|
Name |
Accession |
Description |
Interval |
E-value |
| YydB |
COG5293 |
Uncharacterized conserved protein YydD, contains DUF2326 domain [Function unknown]; |
1-539 |
2.56e-112 |
|
Uncharacterized conserved protein YydD, contains DUF2326 domain [Function unknown];
Pssm-ID: 444096 [Multi-domain] Cd Length: 572 Bit Score: 345.39 E-value: 2.56e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 1 MLTEIRSEKfaPEHQTIRFNSGLNTVLG-------SAGGSNAIGKSTFLWIIDYAFGGESYYSLSDDIKKEIGPHTIYFT 73
Cdd:COG5293 2 MLKKLYSNL--PRFKPIEFNPGLNVILGeisspenDKDSTNGVGKSTLLELIDFCLGADKDKKRFLKHEDELGDHTFFLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 74 HQFEEQPHYFYRSTDNPKNVYRCDKDHHFI-AKLTLDEFRSFLFQEYkVGLPA---LTFPEITERYFRIYGREntlEKYP 149
Cdd:COG5293 80 FELDGKDLTIRRSVSDPKKISLCGDGYEWDhEKVSLEEAKALLEELL-FGLPAlkgPSFRSLLGYFLRRQGDD---FKDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 150 L-LVKPREQDEKAVDFLMKLFGHHNILAAIKSMEEELGVKFSQLKSRQRQQVD---IEKIEMNRKTIESLKKRLQKLMKN 225
Cdd:COG5293 156 LqLFSTAQKDADWKLYLAYLLGLDWDLAAEKYELKEEIKELKKLRKALKDELIgsvVKSISELRAEILELEEEIEKLEKD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 226 SEEAQLAMfgFDTQTFERITVAQKELNSFIRKRNRLQSQLNAIESNIADSNP----ETASEFDSLVHFFPNTDIKAFEEI 301
Cdd:COG5293 236 LEKFDVAE--NYEELEKELDELKREINELRNERYSLERRLKKIERSLEEEIDidpdELEKLYEEAGVFFPDQVKKRFEEV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 302 EHFHKKIREILSEEMAQEIERLQPLIEHCDKEIKRLHQKIEESGLAKEmSERVLSQCVNVSKSIDRLEEETAELIHQ--- 378
Cdd:COG5293 314 EAFHKSIVENRREYLEEEIAELEAELEELEAELAELGKERAELLSLLD-SKGALDKYKELQEELAELEAELEELESRlek 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 379 -KELQEARAEAEHRLAEL---LQQQTEKLEEIQDAINMRMELINGVVTEqqETAPLLQITPQK----DIFFGTPGNTSEG 450
Cdd:COG5293 393 lQELEDEIRELKEERAELkeeIESDIEERKELLDEINKLFSEIVEELYG--NRKASLSIEVNKqghlDFDAEIPTDGSTG 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 451 TAFKSLVIYDLSVL----ELRPIPALIHDSNILKRIEDIHLEHILERYMDSGR----QIFIAFDKADSTTA--KAHEILE 520
Cdd:COG5293 471 INYMKIFCFDLALLlahlNGRFPGFLVHDSHLFDGVDDRQKANLLNLIAEVAReggfQYIVTLNSDDLPKAddEGFDFLD 550
|
570 580
....*....|....*....|..
gi 501240897 521 TTAVLRLSD---GNELFGRSWS 539
Cdd:COG5293 551 KEIVLRLTDegeSGRLFGFRFW 572
|
|
| DUF2326 |
pfam10088 |
Uncharacterized protein conserved in bacteria (DUF2326); This domain, found in various ... |
424-538 |
5.73e-08 |
|
Uncharacterized protein conserved in bacteria (DUF2326); This domain, found in various hypothetical bacterial proteins, has no known function.
