|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
82-393 |
1.56e-145 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 415.47 E-value: 1.56e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 82 NEKITMQNLNDRLASYLDKVRALEQANGELEVKIRDWYQKQGPGPFRDYSQYFKTIEDLRDKILGATIENSKIVLQIDNA 161
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 162 RLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIENLKEELAYLKKNHEEEISALRSQVG-GQVSVEV 240
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 241 DSTPGIDLAKILSEMRSQYEAMAEKNRKDAEAWYLTQIDELNTQVAVHTTQIQINKTEVTELRRKVQDLEIELQSQLSMK 320
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42409519 321 AALEGTVAEIEARYGAQLSHIQGVISSIEVQLSNVRADTERQNQEYQQLMDIKSRLEQEIATYRSLLEGQEAH 393
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
137-391 |
1.97e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 137 IEDLRDKILGATIENSKIVLQIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIENLKEELAY 216
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 217 L----------------KKNHEEEISALRSQVGGQVSVEVDStpgidLAKILSEMRSQYEAMAEKNRKDAEAW--YLTQI 278
Cdd:TIGR02168 314 LerqleeleaqleelesKLDELAEELAELEEKLEELKEELES-----LEAELEELEAELEELESRLEELEEQLetLRSKV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 279 DELNTQVAVHTTQIQINKTEVTEL--RRKVQDLEIELQSQLSMKAALEGTVAEIEARyGAQLSHIQGVISSIEVQLSNVR 356
Cdd:TIGR02168 389 AQLELQIASLNNEIERLEARLERLedRRERLQQEIEELLKKLEEAELKELQAELEEL-EEELEELQEELERLEEALEELR 467
|
250 260 270
....*....|....*....|....*....|....*
gi 42409519 357 ADTERQNQEYQQLMDIKSRLEQEIATYRSLLEGQE 391
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
189-403 |
4.79e-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: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 189 LRRVLDELTLARTDLEMQIENLKEELAylkkNHEEEISALRSQVGGqVSVEVDSTpgiDLAKILSEMRSQYEAmAEKNRK 268
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELE----EAEAALEEFRQKNGL-VDLSEEAK---LLLQQLSELESQLAE-ARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 269 DAEAwyltQIDELNTQVAVHTTQIQ--INKTEVTELRRKVQDLEIELQSQLS-----------MKAALEGTVAEIEARYG 335
Cdd:COG3206 237 EAEA----RLAALRAQLGSGPDALPelLQSPVIQQLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQ 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42409519 336 AQLSHIQGVISSIEVQLSNVRADTERQNQEYQQLMDIK---SRLEQEIATYRSLLEGQEAHYNSLSIAKAL 403
Cdd:COG3206 313 RILASLEAELEALQAREASLQAQLAQLEARLAELPELEaelRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
135-383 |
1.76e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 135 KTIEDL-------------RDKILGATIENSKIVLQIDNA--RLAAddfRTKFETEQalRMSVEADINGLRRVLDELTLA 199
Cdd:PHA02562 154 KLVEDLldisvlsemdklnKDKIRELNQQIQTLDMKIDHIqqQIKT---YNKNIEEQ--RKKNGENIARKQNKYDELVEE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 200 RTDLEMQIENLKEELAYLKKNHEEEISALR--SQVGGQVSVEVDStpgidLAKILSEMR------------SQYEAMAEK 265
Cdd:PHA02562 229 AKTIKAEIEELTDELLNLVMDIEDPSAALNklNTAAAKIKSKIEQ-----FQKVIKMYEkggvcptctqqiSEGPDRITK 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 266 NRKDAEAwYLTQIDELNTqvavHTTQIQINKTEVTELRRKVQdleiELQSQLS-MKAALEGTVAEIEArygaqlshIQGV 344
Cdd:PHA02562 304 IKDKLKE-LQHSLEKLDT----AIDELEEIMDEFNEQSKKLL----ELKNKIStNKQSLITLVDKAKK--------VKAA 366
|
250 260 270
....*....|....*....|....*....|....*....
