|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
93-403 |
1.23e-125 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 367.71 E-value: 1.23e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 93 NEKEQLQGLNDRFAMFIEKVRNLEQHNKVLETELVSLRQRQN-EPSRLAELYQQEIRDLRAQVDELNNEKSHILIERDSI 171
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 172 EEDLQKLRGKFEEEIRAREEAEQTLRSYKKDVDDATMVRVDLERKVESLLDEINFLRKVHDEEVTELTNMIQAAQISVEV 251
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 252 ELS-KPDLTSALKDIRGQYETLASKNLQSAEEWYKSKFASLNEQATRTNEAMRATREEVNDYRRQLQSKTIEIETLRGTN 330
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221307553 331 ESLERQIREMEEAHNAEVAGYQETIGQLDLELRNTKSEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETH 403
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Filament_head |
pfam04732 |
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ... |
8-92 |
3.74e-13 |
|
Intermediate filament head (DNA binding) region; This family represents the N-terminal head region of intermediate filaments. Intermediate filament heads bind DNA. Vimentin heads are able to alter nuclear architecture and chromatin distribution, and the liberation of heads by HIV-1 protease liberates may play an important role in HIV-1 associated cytopathogenesis and carcinogenesis. Phosphorylation of the head region can affect filament stability. The head has been shown to interaction with the rod domain of the same protein.
Pssm-ID: 461414 [Multi-domain] Cd Length: 83 Bit Score: 64.72 E-value: 3.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 8 YMSSSYRKLFGDnPRFAGSRMSnvspRSSMSSSGFRSQSVSRSSASPAGYYKRSGRS---SSFSPVHFDSVDFSQTSVLN 84
Cdd:pfam04732 1 YSSSSYRRMFGD-SSSSRPSYS----SSSGSRSVSSRSYSRSSSSSPSSSSRRSSRSssrSSYPSLAADSLDFSLADALN 75
|
....*...
gi 221307553 85 NEFKIVRT 92
Cdd:pfam04732 76 QEFKATRT 83
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
143-406 |
1.97e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 143 YQQEIRDLRAQVDELNNEKSHILIERDSIEEDLQKLRGKFEEEIRAREEAEQTLRSYKKDVDdatmvrvDLERKVESLLD 222
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA-------RLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 223 EINFLrkvhDEEVTELTNMIQAAQISVEvelskpDLTSALKDIRGQYETLASKNLQSAEEW--YKSKFASLNEQATRTNE 300
Cdd:TIGR02168 748 RIAQL----SKELTELEAEIEELEERLE------EAEEELAEAEAEIEELEAQIEQLKEELkaLREALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 301 AMRATREEVNDYRRQLQSKTIEIETLRGTNESLERQIREMEEAHNAEVAGYQETIGQLD--LELRNTKSE-MARHLREYQ 377
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEalLNERASLEEaLALLRSELE 897
|
250 260
....*....|....*....|....*....
gi 221307553 378 DLLNVKMALDIEIAAYRKLLEGEETHFSS 406
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQ 926
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
138-401 |
9.32e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 9.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 138 RLAELYQQEIRDLRAQVDELNNEKSHILIERDSIEEDLQKLRGKFEEEIRAREEAEQTLRSYKKDVDDATMVRVDLERKV 217
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 218 ESLLDEINFLRKVHDEEVTELTNMIQAAQisvevelskpDLTSALKDIRGQYETLASKNLQSAEEwykskFASLNEQATR 297
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELE----------ELEEELEELEEELEEAEEELEEAEAE-----LAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 298 TNEAMRATREEVNDYRRQLQSKTIEIETLRGTNESLERQIREME---EAHNAEVAGYQETIGQLDLELRNTKSEMARHLR 374
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLerlERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260
....*....|....*....|....*..
