|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
82-393 |
4.54e-151 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 429.73 E-value: 4.54e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 82 NEKITMQNLNDRLASYLDKVRALEQANGELEVKIRDWYQKQGPGPSRDYNHYFKTIEDLRDKILGATIDNSKIVLQIDNA 161
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 162 RLAADDFRTKFETEHALRLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAYLKKNHEEEITALRSQVG-GQVSVEV 240
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 241 DSTPGVDLAKILSEMRSQYEIMAEKNRKDAEATYLARIEELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIELQSQLSMK 320
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6680606 321 AALEGTLAETEARYGVQLSQIQSVISGFEAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATYRSLLEGQEAH 393
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
137-399 |
1.91e-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: 59.69 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 137 IEDLRDKILGATIDNSKIVLQIDNARLAADDFRTKFETEHALRLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAY 216
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 217 L---KKNHEEEITALRSQVGG-QVSVEVDSTPGVDLAKILSEMRSQY---EIMAEKNRKDAEATYlARIEELNTQVAVHS 289
Cdd:TIGR02168 773 AeeeLAEAEAEIEELEAQIEQlKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATE-RRLEDLEEQIEELS 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 290 EQIQISKTEVTDLRRTLQGLEIELQSQLSMKAALEGTLAETEARYGVQLSQIQSVisgfEAQLSDVRADIERQNQEYKQL 369
Cdd:TIGR02168 852 EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL----ESKRSELRRELEELREKLAQL 927
|
250 260 270
....*....|....*....|....*....|....*...
gi 6680606 370 MDIKSRLEQEIAT--------YRSLLEGQEAHYNNLPT 399
Cdd:TIGR02168 928 ELRLEGLEVRIDNlqerlseeYSLTLEEAEALENKIED 965
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-388 |
2.00e-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: 56.60 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 190 RRVLDELTLARTDLEMQIESLKEELAYLKKNHEE-----------------EITALRSQVG------GQVSVEVDSTpGV 246
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEEleeeleqlrkeleelsrQISALRKDLArleaevEQLEERIAQL-SK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 247 DLAKILSEMRSQYEIMAEKNRKDAEAtyLARIEELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIELQSQLSMKAALEGT 326
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEA--EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6680606 327 LAETEARYGV---QLSQIQSVISGFEAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATYRSLLE 388
Cdd:TIGR02168 833 IAATERRLEDleeQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
137-397 |
2.41e-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: 56.22 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 137 IEDLRDKILGATIDNSKIVLQIDNARLAADDFRTKFETEHALRLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAY 216
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 217 L----------------KKNHEEEITALRSQVGGQVSVEVDStpgvdLAKILSEMRSQYEIMAEKNR-KDAEATYLAR-I 278
Cdd:TIGR02168 314 LerqleeleaqleelesKLDELAEELAELEEKLEELKEELES-----LEAELEELEAELEELESRLEeLEEQLETLRSkV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 279 EELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIELQSQLsmKAALEGTLAETEArygvQLSQIQSVISGFEAQLSDVRAD 358
Cdd:TIGR02168 389 AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL--KKLEEAELKELQA----ELEELEEELEELQEELERLEEA 462
|
250 260 270
....*....|....*....|....*....|....*....