gi 42409519 345 ISSIEVQLSNVRADTERQNQEYQQLMDIKSRLEQEIATY 383
Cdd:PHA02562 367 IEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
132-308 |
1.76e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.00 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 132 QYFKTIEDLRDKIlgatieNSKIVLQIDNARLAAD----DFRTKFEteQALRMSVEADINGLRRVLDELTlartDLEMQI 207
Cdd:smart00787 103 EYFSASPDVKLLM------DKQFQLVKTFARLEAKkmwyEWRMKLL--EGLKEGLDENLEGLKEDYKLLM----KELELL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 208 ENLKEELAYLKKNHEEEISALRsqvggQVSVEVDSTPGIDLAKILSEMRSQYEAMAEKNRKDAEawYLTQIDELNTQVAV 287
Cdd:smart00787 171 NSIKPKLRDRKDALEEELRQLK-----QLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEE--LEEELQELESKIED 243
|
170 180
....*....|....*....|.
gi 42409519 288 HTTQIQINKTEVTELRRKVQD 308
Cdd:smart00787 244 LTNKKSELNTEIAEAEKKLEQ 264
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
82-393 |
1.56e-145 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 415.47 E-value: 1.56e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 82 NEKITMQNLNDRLASYLDKVRALEQANGELEVKIRDWYQKQGPGPFRDYSQYFKTIEDLRDKILGATIENSKIVLQIDNA 161
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 162 RLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIENLKEELAYLKKNHEEEISALRSQVG-GQVSVEV 240
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 241 DSTPGIDLAKILSEMRSQYEAMAEKNRKDAEAWYLTQIDELNTQVAVHTTQIQINKTEVTELRRKVQDLEIELQSQLSMK 320
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42409519 321 AALEGTVAEIEARYGAQLSHIQGVISSIEVQLSNVRADTERQNQEYQQLMDIKSRLEQEIATYRSLLEGQEAH 393
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
137-391 |
1.97e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 137 IEDLRDKILGATIENSKIVLQIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIENLKEELAY 216
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 217 L----------------KKNHEEEISALRSQVGGQVSVEVDStpgidLAKILSEMRSQYEAMAEKNRKDAEAW--YLTQI 278
Cdd:TIGR02168 314 LerqleeleaqleelesKLDELAEELAELEEKLEELKEELES-----LEAELEELEAELEELESRLEELEEQLetLRSKV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 279 DELNTQVAVHTTQIQINKTEVTEL--RRKVQDLEIELQSQLSMKAALEGTVAEIEARyGAQLSHIQGVISSIEVQLSNVR 356
Cdd:TIGR02168 389 AQLELQIASLNNEIERLEARLERLedRRERLQQEIEELLKKLEEAELKELQAELEEL-EEELEELQEELERLEEALEELR 467
|
250 260 270
....*....|....*....|....*....|....*
gi 42409519 357 ADTERQNQEYQQLMDIKSRLEQEIATYRSLLEGQE 391
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
84-390 |
7.26e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 84 KITMQNLNDRLASYLDKVRALEQANGELEVKIRDwYQKQGpgpfrdySQYFKTIEDLRDKILGATIENSKIVLQIDNARL 163
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEE-LEEEL-------EQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 164 AADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIENLKEELAYLKKNH---EEEISALRSQVGGQVSVEV 240
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 241 DSTPGIDLAKILSEMRSQYEAMAEKNRKDAEAwyltQIDELNTQVAVHTTQIQINKTEVTELRRKVQDLEIELQSQLSMK 320
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAA----EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42409519 321 AALEGTVAEIEARYGA---QLSHIQGVISSIEVQLSNVRadtERQNQEYQQLMDIKSRLEQEIATYRSLLEGQ 390
Cdd:TIGR02168 904 RELESKRSELRRELEElreKLAQLELRLEGLEVRIDNLQ---ERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
189-403 |
4.79e-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: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 189 LRRVLDELTLARTDLEMQIENLKEELAylkkNHEEEISALRSQVGGqVSVEVDSTpgiDLAKILSEMRSQYEAmAEKNRK 268