gi 221307553 375 EYQDLLNVKMALDIEIAAYRKLLEGEE 401
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLE 476
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
111-391 |
2.10e-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: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 111 KVRNLEQHNKVLETELVSLRQRQNEPSRLAELYQQEIRDLRAQVDELNnekshilIERDSIEEDLQKLRgkfeeeirare 190
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS-------RQISALRKDLARLE----------- 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 191 eaeQTLRSYKKDVDDATMVRVDLERKVESLLDEINFLR---KVHDEEVTELTNMIQAAQISVEvelskpDLTSALKDIRG 267
Cdd:TIGR02168 740 ---AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEeelAEAEAEIEELEAQIEQLKEELK------ALREALDELRA 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 268 QYETLASK--NLQSAEEWYKSKFASLNEQATRTNEAMRATREEVNDYRRQLQSKTIEIETLRGTNESLERQIREMEEAHN 345
Cdd:TIGR02168 811 ELTLLNEEaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 221307553 346 AEVAGYQETIGQLDlELRNTKSEMARHLREYQDLLNvKMALDIEIA 391
Cdd:TIGR02168 891 LLRSELEELSEELR-ELESKRSELRRELEELREKLA-QLELRLEGL 934
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
95-362 |
3.04e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 95 KEQLQGLNDRFAMFIEKVRNLEQHNKVLETELVSLRQRQNEPSRLAELYQQEIRDLRAQVDELNNEKSHILIERDSIEED 174
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 175 LQKLRGKFEEEIRAREEAEQTLRSYKKDVDDATMVRVDLERKVESLLDEINFLRKVHDEEVTELTNMIQAAQisvEVELS 254
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL---EALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 255 KPDLTSALKDIRGQYETLASKNLQSAEEWykskfASLNEQATRTNEAMRATREEVNDYRRQLQSKTIEIETLRGTNESLE 334
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEEL-----EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260
....*....|....*....|....*...
gi 221307553 335 RQIREMEEAHNAEVAGYQETIGQLDLEL 362
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
141-376 |
5.92e-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: 52.37 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 141 ELYQQEIRDLRAQVDELNNEKSHILIERDSIEEDLQKLRGKFEEEIRAREEAEQTLRSYKKDVDDATMVRVDLERKVESL 220
Cdd:TIGR02168 228 ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 221 LDEINFLRKVHDEEVTELTNMIQAAQISVE-VELSKPDLTSALKDIRGQYETLASKNLQSAEewYKSKFASLNEQATRTN 299
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEeLAELEEKLEELKEELESLEAELEELEAELEE--LESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221307553 300 EAMRATREEVNDYRRQLQSKTIEIETLRGTNESLERQIREME-EAHNAEVAGYQETIGQLDLELRNTKSEMARHLREY 376
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLkKLEEAELKELQAELEELEEELEELQEELERLEEAL 463
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
111-399 |
9.19e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 9.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 111 KVRNLEQHNKVLETELVSLRQRQNEPSRLAELYQQEIRDLRAQVDELNNEKSHILIERDSIEEDLQKLRGKFEEEIRARE 190
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 191 EAEQTLRSYKKDVDDATMVRVDLERKVESLLDEInflrkvhdEEVTELTNMIQAAQISVEVELSkpDLTSALKDIRGQYE 270
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEEL--------EEAEEELEEAEAELAEAEEALL--EAEAELAEAEEELE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 271 TLASKNLQSAEEwyKSKFASLNEQATRTNEAMRATREEVNDYRRQLQSKTIEIETLRGTNESLERQIREMEEAHNAEVAG 350
Cdd:COG1196 383 ELAEELLEALRA--AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 221307553 351 YQETIGQLDLELRNTKSEMARHLREYQDLLNVKMALDIEIAAYRKLLEG 399