Pssm-ID: 431043 Cd Length: 139 Bit Score: 51.97 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 424 QQETAPLLQITPQK----DIFFGTPGNTSEGTAFKSLVIYDLSVLEL-----RPIPALIHDSNILKRIEDIHLEHILERY 494
Cdd:pfam10088 5 DEKLPAYLDIEINNngrlEFTAEIPTDRSTGINYMKIFCFDLALLLAahengTGPDFLVHDSHLFEGVDPRQVAKLLELI 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 501240897 495 M----DSGRQIFIAFDKADST---------TAKAHEILEttavLRLSDG--NELFGRSW 538
Cdd:pfam10088 85 AeyaeELGFQYIVTINKDDLPreeegpfdfDFDDNVVLE----LSLTDEgdGKLFGIRF 139
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
196-435 |
4.43e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 196 QRQQVDiEKIEMNRKTIESLKKRLQKLMKNSEEAQLAMFGF------------DTQTFERITVAQKELNSFIRKRNRLQS 263
Cdd:COG3206 162 LEQNLE-LRREEARKALEFLEEQLPELRKELEEAEAALEEFrqknglvdlseeAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 264 QLNAIESNIADSNPETASEFDSlvhffpntdikafEEIEHFHKKIREiLSEEMAQEIERLQPliEHcdKEIKRLHQKIEE 343
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQS-------------PVIQQLRAQLAE-LEAELAELSARYTP--NH--PDVIALRAQIAA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 344 sgLAKEMSERVLSQCVNVSKSIDRLEEETAELIHQKELQEARA----EAEHRLAElLQQQTEKLEEIQDAINMRMELINg 419
Cdd:COG3206 303 --LRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLaelpELEAELRR-LEREVEVARELYESLLQRLEEAR- 378
|
250
....*....|....*.
gi 501240897 420 vVTEQQETAPLLQITP 435
Cdd:COG3206 379 -LAEALTVGNVRVIDP 393
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
182-411 |
5.19e-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: 52.75 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 182 EEELGVkfSQLKSRQRQ-QVDIEKIEMNRKTIE----SLKKRLQKLMKNSEEAQLAMFGFDTQTFERITVAQKELNSFIR 256
Cdd:TIGR02168 162 EEAAGI--SKYKERRKEtERKLERTRENLDRLEdilnELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 257 KRNRLQSQLNAIESNIADSNPEtASEFDSLVhffpNTDIKAFEEIEhfhKKIREILSE--EMAQEIERLQPLIEHCDKEI 334
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAE-LQELEEKL----EELRLEVSELE---EEIEELQKElyALANEISRLEQQKQILRERL 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501240897 335 KRLHQKIEEsglAKEMSERVLSQCVNVSKSIDRLEEETAELihQKELQEARAEAEhRLAELLQQQTEKLEEIQDAIN 411
Cdd:TIGR02168 312 ANLERQLEE---LEAQLEELESKLDELAEELAELEEKLEEL--KEELESLEAELE-ELEAELEELESRLEELEEQLE 382
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
178-438 |
1.45e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 178 IKSMEEELGVKFSQLkSRQRQQVDIEKIEMNR--KTIESLKKRLQKLmkNSEEAQLAmfGFDTQTFERITVAQKELNSFI 255
Cdd:TIGR02169 683 LEGLKRELSSLQSEL-RRIENRLDELSQELSDasRKIGEIEKEIEQL--EQEEEKLK--ERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 256 RKRNRLQSQLNAIESNIADSNPETASEFDSLVHFFPNTDIKAFEEIEHFHKKIREILS-------------EEMAQEIER 322
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLReieqklnrltlekEYLEKEIQE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 323 LQPLIEHCDKEIKRLHQKIEESGLAKEMSERVL-----------SQCVNVSKSIDRLEEETAELihQKELQEARAEAEhR 391
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELeeleaalrdleSRLGDLKKERDELEAQLREL--ERKIEELEAQIE-K 914
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 501240897 392 LAELLQQQTEKLEEIQDAINMRMELINGVVTEQQETAPLLQITPQKD 438
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQ 961
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
209-432 |
1.10e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 209 RKTIESLKK------RLQKLMKNSEEAQLAMFGFDTQTFE-RITVAQKELNSFIRKRNRLQSQLNAIESNIAdsnpETAS 281
Cdd:COG1196 199 ERQLEPLERqaekaeRYRELKEELKELEAELLLLKLRELEaELEELEAELEELEAELEELEAELAELEAELE----ELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 282 EFDSLVhffpntdikafEEIEHFHKKIREILseemaQEIERLQPLIEHCDKEIKRLHQKIEESGLAKEMSERVLSQcvnV 361
Cdd:COG1196 275 ELEELE-----------LELEEAQAEEYELL-----AELARLEQDIARLEERRRELEERLEELEEELAELEEELEE---L 335
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501240897 362 SKSIDRLEEETAEL-IHQKELQEARAEAEHRLAELLQQQTEKLEEIQDAINMRMELINGVVTEQQETAPLLQ 432
Cdd:COG1196 336 EEELEELEEELEEAeEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
173-408 |
6.23e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 173 NILAAIKSMEEElgvkFSQLKS------RQRQQVDI-EKIEMNRKTIESLKKRLQKLmknseEAQLAMFgfdtqtfeRIT 245
Cdd:COG4913 222 DTFEAADALVEH----FDDLERahealeDAREQIELlEPIRELAERYAAARERLAEL-----EYLRAAL--------RLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 246 VAQKELNSFIRKRNRLQSQLNAIESNIAdsnpETASEFDslvhffpntdiKAFEEIEHFHKKIREI---LSEEMAQEIER 322
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELE----RLEARLD-----------ALREELDELEAQIRGNggdRLEQLEREIER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 323 LQPLIEHCDKEIKRLHQKIEESGLAKEMSERVLSQcvNVSKSIDRLEEETAElihQKELQEARAEAEHRLAELLQQQTEK 402
Cdd:COG4913 350 LERELEERERRRARLEALLAALGLPLPASAEEFAA--LRAEAAALLEALEEE---LEALEEALAEAEAALRDLRRELREL 424
|
....*.
