|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
64-289 |
1.15e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 64 EDIIQQRLQSVVHQREELQRLEMELRAQVIAHPQIIEAQRSFEAAAKEhvtAAAKLKEQLHEREKYILELEMKLDDKDRE 143
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE---ELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 144 LDALKIDHQtvwANQDLLREQTKELATFRRERDNSEAERAQHLKQIHDLQEHLREKESQMLALEEQHRAAQDNIIYKDEQ 223
Cdd:COG1196 381 LEELAEELL---EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002291472 224 LREAHAWMARVQEMDTLQSQTMQAELRDRTEQFNQYWIsfQQQYVEMQRGFLHTIQQLQLELNELR 289
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLL--LLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
78-313 |
2.54e-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: 61.23 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 78 REELQRLEMELRAQVI--AHPQIIEAQRSFEAAAKEHVTAAAKLK---EQLHEREKYILELEMKLDDKDRELDALKIDHQ 152
Cdd:TIGR02168 219 KAELRELELALLVLRLeeLREELEELQEELKEAEEELEELTAELQeleEKLEELRLEVSELEEEIEELQKELYALANEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 153 TVwanqdllrEQTKELATFRRERDNS-----EAERAQHLKQIHDLQEHLREKESQMLALEEQHRAAQDNIIYKDEQLREA 227
Cdd:TIGR02168 299 RL--------EQQKQILRERLANLERqleelEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 228 HAWMARVQEmdtlQSQTMQAELRDRTEQFNQywISFQQQYVEMQrgflhtIQQLQLELNELRDRTGAPKDGSQTAQESSA 307
Cdd:TIGR02168 371 ESRLEELEE----QLETLRSKVAQLELQIAS--LNNEIERLEAR------LERLEDRRERLQQEIEELLKKLEEAELKEL 438
|
....*.
gi 1002291472 308 ESTLGQ 313
Cdd:TIGR02168 439 QAELEE 444
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
67-230 |
6.31e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 67 IQQRLQSVVHQREELQRLEMELRAQVIAHPQIIEAQRSFE--AAAKEHVTAAAKLKEQLHEREKYILELEMKLDDKDREL 144
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQelEALEAELAELPERLEELEERLEELRELEEELEELEAEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 145 DALKIDHQTvwANQDLLREQTKELATFRRERDNSEAERAQHLKQIHDLQEHLREKESQMLALEEQHRAAQDNiiykdEQL 224
Cdd:COG4717 173 AELQEELEE--LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-----ERL 245
|
....*.
gi 1002291472 225 REAHAW 230
Cdd:COG4717 246 KEARLL 251
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
67-298 |
1.42e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 67 IQQRLQSVVHQREELQRLEMELRAQVIAHPQIIEAQRSFEAAAKEhvtAAAKLKEQLHEREKYILELEMKLDDKDRELDA 146
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE---RLEELEEELAELEEELEELEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 147 LKIDHQTVWANQDLLREQTKE-----------LATFRRERDNSEAERAQHLKQIHDLQEHLREKESQMLALEEQHRAAQD 215
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEaeaelaeaeeeLEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 216 NIIYKDEQLREAHAWMARVQEMDTLQSQTMQAELRDRTEQFNQYwISFQQQYVEMQRGFLHTIQQLQLELNELRDRTGAP 295
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA-ALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
...
gi 1002291472 296 KDG 298
Cdd:COG1196 508 EGV 510
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
76-291 |
6.43e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 76 HQREELQRLEMELRAQVIAHPQIIEAQRSFEAAAKEHVTAAAKLKEQLHEREKYILELEMKLDDKDRELDALKIDHQtvw 155
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR--- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 156 ANQDLLREQTKELATFRRERDNSEAERAQHLKQIHDLQEHLREKESQMLALEEQHRAAQDNIIYKDEQLREahawmARVQ 235
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE-----LAEE 387
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002291472 236 EMDTLQSQTMQAELRDRTEQFNQYWISFQQQYVEMQRGFLHTIQQLQLELNELRDR 291
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
78-260 |
1.46e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 78 REELQRLEMELRAqviAHPQIIEAQRSFEAAAKEHvTAAAKLkEQLHEREKYILELEMKLDDKDRELDALKIDHQTVWAN 157
Cdd:COG4913 616 EAELAELEEELAE---AEERLEALEAELDALQERR-EALQRL-AEYSWDEIDVASAEREIAELEAELERLDASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 158 QDLLREQTKELATFRRERDNSEAERAQHLKQIHDLQEHLREKESQMLALEEQHRAAQdnIIYKDEQLREAHAWMARVQEM 237
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL--RALLEERFAAALGDAVERELR 768
|
170 180 190
....*....|....*....|....*....|..