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
131-395 |
1.38e-06 |
|
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: 50.15 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 131 QRQNEPSRLAELyQQEIRDLRAQVDELNNEKSHILIERDSIEEDLQKLRgkfeeeirareeaeQTLRSYKKDVDDatmvr 210
Cdd:COG4942 21 AAAEAEAELEQL-QQEIAELEKELAALKKEEKALLKQLAALERRIAALA--------------RRIRALEQELAA----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 211 vdLERKVESLLDEINFLRKVHDEEVTELTNMIQAAQIS-----VEVELSKPDLTSALKdiRGQYetlasknlqsaeewyk 285
Cdd:COG4942 81 --LEAELAELEKEIAELRAELEAQKEELAELLRALYRLgrqppLALLLSPEDFLDAVR--RLQY---------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 286 skFASLNEQATRTNEAMRATREEVNDYRRQLQSKTIEIETLRgtnESLERQIREMEEAHNAEvagyQETIGQLDLELRNT 365
Cdd:COG4942 141 --LKYLAPARREQAEELRADLAELAALRAELEAERAELEALL---AELEEERAALEALKAER----QKLLARLEKELAEL 211
|
250 260 270
....*....|....*....|....*....|
gi 221307553 366 KSEMARHLREYQDLLNVKMALDIEIAAYRK 395
Cdd:COG4942 212 AAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
110-371 |
2.58e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.14 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 110 EKVRNLEQHNKVLETELVSLRQRQNEPSRLAELYQQEIRDLRAQVDELNNEKSHILIERDSIEEDLQKLRGKFEEEIRAR 189
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 190 EEAEQTLRSYKKDVDDATMVRVD---LERKVESLLDEinFLRKVHD--------EEVTELTNMIQAAQISVEVELSKPDL 258
Cdd:COG1340 88 NELREELDELRKELAELNKAGGSidkLRKEIERLEWR--QQTEVLSpeeekelvEKIKELEKELEKAKKALEKNEKLKEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 259 TSALKDIRGQYETlasknlqsaeewYKSKFASLNEQATRTNEAMRATREEVNDYRRQLQSKTIEIETLRGTNESLERQIR 338
Cdd:COG1340 166 RAELKELRKEAEE------------IHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEII 233
|
250 260 270
....*....|....*....|....*....|...
gi 221307553 339 EMEEahnaEVAGYQETIGQLDLELRNTKSEMAR 371
Cdd:COG1340 234 ELQK----ELRELRKELKKLRKKQRALKREKEK 262
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
92-343 |
3.23e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 92 TNEKEQLQGLNDRFAMFIEKVRNLEQHNKVLETELVSLRQRQNEPSRLAELYQQEIRDLRAQVDELNNEKShilierdSI 171
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK-------AL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 172 EEDLQKLRGKFEEEIRAREEAEQTLRSYKKDVDDATMVRVDLERKVESLLDEINFLRKVHDEEVTELTNMIQAAQisvEV 251
Cdd:TIGR02168 802 REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE---AL 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 252 ELSKPDLTSALKDIRGQYETLASKNlqsaeewykskfASLNEQATRTNEAMRATREEVNDYRRQLQSKTIEIETLRGTne 331
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEEL------------RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER-- 944
|
250
....*....|..
gi 221307553 332 SLERQIREMEEA 343
Cdd:TIGR02168 945 LSEEYSLTLEEA 956
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
80-349 |
5.74e-06 |
|
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: 48.96 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 80 TSVLNNEFKIVRTN-EKEQLQGLNDRFAMFIEKVRNLEQHNKVLETELVSLRQRQNEPSRLAELYQQEIRDLRAQVDELN 158
Cdd:pfam15921 503 ASLQEKERAIEATNaEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHG 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 159 NEKSHILIERDSIEEDLQKLRGKFEEEIRAREEAEQTLRSYKKDVDDATMVRV--------------DLERKVESLLDEI 224
Cdd:pfam15921 583 RTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVklvnagserlravkDIKQERDQLLNEV 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 225 -------------------NFLRKVHDEEVTELTNMIQAAQISVEVELSKPDLTS-------ALKDIRGQYETLASKNLQ 278