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELE----EAEAALEEFRQKNGL-VDLSEEAK---LLLQQLSELESQLAE-ARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 269 DAEAwyltQIDELNTQVAVHTTQIQ--INKTEVTELRRKVQDLEIELQSQLS-----------MKAALEGTVAEIEARYG 335
Cdd:COG3206 237 EAEA----RLAALRAQLGSGPDALPelLQSPVIQQLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQ 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42409519 336 AQLSHIQGVISSIEVQLSNVRADTERQNQEYQQLMDIK---SRLEQEIATYRSLLEGQEAHYNSLSIAKAL 403
Cdd:COG3206 313 RILASLEAELEALQAREASLQAQLAQLEARLAELPELEaelRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
135-403 |
4.58e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 135 KTIEDLRDKILGATIENSKIVLQIDNARLAADDFRTKFETEQALRMSVEADI--------------NGLRRVLDELTLAR 200
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELarleqdiarleerrRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 201 TDLEMQIENLKEELAYLKKNHEEEISALRSQVggqvsvevdstpgIDLAKILSEMRSQYEAMAEKNRKDAEAWYltQIDE 280
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAE-------------AELAEAEEALLEAEAELAEAEEELEELAE--ELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 281 LNTQVAVHTTQIQINKTEVTELRRKVQDLEIELQSQLSMKAALEGTVAEIEARYGAQLSHIQGVISSIEVQLSNVRADTE 360
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 42409519 361 RQNQEYQQLMDIKSRLEQEIATYRSLLEGQEAHYNSLSIAKAL 403
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
184-401 |
8.41e-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: 45.05 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 184 ADINGLRRVLDELTLARTDLEMQIENLKEELaylkKNHEEEISALRSQVGgQVSVEVDSTPGI--DLAKILSEMRSQyEA 261
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAEL----QELEEKLEELRLEVS-ELEEEIEELQKElyALANEISRLEQQ-KQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 262 MAEKNRKDAEawylTQIDELNTQVAVHTTQIQINKTEVTELRRKVQDLEIELQSQLSMKAALEGTVAEIEARYGAQLSHI 341
Cdd:TIGR02168 306 ILRERLANLE----RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42409519 342 QGV---ISSIEVQLSNVRADTERQNQEYQQLMDIKSRLEQEIATYRSLLEGQEAHYNSLSIAK 401
Cdd:TIGR02168 382 ETLrskVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE 444
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
251-392 |
9.01e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 9.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 251 ILSEMRSQYEA--------------MAEKNRKDAEAWYLtQIDELNTQVAVHTTQIQINKTEVTELRRKVQDLEIELQSQ 316
Cdd:COG1196 194 ILGELERQLEPlerqaekaeryrelKEELKELEAELLLL-KLRELEAELEELEAELEELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42409519 317 LSMKAALEGTVAEIEARY---GAQLSHIQGVISSIEVQLSNVRADTERQNQEYQQLMDIKSRLEQEIATYRSLLEGQEA 392
Cdd:COG1196 273 RLELEELELELEEAQAEEyelLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
97-397 |
1.22e-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: 44.34 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 97 YLDKVRALEQ----ANGEL-EVKI-RDWYQKQGpGPFRDYSQyfKTIEDL--RDKILGATIENSKIV--------LQIDN 160
Cdd:pfam15921 340 YEDKIEELEKqlvlANSELtEARTeRDQFSQES-GNLDDQLQ--KLLADLhkREKELSLEKEQNKRLwdrdtgnsITIDH 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 161 ARLAADDFRTKFETEQALRMSVEADING--------------------------------LRRVLDELTLARTDLEMQIE 208
Cdd:pfam15921 417 LRRELDDRNMEVQRLEALLKAMKSECQGqmerqmaaiqgkneslekvssltaqlestkemLRKVVEELTAKKMTLESSER 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 209 NLKEELAYLKKNHE------EEISALRSQVGGQVS-VEVDSTPGIDLAKILSEMRSQYEAMAEKNRkdAEAWYLTQIDEL 281
Cdd:pfam15921 497 TVSDLTASLQEKERaieatnAEITKLRSRVDLKLQeLQHLKNEGDHLRNVQTECEALKLQMAEKDK--VIEILRQQIENM 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 282 NTQVAVHTTQIQINKTEVTELRRKVQDLEIELQSQLSMKAALEGTVAEIEARygaqlshiqgvISSIEVQ-LSNVRADTE 360