gi 6680606 359 IERQNQEYKQLMDIKSRLEQEIATYRSLLEGQEAHYNNL 397
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
189-388 |
1.93e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 189 LRRVLDELTLARTDLEMQIESLKEELAylkkNHEEEITALRSQVGGqVSVEVDSTpgvDLAKILSEMRSQYEiMAEKNRK 268
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELE----EAEAALEEFRQKNGL-VDLSEEAK---LLLQQLSELESQLA-EARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 269 DAEAtylaRIEELNTQVAVHSEQIQ--ISKTEVTDLRRTLQGLEIELQSQLS-----------MKAALEGTLAETEARYG 335
Cdd:COG3206 237 EAEA----RLAALRAQLGSGPDALPelLQSPVIQQLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQ 312
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6680606 336 VQLSQIQSVISGFEAQLSDVRADIERQNQEYKQLMDIK---SRLEQEIATYRSLLE 388
Cdd:COG3206 313 RILASLEAELEALQAREASLQAQLAQLEARLAELPELEaelRRLEREVEVARELYE 368
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
251-392 |
2.72e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 251 ILSEMRSQY--------------EIMAEKNRKDAEAtYLARIEELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIELQSQ 316
Cdd:COG1196 194 ILGELERQLeplerqaekaeryrELKEELKELEAEL-LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6680606 317 LSMKAALEGTLAETEARY---GVQLSQIQSVISGFEAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATYRSLLEGQEA 392
Cdd:COG1196 273 RLELEELELELEEAQAEEyelLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
157-385 |
3.21e-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: 45.53 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 157 QIDNARLAADDFRTKFETEHALRLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAYLKKNHEEEITALRSQVggqv 236
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 237 svevdstpgvdlaKILSEMRSQYEIMAEKNRKDAEATY--LARIEELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIELQ 314
Cdd:COG4942 111 -------------RALYRLGRQPPLALLLSPEDFLDAVrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6680606 315 SQLSMKAALEGTLAEtearygvQLSQIQSVISGFEAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATYRS 385
Cdd:COG4942 178 ALLAELEEERAALEA-------LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
140-393 |
6.89e-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: 6.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 140 LRDKILGATIDNSKIVLQIDNARLAADDFRTKFETEHALRLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAYLKK 219
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 220 NHEEEITALRSQVGGQVSVEvdstpgVDLAKILSEMrsqYEIMAEKNRKDAEATYL-ARIEELNTQVAVHSEQIQISKTE 298
Cdd:TIGR02169 372 ELEEVDKEFAETRDELKDYR------EKLEKLKREI---NELKRELDRLQEELQRLsEELADLNAAIAGIEAKINELEEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 299 VTDLRRTLQGLEIELQSQLSMKAALEGT---LAETEARYGVQLSQIQSVISGFEAQLSDVRadiERQNQEYKQLMDIKSR 375
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLAADLSKYEQElydLKEEYDRVEKELSKLQRELAEAEAQARASE---ERVRGGRAVEEVLKAS 519
|
250
....*....|....*...
gi 6680606 376 LEQEIATYRSLLEGQEAH 393
Cdd:TIGR02169 520 IQGVHGTVAQLGSVGERY 537
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
159-385 |
8.77e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 8.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 159 DNARLAADDFRTKF--ETEHALRLSVEA----DINGLRRVLDELTLARTDLEMQIESLKEELAYLKKNHEEEITALRsqv 232
Cdd:COG4913 173 DSFSAYLARLRRRLgiGSEKALRLLHKTqsfkPIGDLDDFVREYMLEEPDTFEAADALVEHFDDLERAHEALEDARE--- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 233 ggQVsvevdstpgvdlaKILSEMRSQYE----IMAEKNRKDAEATYL-------------ARIEELNTQVAVHSEQIQIS 295
Cdd:COG4913 250 --QI-------------ELLEPIRELAEryaaARERLAELEYLRAALrlwfaqrrlelleAELEELRAELARLEAELERL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 296 KTEVTDLRRTLQGLEI-----------ELQSQLSMK------------------AALEGTLAETEARYGVQLSQIQSVIS 346
Cdd:COG4913 315 EARLDALREELDELEAqirgnggdrleQLEREIERLereleererrrarleallAALGLPLPASAEEFAALRAEAAALLE 394
|
250 260 270
....*....|....*....|....*....|....*....