gi 1002291472 238 DTLQSQTMQA---------ELRDRTEQFNQYW 260
Cdd:COG4913 769 ENLEERIDALrarlnraeeELERAMRAFNREW 800
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
62-308 |
2.46e-07 |
|
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: 54.69 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 62 LSEDI--IQQRLQSVVHQREELQRLEMELRAQV-IAHPQIIEAQRSFEAAAKEHvtaaAKLKEQLHEREKYILELEMKLD 138
Cdd:TIGR02169 679 LRERLegLKRELSSLQSELRRIENRLDELSQELsDASRKIGEIEKEIEQLEQEE----EKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 139 DKDRELDAL--KIDHQTVWANQ----------DLLREQTKELatfRRERDNSEAERAQHLKQIHDLQEHLREKESQMLAL 206
Cdd:TIGR02169 755 NVKSELKELeaRIEELEEDLHKleealndleaRLSHSRIPEI---QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 207 EEQHRAAQDNIIYKDEQL----REAHAWMARVQEMDTL--QSQTMQAELRDRTEQFNQYWISFQQQYVEMQRGflhtIQQ 280
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIksieKEIENLNGKKEELEEEleELEAALRDLESRLGDLKKERDELEAQLRELERK----IEE 907
|
250 260
....*....|....*....|....*...
gi 1002291472 281 LQLELNELRDRTGAPKDGSQTAQESSAE 308
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSE 935
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
79-263 |
3.23e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 79 EELQRLEMELRAQVIAHPQIIEAQRSFEAAAKEHVTAAAKLKEQLHEREKY------------ILELEMKLDDKDRELDA 146
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekllqllplyqeLEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 147 lkidhqtvwanqdlLREQTKELATFRRERDNSEAERAQHLKQIHDLQEHLR-EKESQMLALEEQHRAAQDNIIYKDEQLR 225
Cdd:COG4717 151 --------------LEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELE 216
|
170 180 190
....*....|....*....|....*....|....*....
gi 1002291472 226 EAHAWMARV-QEMDTLQSQTMQAELRDRTEQFNQYWISF 263
Cdd:COG4717 217 EAQEELEELeEELEQLENELEAAALEERLKEARLLLLIA 255
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
64-254 |
4.46e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.59 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 64 EDIIQQRLQSVVHQREELQRLEMELRAQVIAHPQIIEAQRSFEAAAKEHvtaAAKLKEQLHEREKYILE------LEMKL 137
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEER---QRKIQQQKVEMEQIRAEqeearqREVRR 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 138 --DDKDRELDALKIDHQTVWANQDLLREQT-----KELATFRRERDNSEAERAQHL---KQIHDLQEHLREKESQMLALE 207
Cdd:pfam17380 440 leEERAREMERVRLEEQERQQQVERLRQQEeerkrKKLELEKEKRDRKRAEEQRRKileKELEERKQAMIEEERKRKLLE 519
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1002291472 208 EQHRAAQdNIIYKDEQLREAHAWMARVQEMDT---LQSQTMQA-ELRDRTE 254
Cdd:pfam17380 520 KEMEERQ-KAIYEEERRREAEEERRKQQEMEErrrIQEQMRKAtEERSRLE 569
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
64-259 |
5.20e-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: 53.52 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 64 EDIIQQRLQSVVHQREELQRLEMELRAQVIAHPQIIEAQRSFEAAAKEHVTAAAKLKEQLHEREKYILELEMKLDDKDRE 143
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 144 LDALKIDHQtvwANQDLLREQTKELATFRRERDNSEAERAQHLKQIHDLQEHLREKESQMLALEEQHRAAQDNIIYKDEQ 223
Cdd:TIGR02168 868 IEELESELE---ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
170 180 190
....*....|....*....|....*....|....*.
