEAKEQFERQSQTLQQQVTVNTEELKGfevQVTELRRTYQNLEIELQS---HLSMKESLERNLED 323
Cdd:pfam14988 13 TEEKQKKIEKLWNQYVQECEEIERRRQELASRYTQQTAELQT---QLLQKEKEQASLKKELQAlrpFAKLKESQEREIQD 89
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 21592285 324 VKARYASQLAAIQEMLSSLEAQLMQIRSDTERQNQEHNILL 364
Cdd:pfam14988 90 LEEEKEKVRAETAEKDREAHLQFLKEKALLEKQLQELRILE 130
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
248-426 |
9.37e-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: 38.51 E-value: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 248 EMRQRYEVLAQKNLQEAKEQFERQSQTLQQQVTVNTEELKGFEVQVTELRRTYQNLEIELQ------SHLSMKESLE--R 319
Cdd:TIGR02169 215 ALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEelnkkiKDLGEEEQLRvkE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21592285 320 NLEDVKARYAS---QLAAIQEMLSSLEAQLMQIRSDTERQNQEHnilldikTRLEQEIATYRRLLE--GEDIKTTEYQLS 394
Cdd:TIGR02169 295 KIGELEAEIASlerSIAEKERELEDAEERLAKLEAEIDKLLAEI-------EELEREIEEERKRRDklTEEYAELKEELE 367
|
170 180 190
....*....|....*....|....*....|..
gi 21592285 395 TLEMKDIKKTRKIKTVVEEVVDGKVVSSEVKE 426
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
|
|
| |