gi 6680606 347 GFEAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATYRS 385
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
272-388 |
1.34e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 272 ATYLARIEELNTQVAVHSEQIQISKTE---VTDLRRTLQGLEiELQSQLSMKAALEGTLAETEARYGvQLSQIQSVISGF 348
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAEldaLQERREALQRLA-EYSWDEIDVASAEREIAELEAELE-RLDASSDDLAAL 690
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 6680606 349 EAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATYRSLLE 388
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
207-392 |
1.59e-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: 43.90 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 207 IESLKEELAYLKKNhEEEITALRSQVGGQVSvevdstpgvDLAKILSEMRSQYEIMAEKNRKDAEatylaRIEELntqva 286
Cdd:TIGR02169 683 LEGLKRELSSLQSE-LRRIENRLDELSQELS---------DASRKIGEIEKEIEQLEQEEEKLKE-----RLEEL----- 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 287 vhSEQIQISKTEVTDLRRTLQGLEIELQSQLSMKAALEGTLAETEARYGVQ-LSQIQSVISGFEAQLSDVRADIERQNQE 365
Cdd:TIGR02169 743 --EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSrIPEIQAELSKLEEEVSRIEARLREIEQK 820
|
170 180 190
....*....|....*....|....*....|
gi 6680606 366 YKQLMDIKSRLEQEIAT---YRSLLEGQEA 392
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQElqeQRIDLKEQIK 850
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
157-378 |
1.65e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 157 QIDNARLAADDFRTKfeteHALrLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAYLKKnheeeitalrsqvggQV 236
Cdd:COG3206 190 ELEEAEAALEEFRQK----NGL-VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRA---------------QL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 237 SVEVDSTPGVDLAKILSEMRSQYeIMAEKNRKDAEATYLAR---IEELNTQVAVHSEQIQisktevTDLRRTLQGLEIEL 313
Cdd:COG3206 250 GSGPDALPELLQSPVIQQLRAQL-AELEAELAELSARYTPNhpdVIALRAQIAALRAQLQ------QEAQRILASLEAEL 322
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6680606 314 QSQLSMKAALEGTLAETEARYGvQLSQIQsvisgfeAQLSDVRADIERQNQEYKQLMdikSRLEQ 378
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLA-ELPELE-------AELRRLEREVEVARELYESLL---QRLEE 376
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
89-397 |
2.66e-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: 43.18 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 89 NLNDRLASYLDKVRALEQA-NGELEVKIRDWYQKQGPGPSRDynHYFKTIEDLRDKI--LGATID--NSKIVLQIDNARL 163
Cdd:pfam15921 374 NLDDQLQKLLADLHKREKElSLEKEQNKRLWDRDTGNSITID--HLRRELDDRNMEVqrLEALLKamKSECQGQMERQMA 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 164 AADDFRTKFETEHALRLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAYLKKNHE------EEITALRSQVGGQVS 237
Cdd:pfam15921 452 AIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERaieatnAEITKLRSRVDLKLQ 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 238 -VEVDSTPGVDLAKILSEMRSQYEIMAEKNRkdAEATYLARIEELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIELQSQ 316
Cdd:pfam15921 532 eLQHLKNEGDHLRNVQTECEALKLQMAEKDK--VIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEF 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 317 LSMKAALEGTLAETEARYG-VQLSQIQSVISGFEaQLSDVRaDIErqnQEYKQLMDiksrleqEIATYRSLLEGQEAHYN 395
Cdd:pfam15921 610 KILKDKKDAKIRELEARVSdLELEKVKLVNAGSE-RLRAVK-DIK---QERDQLLN-------EVKTSRNELNSLSEDYE 677
|
..
gi 6680606 396 NL 397
Cdd:pfam15921 678 VL 679
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
182-392 |
3.28e-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: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 182 VEADINGLRRVLDELTLARTDLEMQIESLKEELAYLKKNHEEEITALRSQVGgqvsvevdstpgvDLAKILSEM-RSQYE 260
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA-------------EEYELLAELaRLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 261 IMAEKNRKDAEAtylARIEELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIELqsqlsmkAALEGTLAETEARYGV---Q 337
Cdd:COG1196 304 IARLEERRRELE---ERLEELEEELAELEEELEELEEELEELEEELEEAEEEL-------EEAEAELAEAEEALLEaeaE 373
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6680606 338 LSQIQSVISGFEAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATYRSLLEGQEA 392
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
135-394 |
3.60e-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: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 135 KTIEDLRDKILGATIDNSKIVLQIDNARLAADDFRTKFETEHALRLSVEADI--------------NGLRRVLDELTLAR 200
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELarleqdiarleerrRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 201 TDLEMQIESLKEELAYLKKNHEEEITALRSQvggQVSVEvdstpgvDLAKILSEMRSQYE--IMAEKNRKDAEATYLARI 278
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEA---EAELA-------EAEEALLEAEAELAeaEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 279 EELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIELQSQLSMKAALEGTLAETEARYGVQLSQiqsvisgfEAQLSDVRAD 358
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE--------EEALLELLAE 467
|
250 260 270
....*....|....*....|....*....|....*.