gi 1002291472 224 LREAHAWMARVQEMDTLQSQTMQAELRDRTEQFNQY 259
Cdd:TIGR02168 945 LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
64-291 |
6.65e-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: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 64 EDIIQQRLQSVVHQREELQRLEMElrAQVIAHPQIIEAQRSFEAAAKEhvtaaAKLKEQLHEREKYILELEMKLDDKDRE 143
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAE--VEQLEERIAQLSKELTELEAEI-----EELEERLEEAEEELAEAEAEIEELEAQ 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 144 LDALKIDHQTVWANQDLLREQTKEL----ATFRRERDNSEAERAQHLKQIHDLQEHLREKESQMLALEEQHRAAQDNIIY 219
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELTLLneeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002291472 220 KDEQLREAHAWMARVQE-MDTLQS--QTMQAELRD---RTEQFNQYWISFQQQYVEMQRgflhTIQQLQLELNELRDR 291
Cdd:TIGR02168 871 LESELEALLNERASLEEaLALLRSelEELSEELRElesKRSELRRELEELREKLAQLEL----RLEGLEVRIDNLQER 944
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
80-236 |
8.29e-07 |
|
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: 51.08 E-value: 8.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 80 ELQRLEMELRAqviahpqiIEAQRsfeaaaKEHVTAAAKLKEQLHEREKYILELEMKLDDKDRELDALKIDHQTVWANQD 159
Cdd:COG1579 11 DLQELDSELDR--------LEHRL------KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 160 LLREQ-------------TKELATFRRERDNSEAERAQHLKQIHDLQEHLREKESQMLALEEQHRAAQDNIiykDEQLRE 226
Cdd:COG1579 77 KYEEQlgnvrnnkeyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAE 153
|
170
....*....|
gi 1002291472 227 AHAWMARVQE 236
Cdd:COG1579 154 LEAELEELEA 163
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
67-291 |
5.23e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 67 IQQRLQSVVHQREELQRlemelraqviAHPQIIEAQRSFEA--AAKEHVTAAAKLKEQLherekyilelemklddkdREL 144
Cdd:COG4913 223 TFEAADALVEHFDDLER----------AHEALEDAREQIELlePIRELAERYAAARERL------------------AEL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 145 DALKiDHQTVWANQDLLREQTKELATFRRERDNSEAERAQHLKQIHDLQEHLREKESQML--------ALEEQHRAAQDN 216
Cdd:COG4913 275 EYLR-AALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggdrleQLEREIERLERE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 217 iiyKDEQLREAHAWMARVQEMDTLQSQT------MQAELRDRTEQFNQYWISFQQQYVEM---QRGFLHTIQQLQLELNE 287
Cdd:COG4913 354 ---LEERERRRARLEALLAALGLPLPASaeefaaLRAEAAALLEALEEELEALEEALAEAeaaLRDLRRELRELEAEIAS 430
|
....
gi 1002291472 288 LRDR 291
Cdd:COG4913 431 LERR 434
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
67-258 |
1.31e-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: 48.91 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 67 IQQRLQSVVHQREELQRLEMELRAQVIAhpqiIEAQR-SFEAAAKEHVTAAAKLKEQLHEREKYILELEMKLDD--KDR- 142
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRID----LKEQIkSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDlkKERd 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 143 ----ELDALKIDHQTVWANQDLLREQTKELATFRRERDNSEAERAQHLKQ----------IHDLQEHLREKESQMLALEE 208
Cdd:TIGR02169 893 eleaQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeeelsLEDVQAELQRVEEEIRALEP 972
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002291472 209 -QHRAAQDniiYKDEQLReahawmarvqeMDTLQSQ--TMQAE---LRDRTEQFNQ 258
Cdd:TIGR02169 973 vNMLAIQE---YEEVLKR-----------LDELKEKraKLEEErkaILERIEEYEK 1014
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
136-304 |
1.37e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 136 KLDDKDRELDALKIDHQTVWANQDLLREQTKELATFRRERDNSEAERAQ---------HLKQIHDLQEHLREKESQMLAL 206
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlekllqllpLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 207 EEQHRAAQDNIIYKDEQLREAHAWMARVQEMDTLQSQTMQAELRDRTEQFNQywisFQQQYVEMQRgflhTIQQLQLELN 286
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE----LQQRLAELEE----ELEEAQEELE 223
|
170
....*....|....*...
gi 1002291472 287 ELRDRTGAPKDGSQTAQE 304
Cdd:COG4717 224 ELEEELEQLENELEAAAL 241
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
68-303 |
1.81e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.43 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 68 QQRLQSVVHQREELQRLEMELRAQVIAHPQ------IIEAQRSFEAAAKEHVTAAAKLKEQLHEREKyILELEMKLDDKD 141
Cdd:TIGR00618 259 QQLLKQLRARIEELRAQEAVLEETQERINRarkaapLAAHIKAVTQIEQQAQRIHTELQSKMRSRAK-LLMKRAAHVKQQ 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 142 RELDALKIDHQTVWANQDLLREQTKELATFRRERDNSEAERaQHLKQIHDLQEHLREKESQMLALEEQHRaaqdniiykd 221
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT-QHIHTLQQQKTTLTQKLQSLCKELDILQ---------- 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 222 eqlREAHAWMARVQEMDTLQSQTMQAElrdRTEQFNQYWISFQQQYVEMQrgfLHTIQQLQLELNELRDRTGAPKDGSQT 301
Cdd:TIGR00618 407 ---REQATIDTRTSAFRDLQGQLAHAK---KQQELQQRYAELCAAAITCT---AQCEKLEKIHLQESAQSLKEREQQLQT 477
|
..