Cdd:pfam15921 663 ktsrnelnslsedyevlkrNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSmegsdghAMKVAMGMQKQITAKRGQ 742
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221307553 279 SaeEWYKSKFASLNEQATRTNEAMRATREEVNDYRRQLQSKTIEIETLRGTNESLERQIREM-EEAHNAEVA 349
Cdd:pfam15921 743 I--DALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLkEKVANMEVA 812
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
95-414 |
1.22e-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: 48.14 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 95 KEQLQGLNDRFAMFIEKVRNLEQHNKVLETELVSLRQRQNEPSRLAELYQQEIRDLRA-----QVDELNNEKSHILIERD 169
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsRIPEIQAELSKLEEEVS 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 170 SIEEDLQKLRGKFEEEIRAREEAEQTLRSYKKDVDDATMVRVDLERKVESLldeINFLRKVhDEEVTELTNMIQaaqisv 249
Cdd:TIGR02169 809 RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL---NGKKEEL-EEELEELEAALR------ 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 250 evelskpDLTSALKDIRGQYETLASK--NLQSAEEWYKSKFASLNEQATRTNEAMRATREEVNDYRRQLQS------KTI 321
Cdd:TIGR02169 879 -------DLESRLGDLKKERDELEAQlrELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeEEL 951
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 322 EIETLRGTNESLERQIREMEEAHNAEVAGYQETIGQLD--LELRNTKSEMARHLREYQDLLNVK-----MALDIEIAA-- 392
Cdd:TIGR02169 952 SLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDelKEKRAKLEEERKAILERIEEYEKKkrevfMEAFEAINEnf 1031
|
330 340 350
....*....|....*....|....*....|...
gi 221307553 393 ---YRKL--------LEGEETHFSSGVTFSSTP 414
Cdd:TIGR02169 1032 neiFAELsggtgeliLENPDDPFAGGLELSAKP 1064
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
92-385 |
2.64e-05 |
|
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: 47.04 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 92 TNEKEQLQGLNDRFAMFIEKVRNLE----QHNKVLETELVSLRQRQNEPSRLaelYQQEIRDLRAQVDELNNEKSHILIE 167
Cdd:pfam15921 288 SSARSQANSIQSQLEIIQEQARNQNsmymRQLSDLESTVSQLRSELREAKRM---YEDKIEELEKQLVLANSELTEARTE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 168 RD-------SIEEDLQKLRGKFEEEIRARE-EAEQTLRSYKKDVDDAtmVRVDLERKVeslLDEINFlrkvhdeEVTELT 239
Cdd:pfam15921 365 RDqfsqesgNLDDQLQKLLADLHKREKELSlEKEQNKRLWDRDTGNS--ITIDHLRRE---LDDRNM-------EVQRLE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 240 NMIQAAQISVEVELSKpdltsALKDIRGQYETLasknlqsaeewykSKFASLNEQATRTNEAMRATREEVNDYRRQLQSK 319
Cdd:pfam15921 433 ALLKAMKSECQGQMER-----QMAAIQGKNESL-------------EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS 494
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221307553 320 TIEIETLRGTNESLERQIremeEAHNAEVAGYQETIGQLDLELRNTKSEmARHLREYQ---DLLNVKMA 385
Cdd:pfam15921 495 ERTVSDLTASLQEKERAI----EATNAEITKLRSRVDLKLQELQHLKNE-GDHLRNVQtecEALKLQMA 558
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
94-341 |
3.65e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 94 EKEQLQGLNDRFAMFIEKVRNLEQHNKVLETELVSLRQRQNEPSRLAELYQQEIRDLRAQVDELNNEKSHILIERDSIEE 173
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 174 DLQKLRGKFEEEIRAREEAEQTLRSYKKDVDDATMVRVDLERKVESLLDEINFLRKVHDEEVTELTNMIQAAQisvevel 253
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE------- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 254 skpDLTSALKDIRGQYETLASKNLQSAEEwykskFASLNEQATRTNEAMRATREEVNDYRRQLQSKTIEIETLRGTNESL 333
Cdd:COG1196 425 ---ELEEALAELEEEEEEEEEALEEAAEE-----EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
....*...