gi 501240897 403 LEEIQD 408
Cdd:COG4913 425 EAEIAS 430
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
189-439 |
8.83e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 189 FSQLKSRQRQQVDIEKIemnRKTIESLKKRLQKLMKNSEEAQLAMFGFDTQ----------TFERITVAQKELNSFIRKR 258
Cdd:COG4942 16 AAQADAAAEAEAELEQL---QQEIAELEKELAALKKEEKALLKQLAALERRiaalarriraLEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 259 NRLQSQLNAIESNIADSNPE--TASEFDSLVHFFPNTDIKAFEEIEHFHKKIreilSEEMAQEIERLQpliehcdKEIKR 336
Cdd:COG4942 93 AELRAELEAQKEELAELLRAlyRLGRQPPLALLLSPEDFLDAVRRLQYLKYL----APARREQAEELR-------ADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 337 LHQKIEEsgLAKEMSErvlsqcvnVSKSIDRLEEEtaelihQKELQEARAEAEHRLAELLQQQTEKLEEIQDAINMRMEL 416
Cdd:COG4942 162 LAALRAE--LEAERAE--------LEALLAELEEE------RAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
250 260
....*....|....*....|...
gi 501240897 417 INGVVTEQQETAPLLQITPQKDI 439
Cdd:COG4942 226 EALIARLEAEAAAAAERTPAAGF 248
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
299-431 |
1.09e-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: 43.76 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 299 EEIEHFHKKIREILSE--EMAQEIERLQPLIEHCDKEIKRLHQKIEESGLAKEMsERVLSQCVNVSKSIDRLEEETAELI 376
Cdd:COG1579 38 DELAALEARLEAAKTEleDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEY-EALQKEIESLKRRISDLEDEILELM 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 501240897 377 HQKE-LQEARAEAEHRLAELLQQQTEKLEEIQDAINMRMELINGVVTEQQETAPLL 431
Cdd:COG1579 117 ERIEeLEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
203-416 |
2.89e-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: 43.89 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 203 EKIEMNRKTIESLKKRLQKLMKNSEEAQLAMFGFDTQTFE---RITVAQKELNSFIRKRNRLQSQLNAIESNIADSNPET 279
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 280 ASEFDSLvhffpntdIKAFEEIEHFHKKIREiLSEEMAQEIERLQPLIEHCDKEIKRLHQKIEESGLAKEMSERVLSQCV 359
Cdd:TIGR02168 764 EELEERL--------EEAEEELAEAEAEIEE-LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 501240897 360 NVSKSIDRLEEETaelihqKELQEARAEAEHRLAELlQQQTEKLE-EIQDAINMRMEL 416
Cdd:TIGR02168 835 ATERRLEDLEEQI------EELSEDIESLAAEIEEL-EELIEELEsELEALLNERASL 885
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
214-413 |
6.72e-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: 42.75 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 214 SLKKRLQKLMKNSEEAQLAMFGfdtqtfERITVAQKELNSFIRKRNRLQSQLNAIESNIADSNPETAsefdslvhffpnT 293
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLR------ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG------------E 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 294 DIKAFEEIEHFHKKIREILSEEMA------QEIERLQPLIEHCDKEIKRLHQKIEESGLAKEMSERVL--SQCVNVSKSI 365
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEELEEdlssleQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshSRIPEIQAEL 800
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 501240897 366 DRLEEETAELIHQKELQEARAEAEHRLAELLQQQTEKLEEIQDAINMR 413
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
239-428 |
6.88e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 239 QTFERITVAQKELNSFIRKRNRLQSQLNAIESNIADSNpetaSEFDSLvhffpNTDI-KAFEEIEHFHKKIREILS---- 313
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ----AEIDKL-----QAEIaEAEAEIEERREELGERARalyr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 314 -----------------EEMAQEIERLQPLIEHCDKEIKRLHQKIEEsgLAKEMSErvlsqcvnVSKSIDRLEEETAELI 376
Cdd:COG3883 98 sggsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAE--LEAKKAE--------LEAKLAELEALKAELE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 501240897 377 -HQKELQEARAEAEHRLAELLQQQTEKLEEIQDAINMRMELINGVVTEQQETA 428
Cdd:COG3883 168 aAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
189-418 |