gi 6680606 359 IERQNQEYKQLMDIKSRLEQEIATYRSLLEGQEAHY 394
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
157-354 |
5.99e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 157 QIDNARLAADDFRTKFETEHALRLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAYLKKN---HEEEITALRSQVG 233
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiasLNNEIERLEARLE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 234 G-QVSVEVDSTPGVDLAKILSEMRSQyEIMAEKNRKDAEatylarIEELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIE 312
Cdd:TIGR02168 411 RlEDRRERLQQEIEELLKKLEEAELK-ELQAELEELEEE------LEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6680606 313 LQSQLSMKAALEGTL--AETEARYGVQLSQIQSVISGFEAQLSD 354
Cdd:TIGR02168 484 LAQLQARLDSLERLQenLEGFSEGVKALLKNQSGLSGILGVLSE 527
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
159-368 |
9.38e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 9.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 159 DNARLAADDFRTKFETEHALRLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAYLKKN------------------ 220
Cdd:COG4913 585 GNGTRHEKDDRRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidva 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 221 -HEEEITALRSQVGgqvsvEVDSTPGVdlakiLSEMRSQYEImAEKNRKDAEatylARIEELNTQVAVHSEQIQISKTEV 299
Cdd:COG4913 665 sAEREIAELEAELE-----RLDASSDD-----LAALEEQLEE-LEAELEELE----EELDELKGEIGRLEKELEQAEEEL 729
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6680606 300 TDLRRTLQGLEIELQSQLSmkAALEGTLAE--TEARYGVQLSQIQSVISGFEAQLSDVRADIERQNQEYKQ 368
Cdd:COG4913 730 DELQDRLEAAEDLARLELR--ALLEERFAAalGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
246-397 |
9.94e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 246 VDLAKILSEMRSqyeimAEKNRKDAEAtylaRIEELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIELQsqlsmkaaleg 325
Cdd:COG1579 10 LDLQELDSELDR-----LEHRLKELPA----ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE----------- 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6680606 326 TLAETEARYGVQLSQIQSV--ISGFEAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATYRSLLEGQEAHYNNL 397
Cdd:COG1579 70 EVEARIKKYEEQLGNVRNNkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
135-383 |
1.11e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 135 KTIEDL-------------RDKILGATIDNSKIVLQIDNA--RLAAddfRTKFETEhaLRLSVEADINGLRRVLDELTLA 199
Cdd:PHA02562 154 KLVEDLldisvlsemdklnKDKIRELNQQIQTLDMKIDHIqqQIKT---YNKNIEE--QRKKNGENIARKQNKYDELVEE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 200 RTDLEMQIESLKEELAYLKKNHEEEITALR--SQVGGQVSVEVDStpgvdLAKIL-------------SEMRSQYEIMAE 264
Cdd:PHA02562 229 AKTIKAEIEELTDELLNLVMDIEDPSAALNklNTAAAKIKSKIEQ-----FQKVIkmyekggvcptctQQISEGPDRITK 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 265 KNRKDAEATYlaRIEELNTQVavhsEQIQISKTEVTDLRRTLQgleiELQSQLSmkaALEGTLAETEArygvQLSQIQSV 344
Cdd:PHA02562 304 IKDKLKELQH--SLEKLDTAI----DELEEIMDEFNEQSKKLL----ELKNKIS---TNKQSLITLVD----KAKKVKAA 366
|
250 260 270
....*....|....*....|....*....|....*....