Cdd:pfam15921 575 TQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEAR-----------VSDLELEkVKLVNAGSE 643
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 42409519 361 RqnqeYQQLMDIKSRLEQ---EIATYRSLLEGQEAHYNSL 397
Cdd:pfam15921 644 R----LRAVKDIKQERDQllnEVKTSRNELNSLSEDYEVL 679
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
83-382 |
1.98e-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: 43.57 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 83 EKITMQN----LNDRLASYLDKVRALEQANGEL-EVKIRDWYQKQGPGPFRDYSQYFKTIEDLRDKILGATIENSKIV-- 155
Cdd:pfam15921 487 KKMTLESsertVSDLTASLQEKERAIEATNAEItKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIei 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 156 --LQIDN-ARLAADDFRTKfETEQALRMSVEADINGLRRVLDELTLART-------DLEMQIENLKEELAYLKKNHEEEI 225
Cdd:pfam15921 567 lrQQIENmTQLVGQHGRTA-GAMQVEKAQLEKEINDRRLELQEFKILKDkkdakirELEARVSDLELEKVKLVNAGSERL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 226 SALR--SQVGGQVSVEVDSTpgidlAKILSEMRSQYEAMAEKNRKDAEawyltqidELNTQVAVHTTQIQINKTEVTELR 303
Cdd:pfam15921 646 RAVKdiKQERDQLLNEVKTS-----RNELNSLSEDYEVLKRNFRNKSE--------EMETTTNKLKMQLKSAQSELEQTR 712
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42409519 304 RKVQDLEieLQSQLSMKAALeGTVAEIEARYGaQLSHIQGVISSIEVQLSNVradterqNQEYQQLMDIKSRLEQEIAT 382
Cdd:pfam15921 713 NTLKSME--GSDGHAMKVAM-GMQKQITAKRG-QIDALQSKIQFLEEAMTNA-------NKEKHFLKEEKNKLSQELST 780
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
172-388 |
3.51e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 172 FETEQALRmSVEADINGLRRVLDELTLARTDLEMQIENLKEELAYLKKNHEE---EISALRSQVG------GQVSVEVDS 242
Cdd:TIGR02168 673 LERRREIE-ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrQISALRKDLArleaevEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 243 TpGIDLAKILSEMRSQYEAMAEKNRKDAEAwyLTQIDELNTQVAVHTTQIQINKTEVTElrrkvqdLE-------IELQS 315
Cdd:TIGR02168 752 L-SKELTELEAEIEELEERLEEAEEELAEA--EAEIEELEAQIEQLKEELKALREALDE-------LRaeltllnEEAAN 821
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42409519 316 QLSMKAALEGTVAEIEARYG---AQLSHIQGVISSIEVQLSNVRADTERQNQEYQQLMDIKSRLEQEIATYRSLLE 388
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEdleEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
173-385 |
7.75e-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: 41.29 E-value: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 173 ETEQALRmSVEADINGLRRVLDELTLARTDLEMQIENLKEELAYLKK---NHEEEISALRSQVGgQVSVEVDstpgiDLA 249
Cdd:COG4942 24 EAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEAELA-ELEKEIA-----ELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 250 KILSEMRSQYEAMAEKNRKDAEAWYLT------QIDELNTQVAVHTTQIQINKTEVTELRRKVQDLEIELQSQLSMKAAL 323
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLAlllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42409519 324 EGTVAEIEA---RYGAQLSHIQGVISSIEVQLSNVRADTERQNQEYQQLMDIKSRLEQEIATYRS 385
Cdd:COG4942 177 EALLAELEEeraALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
247-402 |
1.64e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 247 DLAKILSEMRSQYEAMAEKNRKDAEAwyLTQIDELNTQVAVHTTQIQINKTEVTELRRKVQDLEIELqsqlsmkAALEGT 326
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKAL--LKQLAALERRIAALARRIRALEQELAALEAELAELEKEI-------AELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 327 VAEIEARYGAQLSHIQ--GVISSIEVQLSN-------------------VRADTERQNQEYQQLMDIKSRLEQEIATYRS 385
Cdd:COG4942 99 LEAQKEELAELLRALYrlGRQPPLALLLSPedfldavrrlqylkylapaRREQAEELRADLAELAALRAELEAERAELEA 178
|
170
....*....|....*..