1.30e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 189 FSQLKSRQRQQVDIEKIEmnrKTIESLKKRLQKLMKNSEE-AQLAmfgfdtqtfERITVAQKELNSFIRKRNRLQSQLNA 267
Cdd:COG4913 650 LQRLAEYSWDEIDVASAE---REIAELEAELERLDASSDDlAALE---------EQLEELEAELEELEEELDELKGEIGR 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 268 IESNIADSNPETASEFDSLVHFfpnTDIKAFEEIEHFHKKIREILSEEMAQEI-ERLQPLIEHCDKEIKRLHQKIEEsgL 346
Cdd:COG4913 718 LEKELEQAEEELDELQDRLEAA---EDLARLELRALLEERFAAALGDAVERELrENLEERIDALRARLNRAEEELER--A 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 347 AKEMSERVLSQCVNVSKSIDRLEEETAELihqKELQEAR-AEAEHRLAELLQQQTEK-----LEEIQDAINM---RMELI 417
Cdd:COG4913 793 MRAFNREWPAETADLDADLESLPEYLALL---DRLEEDGlPEYEERFKELLNENSIEfvadlLSKLRRAIREikeRIDPL 869
|
.
gi 501240897 418 N 418
Cdd:COG4913 870 N 870
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
277-410 |
1.38e-03 |
|
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: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 277 PETASEFDSLVHFFpntdikafEEIEHFHKKIreilsEEMAQEIERLQPLIEHCDkEIKRLHQKIEE-----SGLAKEMS 351
Cdd:COG4913 221 PDTFEAADALVEHF--------DDLERAHEAL-----EDAREQIELLEPIRELAE-RYAAARERLAEleylrAALRLWFA 286
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501240897 352 ERVLSQCVNVsksIDRLEEETAEL-----IHQKELQEARAEAEHRLAELLQQQTEKLEEIQDAI 410
Cdd:COG4913 287 QRRLELLEAE---LEELRAELARLeaeleRLEARLDALREELDELEAQIRGNGGDRLEQLEREI 347
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
242-428 |
1.42e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 242 ERITVAQKELNSFIRKRNRLQSQLNAIESNIADSNpetasefdslvhffpntdikafEEIEHFHKKIreilsEEMAQEIE 321
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQ----------------------AELEALQAEI-----DKLQAEIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 322 RLQPLIEHCDKEIKRLHQKIEESGLAKEMSERVLSqcvnvSKS----------IDRLEEETAELIH-----QKELQEARA 386
Cdd:COG3883 76 EAEAEIEERREELGERARALYRSGGSVSYLDVLLG-----SESfsdfldrlsaLSKIADADADLLEelkadKAELEAKKA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 501240897 387 EAEHRLAELLQQQTE---KLEEIQDAINMRMELINGVVTEQQETA 428
Cdd:COG3883 151 ELEAKLAELEALKAEleaAKAELEAQQAEQEALLAQLSAEEAAAE 195
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
198-410 |
1.48e-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: 40.29 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 198 QQVDIEkIEMNRKTIESLKKRLQKLMKNSEEAQlamfgfdtqtfERITVAQKELNSFIRKRNRLQSQLNAIESNIADS-- 275
Cdd:COG1579 13 QELDSE-LDRLEHRLKELPAELAELEDELAALE-----------ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYee 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 276 ---NPETASEFDSLVHffpntdikafeEIEHFHKKIREIlsEEmaqEIERLQPLIEHCDKEIKRLHQKIEEsglakemse 352
Cdd:COG1579 81 qlgNVRNNKEYEALQK-----------EIESLKRRISDL--ED---EILELMERIEELEEELAELEAELAE--------- 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 501240897 353 rvlsqcvnvsksidrLEEETAELihQKELQEARAEAEHRLAELLQQQTEKLEEIQDAI 410
Cdd:COG1579 136 ---------------LEAELEEK--KAELDEELAELEAELEELEAEREELAAKIPPEL 176
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
171-411 |
1.65e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 41.17 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 171 HHNILAAIKSMEEELGVKfsqlkSRQRQQVDIEKIEMNRKTIES-LKKRLQKLMKNSEEAQLAMfGFDTQTFeritvaQK 249
Cdd:pfam05667 212 NAAELAAAQEWEEEWNSQ-----GLASRLTPEEYRKRKRTKLLKrIAEQLRSAALAGTEATSGA-SRSAQDL------AE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 250 ELNSFIrkrnrlqsqlnaiESNIADSNPETASEFDSLVHFFPNTDIKAFEEIEHFHKKIREILSEEMAQEIERLQplieh 329
Cdd:pfam05667 280 LLSSFS-------------GSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQREEELEELQ----- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 330 cdKEIKRLHQKIEEsgLAKEMServlsqcvNVSKSIDRLEEETAELIHQKELQEARAEAEHRLAELLQQQTEKLEEIQDA 409
Cdd:pfam05667 342 --EQLEDLESSIQE--LEKEIK--------KLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLPDAEENIAKLQAL 409
|
..