gi 221307553 334 ERQIREME 341
Cdd:COG1196 497 LEAEADYE 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
122-380 |
3.75e-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: 46.60 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 122 LETELVSLRQRQNEPSRLAELYQQEIRDLRAQVDELNN-----EKSHILIERD--SIEEDLQKLRGKFEEEIRAREEAEQ 194
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQelsdaSRKIGEIEKEieQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 195 TLRSYKKDVDDATMVRVDLERKVESLLDEINFL-RKVHDEEVTELTNMIQAAQ-ISVEVELSKPDLTSAL--KDIRGQYE 270
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDLeARLSHSRIPEIQAELSKLEeEVSRIEARLREIEQKLnrLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 271 TLASKNLQSAEEWYKSKFASLNEQATRTNEAMRATREEVNDYRRQLQSKTIEIETLRGTNESLERQIREMEEAHNaEVAG 350
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE-ELEA 910
|
250 260 270
....*....|....*....|....*....|
gi 221307553 351 YQETIGQLDLELRNTKSEMARHLREYQDLL 380
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALEEELSEIEDPK 940
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
83-309 |
3.82e-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: 46.20 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 83 LNNEFKIVRT---NEKEQLQGLNDRFAMFIEKVRNLEQHNKVLETELVSLRQRQNEPSRLAELYQQEIRDLRAQVDELNN 159
Cdd:TIGR02168 794 LKEELKALREaldELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 160 EKSHILIERDSIEEDLQKLRGKFEEEIRAREEAEQTLRSYKKDVDDATMVRVDLERKVESL-LDEINFLRKVHDEEVTEL 238
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLeVRIDNLQERLSEEYSLTL 953
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221307553 239 TNmiqAAQISVEVELSKPDLTSALKDIRGQYETLASKNLQSAEEW--YKSKFASLNEQATRTNEAmRATREEV 309
Cdd:TIGR02168 954 EE---AEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYeeLKERYDFLTAQKEDLTEA-KETLEEA 1022
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
95-375 |
3.88e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 95 KEQLQGLNDRFAMFIEKVRNLEQHNKVLETELVSLRQRQNEP-SRLAELYQQ---EIRDLRAQVDELNNEKSHILIERDS 170
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENiARKQNKYDElveEAKTIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 171 IEEDLQKLRgkfeeeirareeaeqtlrsykkdvddatMVRVDLERKVESLLDEINFLRKvHDEEVTeltnmiQAAQISVE 250
Cdd:PHA02562 253 PSAALNKLN----------------------------TAAAKIKSKIEQFQKVIKMYEK-GGVCPT------CTQQISEG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 251 VELSKpDLTSALKDIRGQYEtlaskNLQSAEEWYKSKFASLNEQATRTNEamratreevndyrrqLQSKtieIETLRGTN 330
Cdd:PHA02562 298 PDRIT-KIKDKLKELQHSLE-----KLDTAIDELEEIMDEFNEQSKKLLE---------------LKNK---ISTNKQSL 353
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 221307553 331 ESLERQIR----EMEEAhNAEVAGYQETIGQLDLELRNTKSEMARHLRE 375
Cdd:PHA02562 354 ITLVDKAKkvkaAIEEL-QAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
119-383 |
5.35e-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: 45.87 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 119 NKVLETELVSLRQRQNEPSRLAELYQQEIRDLRAQVDELNNEKSHILIERDSIEEDLQKLRGKfeeEIRAREEAEQTLRS 198
Cdd:pfam05483 424 KKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLK---NIELTAHCDKLLLE 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 199 YKKDVDDATMVRVDLERKVEslldEINFLRKVHDEEVTELTNMIQAaqisvEVELsKPDLTSALKDIRGQYETLASKnLQ 278
Cdd:pfam05483 501 NKELTQEASDMTLELKKHQE----DIINCKKQEERMLKQIENLEEK-----EMNL-RDELESVREEFIQKGDEVKCK-LD 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 279 SAEEwyksKFASLNEQATRTNEAMRATREEVNDYRRQLQSKTIEIETLRGTNESLERQiremEEAHNAEVAGYQETIGQL 358
Cdd:pfam05483 570 KSEE----NARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK----GSAENKQLNAYEIKVNKL 641