gi 1002291472 302 AQ 303
Cdd:TIGR00618 478 KE 479
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
66-313 |
2.57e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.79 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 66 IIQQRLQSVVHQREELQRL------EMELRAQVIAHPQ-IIEAQRSFEAAAKEHVTAAAKLKEQLHEREKYILELEMKL- 137
Cdd:pfam05483 381 IITMELQKKSSELEEMTKFknnkevELEELKKILAEDEkLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLt 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 138 -------------DDKDRELDALKIDHQTVWANQDLLREQTK-----------ELATFRRERDNSEAERAQHLKQIHDLQ 193
Cdd:pfam05483 461 aiktseehylkevEDLKTELEKEKLKNIELTAHCDKLLLENKeltqeasdmtlELKKHQEDIINCKKQEERMLKQIENLE 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 194 EHLREKESQMLALEEQHRAAQDNI---IYKDEQLREAHAWMARVQEMDTLQSQTMQAELRDRTEQFNQYWISFQQQYVEM 270
Cdd:pfam05483 541 EKEMNLRDELESVREEFIQKGDEVkckLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAL 620
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002291472 271 QR----------GFLHTIQQLQLELNELRDRTGAPKDGSQTAQES---SAESTLGQ 313
Cdd:pfam05483 621 KKkgsaenkqlnAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDkkiSEEKLLEE 676
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
105-291 |
3.17e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 105 FEAAAKehvtaAAKLKEQLHEREKYILELEMKLDDKDRELDALKiDHQTVWANQDLLREQTKELATFRRERDNSEAERAQ 184
Cdd:COG4913 606 FDNRAK-----LAALEAELAELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYSWDEIDVASAEREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 185 ---------HLK-QIHDLQEHLREKESQMLALEEQHRAAQDNIIYKDEQLREAHawmARVQEMDTLQSQTMQAELRDRTE 254
Cdd:COG4913 680 ldassddlaALEeQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ---DRLEAAEDLARLELRALLEERFA 756
|
170 180 190
....*....|....*....|....*....|....*..
gi 1002291472 255 QfnqywISFQQQYVEMQRGFLHTIQQLQLELNELRDR 291
Cdd:COG4913 757 A-----ALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
78-227 |
3.25e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 78 REELQRLEMELRAQVIAHPQIIEAQRSFEAAAKEHVTAA-AKLKEQLHEREKYILELEMKLDDKDRELDALKI----DHQ 152
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLplpaSAE 380
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002291472 153 TVWANQDLLREQtkeLATFRRERDNSEAERAQHLKQIHDLQEHLREKESQMLALEEQhraaQDNIIYKDEQLREA 227
Cdd:COG4913 381 EFAALRAEAAAL---LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR----KSNIPARLLALRDA 448
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
58-255 |
4.38e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 58 GSGGLSEDIIQQRLQSVVHQREELQRLEMELRAQVIAHPQIIEAQR----SFEAAAKEHVTAAAKL-------------- 119
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRedadDLEERAEELREEAAELeseleeareavedr 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 120 KEQLHEREKYILELEMKLDDKDRELDALKIDHQTVWANQDLLREQTKEL-ATFRRERDN-SEAER--------------- 182
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELeATLRTARERvEEAEAlleagkcpecgqpve 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 183 -AQHLKQIHDLQEHLREKESQMLALEEQhRAAQDNIIYKDEQLREAHAWMARVQEM------------DTLQSQTMQAE- 248
Cdd:PRK02224 463 gSPHVETIEEDRERVEELEAELEDLEEE-VEEVEERLERAEDLVEAEDRIERLEERredleeliaerrETIEEKRERAEe 541
|
....*..