gi 501240897 410 IN 411
Cdd:pfam05667 410 VD 411
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
173-438 |
2.30e-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: 40.98 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 173 NILAAIKSMEEElgvkfSQLKSR-QRQQVD------------------IEKIEMNRKTIESLKKRLQKLMKNSEEAQLam 233
Cdd:pfam12128 200 SMIVAILEDDGV-----VPPKSRlNRQQVEhwirdiqaiagimkirpeFTKLQQEFNTLESAELRLSHLHFGYKSDET-- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 234 fgfdtqtfeRITVAQKElnsFIRKRNRLQSQLNAIESNIADSNPETASEFDSLvhffpNTDIKAFEE----IEHFHKKIR 309
Cdd:pfam12128 273 ---------LIASRQEE---RQETSAELNQLLRTLDDQWKEKRDELNGELSAA-----DAAVAKDRSeleaLEDQHGAFL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 310 EILSEEMAQEIERL---QPLIEHCDKEIKRL---HQKIEESGLAKEMseRVLSQCVNVsksIDRLEEETAELIHQKELQE 383
Cdd:pfam12128 336 DADIETAAADQEQLpswQSELENLEERLKALtgkHQDVTAKYNRRRS--KIKEQNNRD---IAGIKDKLAKIREARDRQL 410
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 384 ARAEA-----EHRLAELLQQQTEKLEEIQDAINMRMELINGVVTEQQETAPLLQITPQKD 438
Cdd:pfam12128 411 AVAEDdlqalESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFD 470
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
244-432 |
2.51e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 244 ITVAQKELNSFIRKRNRLQSQLNAIESNIAdsnpETASEFDSLvhffpNTDIKAFEEiehfhkkirEIlsEEMAQEIERL 323
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELE----ELNEEYNEL-----QAELEALQA---------EI--DKLQAEIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 324 QPLIEHCDKEIKRLHQKIEESGLAKEMSERVL---------SQCVNVSK-------SIDRLEEETAELIHQK-------- 379
Cdd:COG3883 78 EAEIEERREELGERARALYRSGGSVSYLDVLLgsesfsdflDRLSALSKiadadadLLEELKADKAELEAKKaeleakla 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 501240897 380 ELQEARAEAEHRLAELLQQQTEK------LEEIQDAINMRMELINGVVTEQQETAPLLQ 432
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQeallaqLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
176-417 |
3.98e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.05 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 176 AAIKSMEEELGVKFSQLKSRQRQQVDIE-KIEMNRKTIESLKKRLQKLMKNSEEAQLAMFGFDtqtferitvaqKELNSF 254
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKeQIKSIEKEIENLNGKKEELEEELEELEAALRDLE-----------SRLGDL 887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 255 IRKRNRLQSQLNAIESNIADSNpETASEFDSLVHFFPNTDIKAFEEIEHFHKKIREIlseemaQEIERLQPLIEHCDKEI 334
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELE-AQIEKKRKRLSELKAKLEALEEELSEIEDPKGED------EEIPEEELSLEDVQAEL 960
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 335 KRLHQKIEESG----LAKEMSERVLsqcvnvsKSIDRLEEEtaelihQKELQEARAEAEHRLAELLQQQTEKLEEIQDAI 410
Cdd:TIGR02169 961 QRVEEEIRALEpvnmLAIQEYEEVL-------KRLDELKEK------RAKLEEERKAILERIEEYEKKKREVFMEAFEAI 1027
|
....*..