gi 42409519 386 LLEGQEAHYNSLSIAKA 402
Cdd:COG4942 179 LLAELEEERAALEALKA 195
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
135-383 |
1.76e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 135 KTIEDL-------------RDKILGATIENSKIVLQIDNA--RLAAddfRTKFETEQalRMSVEADINGLRRVLDELTLA 199
Cdd:PHA02562 154 KLVEDLldisvlsemdklnKDKIRELNQQIQTLDMKIDHIqqQIKT---YNKNIEEQ--RKKNGENIARKQNKYDELVEE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 200 RTDLEMQIENLKEELAYLKKNHEEEISALR--SQVGGQVSVEVDStpgidLAKILSEMR------------SQYEAMAEK 265
Cdd:PHA02562 229 AKTIKAEIEELTDELLNLVMDIEDPSAALNklNTAAAKIKSKIEQ-----FQKVIKMYEkggvcptctqqiSEGPDRITK 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 266 NRKDAEAwYLTQIDELNTqvavHTTQIQINKTEVTELRRKVQdleiELQSQLS-MKAALEGTVAEIEArygaqlshIQGV 344
Cdd:PHA02562 304 IKDKLKE-LQHSLEKLDT----AIDELEEIMDEFNEQSKKLL----ELKNKIStNKQSLITLVDKAKK--------VKAA 366
|
250 260 270
....*....|....*....|....*....|....*....
gi 42409519 345 ISSIEVQLSNVRADTERQNQEYQQLMDIKSRLEQEIATY 383
Cdd:PHA02562 367 IEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
132-308 |
1.76e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.00 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 132 QYFKTIEDLRDKIlgatieNSKIVLQIDNARLAAD----DFRTKFEteQALRMSVEADINGLRRVLDELTlartDLEMQI 207
Cdd:smart00787 103 EYFSASPDVKLLM------DKQFQLVKTFARLEAKkmwyEWRMKLL--EGLKEGLDENLEGLKEDYKLLM----KELELL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 208 ENLKEELAYLKKNHEEEISALRsqvggQVSVEVDSTPGIDLAKILSEMRSQYEAMAEKNRKDAEawYLTQIDELNTQVAV 287
Cdd:smart00787 171 NSIKPKLRDRKDALEEELRQLK-----QLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEE--LEEELQELESKIED 243
|
170 180
....*....|....*....|.