gi 1002291472 249 LRDRTEQ 255
Cdd:PRK02224 542 LRERAAE 548
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
70-291 |
5.02e-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: 46.98 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 70 RLQSVVHQ-REELQRLEMElRAQVIAHPQIIEAQRSFEAaaKEHVTAAAKLKEQLHEREKYILELEMKLDDKDRELDALK 148
Cdd:TIGR02169 188 RLDLIIDEkRQQLERLRRE-REKAERYQALLKEKREYEG--YELLKEKEALERQKEAIERQLASLEEELEKLTEEISELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 149 idhQTVWANQDLLREQTKELatfrreRDNSEAERAQHLKQIHDL-------QEHLREKESQMLALEEQHRAAQ---DNII 218
Cdd:TIGR02169 265 ---KRLEEIEQLLEELNKKI------KDLGEEEQLRVKEKIGELeaeiaslERSIAEKERELEDAEERLAKLEaeiDKLL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 219 YKDEQLREA--------HAWMARV----QEMDTLQSQTMQAELRDRTeqfnqyWISFQQQYVEMQRGFLHTIQQLQLELN 286
Cdd:TIGR02169 336 AEIEELEREieeerkrrDKLTEEYaelkEELEDLRAELEEVDKEFAE------TRDELKDYREKLEKLKREINELKRELD 409
|
....*
gi 1002291472 287 ELRDR 291
Cdd:TIGR02169 410 RLQEE 414
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
68-291 |
6.29e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 68 QQRLQSVvhqREELQRLE---MELRAQViahpQIIEAQRsfEAAAKehvtaAAKLKEQLHEREKYIL-----ELEMKLDD 139
Cdd:COG1196 178 ERKLEAT---EENLERLEdilGELERQL----EPLERQA--EKAER-----YRELKEELKELEAELLllklrELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 140 KDRELDALKIDHQTVWANQDLLrEQTKELATFRRERDNSEAERAQ-----HLKQIHDLQ---EHLREK-----------E 200
Cdd:COG1196 244 LEAELEELEAELEELEAELAEL-EAELEELRLELEELELELEEAQaeeyeLLAELARLEqdiARLEERrreleerleelE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 201 SQMLALEEQHRAAQDNIIYKDEQLREAHAWMARVQEMDTLQSQTMQAELRDRTEQFNQyWISFQQQYVEMQRG---FLHT 277
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE-LEELAEELLEALRAaaeLAAQ 401
|
250
....*....|....
gi 1002291472 278 IQQLQLELNELRDR 291
Cdd:COG1196 402 LEELEEAEEALLER 415
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
57-206 |
6.98e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 45.52 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 57 DGSGGLSEDIIQQRlQSVVHQREELQRLEMELRaQVIAHPQIIEAQRSFEA-AAKEHVTaaaKLKEQLHEREKYILELEM 135
Cdd:pfam09787 40 DSSTALTLELEELR-QERDLLREEIQKLRGQIQ-QLRTELQELEAQQQEEAeSSREQLQ---ELEEQLATERSARREAEA 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002291472 136 KLDDKDRELDALKID-HQTVWANQDLLREQTKELATFRRE---RDNSEAERAQHLKQIHDLQEHLREKESQMLAL 206
Cdd:pfam09787 115 ELERLQEELRYLEEElRRSKATLQSRIKDREAEIEKLRNQltsKSQSSSSQSELENRLHQLTETLIQKQTMLEAL 189
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
77-272 |
1.13e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.29 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 77 QREELQRLEMELRAQVIAHPQIIEAQRSFEAAAKEH---------VTAAAKLKEQLHERE-KYILELEMKLDDKD----- 141
Cdd:pfam13868 27 QIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEkeeerkeerKRYRQELEEQIEEREqKRQEEYEEKLQEREqmdei 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 142 ----------------RELDALKIDHQTVWANQDLLREQTKE--------LATFRRERDNSEAERAQHLKQIHDLQEHLR 197
Cdd:pfam13868 107 veriqeedqaeaeeklEKQRQLREEIDEFNEEQAEWKELEKEeereederILEYLKEKAEREEEREAEREEIEEEKEREI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 198 EKESQMLALEEQHRAAQDNII---YKDEQLRE----AHAWMARVQEMDTLQSQT----------MQAELRDRTEQFNQYW 260
Cdd:pfam13868 187 ARLRAQQEKAQDEKAERDELRaklYQEEQERKerqkEREEAEKKARQRQELQQAreeqielkerRLAEEAEREEEEFERM 266
|
250
....*....|..
gi 1002291472 261 ISFQQQYVEMQR 272
Cdd:pfam13868 267 LRKQAEDEEIEQ 278
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
114-226 |
1.41e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.46 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 114 TAAAKLKEQLHEREKYILELEMKLDDKDRELDALKIDHQTvwANQDLLREQTKELATFRRERDNSEA---ERAQHLKQIH 190
Cdd:COG0542 397 EAAARVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDE--ASFERLAELRDELAELEEELEALKArweAEKELIEEIQ 474
|
90 100 110
....*....|....*....|....*....|....*.