gi 501240897 411 NMRMELI 417
Cdd:TIGR02169 1028 NENFNEI 1034
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
169-383 |
4.29e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.84 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 169 FGHHNILAAIKSMEEELGVKFSQLKsrqrqQVDIEKIEMNRKTIES-------------------------LKKRLQKLM 223
Cdd:pfam06160 230 LEHLNVDKEIQQLEEQLEENLALLE-----NLELDEAEEALEEIEEridqlydllekevdakkyveknlpeIEDYLEHAE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 224 KNSEEAQLAM------FGFDTQTFERITVAQKELNSFIRKRNR--------------LQSQLNAIESNIADSNPETASEF 283
Cdd:pfam06160 305 EQNKELKEELervqqsYTLNENELERVRGLEKQLEELEKRYDEiverleekevayseLQEELEEILEQLEEIEEEQEEFK 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 284 DSLVHFfPNTDIKAFEEIEHFHKKIREILSEEMAQEI----ERLQPLIEHCDKEIKRLHQKIEESGLakEMsERVLSQCV 359
Cdd:pfam06160 385 ESLQSL-RKDELEAREKLDEFKLELREIKRLVEKSNLpglpESYLDYFFDVSDEIEDLADELNEVPL--NM-DEVNRLLD 460
|
250 260
....*....|....*....|....
gi 501240897 360 NVSKSIDRLEEETAELIHQKELQE 383
Cdd:pfam06160 461 EAQDDVDTLYEKTEELIDNATLAE 484
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
209-411 |
5.65e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 209 RKTIESLKKRLQKLMKNSEEAQlamfgfdtqtfERITVAQKELNSFIRKRNRLQSQLnaiesniadsnPETASEFDSLVH 288
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIE-----------ELIKEKEKELEEVLREINEISSEL-----------PELREELEKLEK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 289 FFPNTDiKAFEEIEHFHKKIREILSEEMAQE--IERLQPLIEHCDKEIKRLHQKIEES----GLAKEMS------ERVLS 356
Cdd:PRK03918 229 EVKELE-ELKEEIEELEKELESLEGSKRKLEekIRELEERIEELKKEIEELEEKVKELkelkEKAEEYIklsefyEEYLD 307
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 501240897 357 QCVNVSKSIDRLEEETAELihQKELQEArAEAEHRLAELlqqqTEKLEEIQDAIN 411
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGI--EERIKEL-EEKEERLEEL----KKKLKELEKRLE 355
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
296-426 |
7.45e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 296 KAFEEIEHFHKKIREIlsEEMAQEIERLQPLIEHCDKEIKRLHQKIEESGLAKEMS--ERVLSQCVNVSKSIDRLEEETA 373
Cdd:COG4717 82 EAEEKEEEYAELQEEL--EELEEELEELEAELEELREELEKLEKLLQLLPLYQELEalEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501240897 374 ELIHQ-KELQEARAEAEHRLAEL-----------LQQQTEKLEEIQDAINMRMELINGVVTEQQE 426
Cdd:COG4717 160 ELEEElEELEAELAELQEELEELleqlslateeeLQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
|
| Dynamin_M |
pfam01031 |
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ... |
307-418 |
9.84e-03 |
|
Dynamin central region; This is the stalk region which lies between the GTPase domain, see pfam00350, and the pleckstrin homology (PH) domain, see pfam00169. This region dimerizes in a cross-like fashion forming a dynamin dimer in which the two G-domains are oriented in opposite directions.
Pssm-ID: 460033 Cd Length: 287 Bit Score: 38.27 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501240897 307 KIREILSEEMAQEIERLQPLIEHCDKEIK---RLHQKIEESGLAKEMSERVLsqcvnVSKSIDRLEE---ETAELIHQkE 380
Cdd:pfam01031 146 RIRYIFNEIFPKSLEKIDPLENLSDEEIRtaiRNSRGIRLPLFVPEKAFELL-----VKQQIKRLEEpalKCVELVYE-E 219
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 501240897 381 LQEA--------------RAEAEHRLAELLQQQTEKLEE-IQDAINMRMELIN 418
Cdd:pfam01031 220 LERIihkctpelkrfpnlRERIKEVVEDLLRERLEPTEKmIRSLIEMELAYIN 272
|
|
| |