gi 6680606 345 ISGFEAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATY 383
Cdd:PHA02562 367 IEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
235-392 |
1.53e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 40.22 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 235 QVSVEVDSTPGV----------DLAKILSEM---RSQYEI--MAEKNRKDAeatyLARIEElntQVAVHSEQIQISKTEV 299
Cdd:COG3524 128 RVKVEYDSTSGIitlevrafdpEDAQAIAEAllaESEELVnqLSERAREDA----VRFAEE---EVERAEERLRDAREAL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 300 TDLRRTLQGL--EIELQSQLSMKAALEGTLAETEArygvQLSQIQSVISGFEAQLSDVRADIErqnqeykqlmdiksRLE 377
Cdd:COG3524 201 LAFRNRNGILdpEATAEALLQLIATLEGQLAELEA----ELAALRSYLSPNSPQVRQLRRRIA--------------ALE 262
|
170
....*....|....*
gi 6680606 378 QEIATYRSLLEGQEA 392
Cdd:COG3524 263 KQIAAERARLTGASG 277
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
177-388 |
1.95e-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: 40.26 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 177 ALRLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAYLKKNHEEEitalrsqvggqvsvevdstpgvdLAKILSEMR 256
Cdd:pfam07888 52 AANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEEL-----------------------EEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 257 SQYEIMAEKNR-KDAEATYLARIEELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIELQSQLSMKAALEGTLAETEARYG 335
Cdd:pfam07888 109 SSEELSEEKDAlLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6680606 336 VQLSQIQSVISGFEAQLSDV---RADIERQNQEYKQLMDIKSRLEQEIATYRSLLE 388
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVlqlQDTITTLTQKLTTAHRKEAENEALLEELRSLQE 244
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
193-360 |
3.21e-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: 38.40 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 193 LDELTLARTDLEMQIESLKEELaylKKNHEEEITALRSQVGGQVS-VEVDSTPGVD-----LAKILSEMRSQYEIMAEKN 266
Cdd:pfam01442 6 LDELSTYAEELQEQLGPVAQEL---VDRLEKETEALRERLQKDLEeVRAKLEPYLEelqakLGQNVEELRQRLEPYTEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 267 RKDAEAtylaRIEELNTQVAVHSEQIQ-ISKTEVTDLRRTLQGLEIELQSQLSMKA-ALEGTLAETEARYGVQLSQ-IQS 343
Cdd:pfam01442 83 RKRLNA----DAEELQEKLAPYGEELReRLEQNVDALRARLAPYAEELRQKLAERLeELKESLAPYAEEVQAQLSQrLQE 158
|
170
....*....|....*..
gi 6680606 344 VISGFEAQLSDVRADIE 360
Cdd:pfam01442 159 LREKLEPQAEDLREKLD 175
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
276-397 |
4.71e-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: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 276 ARIEELNTQVAVHSEQIQISKTEVTDLRRTLQGLE----------IELQSQLSMKAALEGTLAETEARYGVQLSQIQSVI 345
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEeeleqlrkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 6680606 346 SGFEAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATYRSLLEGQEAHYNNL 397
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
75-388 |
5.53e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 38.79 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 75 SDGLLSGNEKITMQNLNDRLASYLDKVRALEQANGELE--VKIRDWYQKQGPGPSRDY--------NHYFKTIEDLRDKI 144
Cdd:COG5185 219 STLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEklVEQNTDLRLEKLGENAESskrlnenaNNLIKQFENTKEKI 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 145 LGATIDNS-KIVLQIDNARLAADDFRTKFEtehALRLSVEADINGLRRvldELTLARTDLEMQIESLKEELAYLKknhEE 223
Cdd:COG5185 299 AEYTKSIDiKKATESLEEQLAAAEAEQELE---ESKRETETGIQNLTA---EIEQGQESLTENLEAIKEEIENIV---GE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 224 EITALRSQVGGQVSVEVDSTPgvdlAKILSEMRSQ--YEIMAEKNRKDAEATYLARIEELNTQV----AVHSEQIQISKT 297
Cdd:COG5185 370 VELSKSSEELDSFKDTIESTK----ESLDEIPQNQrgYAQEILATLEDTLKAADRQIEELQRQIeqatSSNEEVSKLLNE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 298 EVTDLRRTLQGLEIELQSQLSMKA-ALEGTLAETEARYGVQLSQIQSVISGFEAQLSDVRADIERQNQEYKQLMDIKSRL 376
Cdd:COG5185 446 LISELNKVMREADEESQSRLEEAYdEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAES 525
|
330
....*....|..
gi 6680606 377 EQEIATYRSLLE 388
Cdd:COG5185 526 LKDFMRARGYAH 537
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
247-391 |
5.70e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 38.93 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606 247 DLAKILSE-MRSQYEIMAEKNRKDAE--ATYLARIEELNTQVAVhseqIQISKTEVTDLRRTLQGLEIELQSQLSMKAAL 323
Cdd:pfam03528 12 ELEKENAEfYRLKQQLEAEFNQKRAKfkELYLAKEEDLKRQNAV----LQEAQVELDALQNQLALARAEMENIKAVATVS 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6680606 324 EGTlaETEARYGVQlSQIQSVISGFEAQLSDVRADIERQ-----NQEYKQLMDIKSRLEQEIATY-RSLLEGQE 391
Cdd:pfam03528 88 ENT--KQEAIDEVK-SQWQEEVASLQAIMKETVREYEVQfhrrlEQERAQWNQYRESAEREIADLrRRLSEGQE 158
|
|
|