gi 1002291472 191 DLQEHLREKESQMLALEEQHRAAQDNIIYKDEQLRE 226
Cdd:COG0542 475 ELKEELEQRYGKIPELEKELAELEEELAELAPLLRE 510
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
117-304 |
1.93e-04 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 44.25 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 117 AKLKEQLHEREKYILELEMKLDDKDrelDALKIdhqtvWANQDllREQTKELATFRRERDNSEAERAQHLKQIHDLQEHL 196
Cdd:pfam04849 104 EALEEQLGSAREEILQLRHELSKKD---DLLQI-----YSNDA--EESETESSCSTPLRRNESFSSLHGCVQLDALQEKL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 197 REKESQMLAL-EEQHRAAQDNIIYKD----------EQLREAHAWMARVQE-----MDTLQSQ-----TMQAELRDRTEQ 255
Cdd:pfam04849 174 RGLEEENLKLrSEASHLKTETDTYEEkeqqlmsdcvEQLSEANQQMAELSEelarkMEENLRQqeeitSLLAQIVDLQHK 253
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1002291472 256 FNQYWISFQ--QQYVEMQRGflhTIQQLQLELNELRDRTGAPKDGSQTAQE 304
Cdd:pfam04849 254 CKELGIENEelQQHLQASKE---AQRQLTSELQELQDRYAECLGMLHEAQE 301
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
70-257 |
3.94e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 70 RLQSVVHQREELQRLEMELRAQVIAHPQIIEAQRS----FEAAAKEHVTAAAKLKEQLHEREKYILELEMKLDDKDRELD 145
Cdd:PRK02224 510 RIERLEERREDLEELIAERRETIEEKRERAEELREraaeLEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 146 ALK----IDHQTVWANQDL--LREQTKELATF---RRERDNSEAERAQHLKQIHD-------------LQEHLREKESQM 203
Cdd:PRK02224 590 SLErirtLLAAIADAEDEIerLREKREALAELndeRRERLAEKRERKRELEAEFDearieearedkerAEEYLEQVEEKL 669
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002291472 204 LALEEQHRAAQDNI------IYKDEQLREAH-AWMARVQEMDTLQS-----QTMQAELRDRTEQFN 257
Cdd:PRK02224 670 DELREERDDLQAEIgaveneLEELEELRERReALENRVEALEALYDeaeelESMYGDLRAELRQRN 735
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
73-316 |
5.00e-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: 43.21 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 73 SVVHQREELQRLEMELRAqviAHPQIIEAQRSFEAAAKEHVTAAAKLKE---QLHEREKYILELEMKLDDKDRELDALKI 149
Cdd:COG4942 14 AAAAQADAAAEAEAELEQ---LQQEIAELEKELAALKKEEKALLKQLAAlerRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 150 DHQTVWANQDLLREQTKEL--ATFRRERDNSEAE--RAQHLKQIHDLQEHLREKESQMLALEEQHRAAQDNIIYKDEQLR 225
Cdd:COG4942 91 EIAELRAELEAQKEELAELlrALYRLGRQPPLALllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 226 EAHAWMARVQEMDTLQSQTMQAELRDRTEQFNQywisFQQQYVEMQRgflhTIQQLQLELNELRDRTGAPKDGSQTAQES 305
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLAR----LEKELAELAA----ELAELQQEAEELEALIARLEAEAAAAAER 242
|
250
....*....|.
gi 1002291472 306 SAESTLGQNKG 316
Cdd:COG4942 243 TPAAGFAALKG 253
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
70-210 |
6.14e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 70 RLQSVVHQ-REELQRLEMELRAQVIAHPQIIEAQRSFEAAAKEHVTAAAKLKEQLHE--REKYiLELEMKLDDKDRELDA 146
Cdd:PRK03918 606 ELKDAEKElEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEelREEY-LELSRELAGLRAELEE 684
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002291472 147 LKIDHQTVWANQDLLREQTKELATFRRERDNSEaeraqhlKQIHDLQEhLREKESQMLALEEQH 210
Cdd:PRK03918 685 LEKRREEIKKTLEKLKEELEEREKAKKELEKLE-------KALERVEE-LREKVKKYKALLKER 740
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
65-227 |
1.08e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 65 DIIQQRLQSVvhqREELQRLEMELRAQviaHPQIIEAQRSFEAAAKEhvtaAAKLKEQLHEREKYILELEMKLDDKDREL 144
Cdd:COG4372 41 DKLQEELEQL---REELEQAREELEQL---EEELEQARSELEQLEEE----LEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 145 DALKIDHQTVWANQDLLREQTKELATFRRERDNSEAERAQHLKQIHDLQEHLREKESQmLALEEQHRAAQDNIIYKDEQL 224
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA-LEQELQALSEAEAEQALDELL 189
|
...