gi 42409519 288 HTTQIQINKTEVTELRRKVQD 308
Cdd:smart00787 244 LTNKKSELNTEIAEAEKKLEQ 264
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
255-388 |
4.11e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 255 MRSQYEAMAEKNRKDA--EAWYL------------TQIDELNTQVAVHTTQIQINKTEVTELRRKVQDLE--IELQSQLS 318
Cdd:COG4913 582 QVKGNGTRHEKDDRRRirSRYVLgfdnraklaaleAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEI 661
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 319 MKAALEGTVAEIEARYgAQLSHIQGVISSIEVQLSNVRADTERQNQEYQQLMDIKSRLEQEIATYRSLLE 388
Cdd:COG4913 662 DVASAEREIAELEAEL-ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
203-398 |
4.55e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 39.34 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 203 LEMQIENLKEELAYLKKNHEEEISALRSQVGG---QVSVEVDSTpgIDLAKILSEMRSQYEAMAEKNRKDAEA--WYLTQ 277
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKRARIELEKKASAlkrQLDRESDRN--QELQKRIRLLEKREAEAEEALREQAELnrLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 278 IDELN--------TQVAVHTTQIQINKtEVTELRRKVQDLEIELQSQLSMKAALEGTVAEIEARYG------AQLSHIQG 343
Cdd:pfam05557 85 LEALNkklnekesQLADAREVISCLKN-ELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASeaeqlrQNLEKQQS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 42409519 344 VISSIEVQLSNVRADTERQNQEYQQLMDIKSRLEQeIATYRSLLEGQE---AHYNSLS 398
Cdd:pfam05557 164 SLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELAR-IPELEKELERLRehnKHLNENI 220
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
181-368 |
5.54e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.66 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 181 SVEADINGLRRVLDELTLARTDLEMQIENLKEELAYLKKN---HEEEISALRSQVGGQVS---VEVDSTPGIDL---AKI 251
Cdd:COG3883 34 AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeAEAEIEERREELGERARalyRSGGSVSYLDVllgSES 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 252 LSEMRSQYEAMAEKNRKDAEAwyLTQIDELNTQVAVHTTQIQINKTEVTELRRKVQDLEIELQSQLSMKAALEGTVAEIE 331
Cdd:COG3883 114 FSDFLDRLSALSKIADADADL--LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191
|
170 180 190
....*....|....*....|....*....|....*..
gi 42409519 332 ARYGAQLSHIQGVISSIEVQLSNVRADTERQNQEYQQ 368
Cdd:COG3883 192 AAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
181-316 |
5.55e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 38.89 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 181 SVEADINGLRRVLDELTlartDLEMQIENLKEELAYLKKNHEEEISALRsqvggqvsvevdstpgiDLAKILSEMRSQYE 260
Cdd:pfam05911 675 SNDLKTEENKRLKEEFE----QLKSEKENLEVELASCTENLESTKSQLQ-----------------ESEQLIAELRSELA 733
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 42409519 261 AMAEKNRKdAEawylTQIDELNTQVAVHTTQIQINKTEVTELRRKVQDLEIELQSQ 316
Cdd:pfam05911 734 SLKESNSL-AE----TQLKCMAESYEDLETRLTELEAELNELRQKFEALEVELEEE 784
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
159-392 |
8.20e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.36 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 159 DNARLAADDFRTKF--ETEQALRMSVEA----DINGLRRVLDELTLARTDLEMQIENLKEELAYLKKNHEEeISALRSQV 232
Cdd:COG4913 173 DSFSAYLARLRRRLgiGSEKALRLLHKTqsfkPIGDLDDFVREYMLEEPDTFEAADALVEHFDDLERAHEA-LEDAREQI 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 233 ggqvsvevdstpgidlaKILSEMRSQYEAMAEKNRKDAEAWYL-----------------TQIDELNTQVAVHTTQIQIN 295
Cdd:COG4913 252 -----------------ELLEPIRELAERYAAARERLAELEYLraalrlwfaqrrlelleAELEELRAELARLEAELERL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42409519 296 KTEVTELRRKVQDLEIEL-QSQLSMKAALEGTVAEIEARYG---AQLSHIQGVISSIEVQLSNVRADTERQNQEYQQLMD 371
Cdd:COG4913 315 EARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEereRRRARLEALLAALGLPLPASAEEFAALRAEAAALLE 394
|
250 260
....*....|....*....|.
gi 42409519 372 IKSRLEQEIATYRSLLEGQEA 392
Cdd:COG4913 395 ALEEELEALEEALAEAEAALR 415
|
|
| |