|
250 260
....*....|....*....|....*
gi 221307553 359 DLELRNTKSEMARHLREYQDLLNVK 383
Cdd:pfam05483 642 ELELASAKQKFEEIIDNYQKEIEDK 666
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
139-362 |
6.12e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 139 LAELYQQEIRDLRAQVDELNNEKSHILIERDSIEEDLQKLRGKFEEEIRAREEAEQTLRSYKKDVDDATMVR-VDLERKV 217
Cdd:TIGR02169 217 LKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqLRVKEKI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 218 ESLLDEINFLRKVHDEEVTELTNMiQAAQISVEVELSKpdLTSALKDIRGQYETLASKNLQSAEEwYKSKFASLNEQATR 297
Cdd:TIGR02169 297 GELEAEIASLERSIAEKERELEDA-EERLAKLEAEIDK--LLAEIEELEREIEEERKRRDKLTEE-YAELKEELEDLRAE 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221307553 298 TNE---AMRATREEVNDYRRQLQSKTIEIETLRGTNESLE---RQIREMEEAHNAEVAGYQETIGQLDLEL 362
Cdd:TIGR02169 373 LEEvdkEFAETRDELKDYREKLEKLKREINELKRELDRLQeelQRLSEELADLNAAIAGIEAKINELEEEK 443
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
129-401 |
1.28e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 129 LRQRQNEPSRLAELYQQEIRDLRAQVDELNNEKSHILIERDSIEEDLQKLRGKFEEEIrarEEAEQTlrsyKKDVDDATM 208
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL---AELARL----EQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 209 VRVDLERKVESLLDEINFLRKVHDEEVTELTNmIQAAQISVEVELSkpDLTSALKDIRGQYETLASKNLQSAEEWYKSKF 288
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEE-LEEELEEAEEELE--EAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 289 ASLNEQATRTNEAMRATREEvndyrRQLQSKTIEIETLRGTNESLERQIREMEEAHNAEvagyQETIGQLDLELRNTKSE 368
Cdd:COG1196 387 ELLEALRAAAELAAQLEELE-----EAEEALLERLERLEEELEELEEALAELEEEEEEE----EEALEEAAEEEAELEEE 457
|
250 260 270
....*....|....*....|....*....|...
gi 221307553 369 MARHLREYQDLLNVKMALDIEIAAYRKLLEGEE 401
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
122-334 |
1.65e-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: 44.28 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 122 LETELVSLRQRQNEPSRLAELYQQEIRDLRAQVDELNNEKSHILIERDSIEEDLQKLRGKFEEEIRAREEAEQTLRSYKK 201
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 202 DVDDATMVRVDLERKVESLLDEINFLRkvhdEEVTELTNMIQAAQISVEVELSKPDLtSALKDIRGQYETlasknLQSAE 281
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNEIERLE----ARLERLEDRRERLQQEIEELLKKLEE-AELKELQAELEE-----LEEEL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 221307553 282 EWYKSKFASLNEQATRTNEAMRATREEVNDYRRQLQSKTIEIETLRGTNESLE 334
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
115-371 |
2.41e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 115 LEQHNKVLETELVSLRQRQNEPSRLAELYQQEIRDLRAQVDELNNEKSHILIERDSIEEDLQKLRGKFEEEIRAREEAEQ 194
Cdd:PRK02224 312 VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 195 TLRSYKKDVDDATMVRVDLERKVESLLDEINFLRkvhdEEVTELTNMIQAAQISVE-----------------VELS--- 254
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNAEDFLEELREERDELR----EREAELEATLRTARERVEeaealleagkcpecgqpVEGSphv 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 255 ---------KPDLTSALKDIRGQYETLASKnLQSAEEwykskFASLNEQATRTNEAMRATREEVNDYRRQLQSKTIEIET 325
Cdd:PRK02224 468 etieedrerVEELEAELEDLEEEVEEVEER-LERAED-----LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE 541
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 221307553 326 LRGTNESLERQIREMEEAHNA---EVAGYQETIGQLDLELRNTKSEMAR 371
Cdd:PRK02224 542 LRERAAELEAEAEEKREAAAEaeeEAEEAREEVAELNSKLAELKERIES 590
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
128-392 |
4.20e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 128 SLRQRQNEPSRLAELYQQEIRDLRAQVDELnnekshilierdsiEEDLQKLRGK--FEEEIRAREEAEQTLRSYKKDVDD 205