gi 1002291472 225 REA 227
Cdd:COG4372 190 KEA 192
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
64-316 |
1.20e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 64 EDIIQQrLQSVVHQREE-LQRLEMElRAQVIAHPQIIEAQRSFEAAAK-----EHVTAAAKLKEqlHEREKYILE----- 132
Cdd:pfam01576 74 EEILHE-LESRLEEEEErSQQLQNE-KKKMQQHIQDLEEQLDEEEAARqklqlEKVTTEAKIKK--LEEDILLLEdqnsk 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 133 -------LEMKLDD----------KDRELDALKIDHQTVWAN-QDLLREQTKELATFRRERDNSEAERAQHLKQIHDLQE 194
Cdd:pfam01576 150 lskerklLEERISEftsnlaeeeeKAKSLSKLKNKHEAMISDlEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 195 HLREKESQMLALEEQHRAAQDNIiyKDEQ---------LREAHAWMARVQE----------------------------- 236
Cdd:pfam01576 230 QIAELRAQLAKKEEELQAALARL--EEETaqknnalkkIRELEAQISELQEdleseraarnkaekqrrdlgeelealkte 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 237 -MDTLQSQTMQAELRDRTEQ--------FNQYWISFQQQYVEMQRGFLHTIQQLQLELNELRDRTGAPKDGSQTAQESSA 307
Cdd:pfam01576 308 lEDTLDTTAAQQELRSKREQevtelkkaLEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENA 387
|
330
....*....|....
gi 1002291472 308 E-----STLGQNKG 316
Cdd:pfam01576 388 ElqaelRTLQQAKQ 401
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
62-233 |
1.29e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.83 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 62 LSEDIIQQRlqsVVHQrEELQrlemELRAQVIAHPQIIEaqrsFEAAAKEHVTAA-AKLKEQLHER-EKYILELEMKLDD 139
Cdd:pfam00038 129 LKEELAFLK---KNHE-EEVR----ELQAQVSDTQVNVE----MDAARKLDLTSAlAEIRAQYEEIaAKNREEAEEWYQS 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 140 KDRELDalkidhQTVWANQDLLREQTKELATFRRERDNSEAERAQHLKQIHDLQEHLREKESQMlalEEQHRAAQDNIIY 219
Cdd:pfam00038 197 KLEELQ------QAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERY---ELQLADYQELISE 267
|
170
....*....|....
gi 1002291472 220 KDEQLREAHAWMAR 233
Cdd:pfam00038 268 LEAELQETRQEMAR 281
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
77-237 |
1.66e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 77 QREELQRLEMELRAQViahpqiieaqrsfeAAAKEHVtaaAKLKEQLHEREKYILELEMKLDD----------KDRELDA 146
Cdd:COG2433 407 ELTEEEEEIRRLEEQV--------------ERLEAEV---EELEAELEEKDERIERLERELSEarseerreirKDREISR 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 147 LKidhqtvWANQDLlreqTKELATFRRERDNSEaERAQHLKQIHDLqEHLREK----------ESQMLALEEQHRAAQDN 216
Cdd:COG2433 470 LD------REIERL----ERELEEERERIEELK-RKLERLKELWKL-EHSGELvpvkvvekftKEAIRRLEEEYGLKEGD 537
|
170 180
....*....|....*....|.
gi 1002291472 217 IIYkdeqLREAHAWMARVQEM 237
Cdd:COG2433 538 VVY----LRDASGAGRSTAEL 554
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
125-308 |
1.98e-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: 41.97 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 125 EREKYILELEMKLD-------DKDRELDALKIDHQTVwanQDLLREQTKELATFRRERDNSEAERAQHLKQIHDLQEHLR 197
Cdd:TIGR02168 674 ERRREIEELEEKIEeleekiaELEKALAELRKELEEL---EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 198 EKESQMLALEEQHRAAQDNIIYKDEQLREAHAWMARVQEmdtlQSQTMQAELRDRTEQFNqywiSFQQQYVEMQRGFlht 277
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA----QIEQLKEELKALREALD----ELRAELTLLNEEA--- 819
|
170 180 190
....*....|....*....|....*....|.
gi 1002291472 278 iQQLQLELNELRDRTGAPKDGSQTAQESSAE 308
Cdd:TIGR02168 820 -ANLRERLESLERRIAATERRLEDLEEQIEE 849
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
64-244 |
2.06e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 64 EDIIQQRLQSVVHQREELQRLEMELRAQVIAHPQIIEAQRSFEAAAKEHvTAAAKLKEQLHEREKYILELEMKLDDK--- 140
Cdd:COG3206 214 AKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS-PVIQQLRAQLAELEAELAELSARYTPNhpd 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 141 ----DRELDALKidhqtvwanQDLLREQTKELATFRRERDNSEAERAQHLKQIHDLQEHLR---EKESQMLALEEQHRAA 213
Cdd:COG3206 293 vialRAQIAALR---------AQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAelpELEAELRRLEREVEVA 363
|
170 180 190
....*....|....*....|....*....|.
gi 1002291472 214 QDniIYkdEQLreahawMARVQEMDTLQSQT 244
Cdd:COG3206 364 RE--LY--ESL------LQRLEEARLAEALT 384
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
63-296 |
2.39e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 63 SEDIIQQRLQSVVHQREELQRLEMELRAQVIAHPQIIEAQRsfeAAAKEHVTAAAKLKEQLHEREKYI-------LELEM 135
Cdd:COG1340 9 SLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELN---AQVKELREEAQELREKRDELNEKVkelkeerDELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 136 KLDDKDRELDALKIDHQTVWAN-----------QDLLRE-QTKELaTFRRERD-----NSEAERAQHLKQIHDLQEHLRE 198
Cdd:COG1340 86 KLNELREELDELRKELAELNKAggsidklrkeiERLEWRqQTEVL-SPEEEKElvekiKELEKELEKAKKALEKNEKLKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 199 KESQMLALEEQHRAAQDNIIYKDEQLREAHAWM-ARVQEMDTL--QSQTMQAELRDRTEQFNQYwisfQQQYVEMQRgfl 275
Cdd:COG1340 165 LRAELKELRKEAEEIHKKIKELAEEAQELHEEMiELYKEADELrkEADELHKEIVEAQEKADEL----HEEIIELQK--- 237
|
250 260
....*....|....*....|.
gi 1002291472 276 hTIQQLQLELNELRDRTGAPK 296
Cdd:COG1340 238 -ELRELRKELKKLRKKQRALK 257
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
158-313 |
3.01e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 158 QDLLREQTKELATFRRERDNSEAERAQHLKQIHDLQEHLREKESQMLALEEQHRAAQDNIIYKDEQLREAHawmarvQEM 237
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ------EEL 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002291472 238 DTLQSQtmQAELRDRTEQFNQYWISFQQQYVEMQRgflhTIQQLQLELNELRDRTGAPKDGSQTAQESSAESTLGQ 313
Cdd:COG4372 118 EELQKE--RQDLEQQRKQLEAQIAELQSEIAEREE----ELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
172-304 |
4.96e-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: 40.81 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 172 RRErdnsEAER-----AQHLKQIHDLqehLREKESQMLALEEQHRAAQDNIIYKDEqLREAHAWMArvqemdTLQSQTMQ 246
Cdd:TIGR02168 173 RRK----ETERklertRENLDRLEDI---LNELERQLKSLERQAEKAERYKELKAE-LRELELALL------VLRLEELR 238
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002291472 247 AELRDRTEQFNQYwisfQQQYVEMQRgflhTIQQLQLELNELRDRTGAPKDGSQTAQE 304
Cdd:TIGR02168 239 EELEELQEELKEA----EEELEELTA----ELQELEEKLEELRLEVSELEEEIEELQK 288
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
61-252 |
8.00e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 61 GLSEDIIQQRLQSVVHQREELQRLEMELRAQvIAHPQIIEAQRSFEA-AAKEHVTAAAKLKEQLHEREKYIlELEMKLDD 139
Cdd:COG4717 329 GLPPDLSPEELLELLDRIEELQELLREAEEL-EEELQLEELEQEIAAlLAEAGVEDEEELRAALEQAEEYQ-ELKEELEE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002291472 140 KDRELDALKIDHQTVWANQDLlREQTKELATFRRERDNSEAERAQhlkqihdLQEHLREKESQMLALEEQHRAAQdnIIY 219
Cdd:COG4717 407 LEEQLEELLGELEELLEALDE-EELEEELEELEEELEELEEELEE-------LREELAELEAELEQLEEDGELAE--LLQ 476
|
170 180 190
....*....|....*....|....*....|....*...
gi 1002291472 220 KDEQLRE-----AHAWMARVQEMDTLqsQTMQAELRDR 252
Cdd:COG4717 477 ELEELKAelrelAEEWAALKLALELL--EEAREEYREE 512
|
|
| |