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEA--------------EAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 206 ATMVRVDLERKVESLLDEINflrkVHDEEVTELTNmiqaaqisvevelskpdlTSALKDIRGQYETLasknlqsaeewyK 285
Cdd:COG3206 231 ARAELAEAEARLAALRAQLG----SGPDALPELLQ------------------SPVIQQLRAQLAEL------------E 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 286 SKFASLNEQATRTNEAMRATREEVNDYRRQLQSKT----IEIETLRGTNESLERQIREMEEAHNAEVAgyqeTIGQLDLE 361
Cdd:COG3206 277 AELAELSARYTPNHPDVIALRAQIAALRAQLQQEAqrilASLEAELEALQAREASLQAQLAQLEARLA----ELPELEAE 352
|
250 260 270
....*....|....*....|....*....|.
gi 221307553 362 LRNTKSEMARHLREYQDLLNVKMALDIEIAA 392
Cdd:COG3206 353 LRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
145-373 |
9.58e-04 |
|
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: 9.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 145 QEIRDLRAQVDELNNEKSHILIERDSIE--EDLQKLRGKFEEEIRAREEAEQ---TLRSYK--KDVDDATMVRVDLERKV 217
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYlraALRLWFaqRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 218 ESLLDEINFLRKVHDEEVTELTNMIQA-AQISVEvelskpDLTSALKDIRGQYETLASKNLQSAEewYKSKFASLNEQAT 296
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQiRGNGGD------RLEQLEREIERLERELEERERRRAR--LEALLAALGLPLP 376
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221307553 297 RTNEAMRATREEVNDYRRQLQSKTIEIETLRGTNESLERQIREMEEAHNAEVAGYQETIGQLDLELRNTKSEMARHL 373
Cdd:COG4913 377 ASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAL 453
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
139-346 |
2.61e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 139 LAELYQQEIRDLRAQVDELNNEKSHILIERDSIEEDLQKLRGKFEEEIRAREEAEQTLRSYKKDVDDATmvRVDLERKVE 218
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE--ELEEELQLE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 219 SLLDEIN-FLRKVHDEEVTELTNMIQAAQISVEvelskpdLTSALKDIRGQYETLASKNLQSAEEWYKskfASLNEQATR 297
Cdd:COG4717 367 ELEQEIAaLLAEAGVEDEEELRAALEQAEEYQE-------LKEELEELEEQLEELLGELEELLEALDE---EELEEELEE 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 221307553 298 TNEAMRATREEVNDYRRQLQSKTIEIETLRGTN---------ESLERQIREMEEAHNA 346
Cdd:COG4717 437 LEEELEELEEELEELREELAELEAELEQLEEDGelaellqelEELKAELRELAEEWAA 494
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
117-381 |
3.04e-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: 40.21 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 117 QHNKVLETELVSLRQRQNEPSRLAELYQQEIRDLRAQVDELNNEKSHILIERDSIEEDLQKLRGkfeeeiRAREEAEQTL 196
Cdd:pfam12128 597 ASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFD------EKQSEKDKKN 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 197 RSYKKDVDDATMVRVDLERKVESLLDEINFLRKVHDEEVTELTNMIQAAQISVEVELS-KPDLTSALKDIRgqyETLASK 275
Cdd:pfam12128 671 KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDaQLALLKAAIAAR---RSGAKA 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 276 NLQSAEEWYKSKFASLN-------------EQATRTNEAMRATREEVNDYRRQLQSK-TIEIETLRGTNESLERQIREME 341
Cdd:pfam12128 748 ELKALETWYKRDLASLGvdpdviaklkreiRTLERKIERIAVRRQEVLRYFDWYQETwLQRRPRLATQLSNIERAISELQ 827
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 221307553 342 EahnaevagyQETIGQLDLELRNTKSEMARH-LREYQDLLN 381
Cdd:pfam12128 828 Q---------QLARLIADTKLRRAKLEMERKaSEKQQVRLS 859
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
285-401 |
3.10e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 285 KSKFASLNEQATRTNEAMRATREEVNDYRRQLQSKTIEIETLRGTNESLERQIREMEeahnaevagyqETIGQLDLELRN 364
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKD-----------ERIERLERELSE 452
|
90 100 110
....*....|....*....|....*....|....*..
gi 221307553 365 TKSEMARHLREYQDLlnvkMALDIEIAAYRKLLEGEE 401
Cdd:COG2433 453 ARSEERREIRKDREI----SRLDREIERLERELEEER 485
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
84-416 |
3.39e-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: 40.11 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 84 NNEFKIVRTNEKEQLQGLNDRFAMFIEKVRNLEQHNKVLETELvslrqrqNEPSRLAELYQQEIR---DLRAQVDELNNE 160
Cdd:pfam05557 219 NIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQEL-------QSWVKLAQDTGLNLRspeDLSRRIEQLQQR 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 161 KSHILIERDSIEEDLQKLRgkfeeeiRAREEAEQTLRSYKKDVDDATMVRVD-------LERKVESLLDEINFLRKVHDE 233
Cdd:pfam05557 292 EIVLKEENSSLTSSARQLE-------KARRELEQELAQYLKKIEDLNKKLKRhkalvrrLQRRVLLLTKERDGYRAILES 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 234 EVTELTNMIQAAQISVEVElSKPDLTSALKDIRGQYETLASKnLQSAEEWYKSKFASLNE--QATRTNEAMR---ATREE 308
Cdd:pfam05557 365 YDKELTMSNYSPQLLERIE-EAEDMTQKMQAHNEEMEAQLSV-AEEELGGYKQQAQTLERelQALRQQESLAdpsYSKEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 309 VNDYRRqlqsktiEIETLRGTNESLERQIREME-EAHNAEVAGYQETIGQLDLELRNTKSEMArhlreYQDLLNVKMALD 387
Cdd:pfam05557 443 VDSLRR-------KLETLELERQRLREQKNELEmELERRCLQGDYDPKKTKVLHLSMNPAAEA-----YQQRKNQLEKLQ 510
|
330 340
....*....|....*....|....*....
gi 221307553 388 IEIAAYRKLLEGEETHFSSGVTFSSTPSI 416
Cdd:pfam05557 511 AEIERLKRLLKKLEDDLEQVLRLPETTST 539
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
83-368 |
4.87e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.62 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 83 LNNEFKIVRTNEKE----------QLQGLNDRFAMFIEKVRNLEQHNKVLETELVSLRQRQNEPSRLAELYQQEI----- 147
Cdd:TIGR04523 73 SNNKIKILEQQIKDlndklkknkdKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIkkkek 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 148 ---------RDLRAQVDELNNEKSHILIERDSIEEDLQKLRGKFEEEI---RAREEAEQTLRSYKKDVDDATMVRVDLER 215
Cdd:TIGR04523 153 eleklnnkyNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLESQISELKKQNNQLKD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 216 KVESLLDEINFLRKVHDEEVTELTNMIQAaQISVEVELSKP------------DLTSALKDIRGQYETLASKNLQSAEEW 283
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTQLNQLKDE-QNKIKKQLSEKqkeleqnnkkikELEKQLNQLKSEISDLNNQKEQDWNKE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 284 YKSKFASLNEQATRTNEAMRATREEVNDYRRQLQSKTIEIETLRGTNESLERQIREME---EAHNAEVAGYQETIGQLDL 360
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQneiEKLKKENQSYKQEIKNLES 391
|
....*...
gi 221307553 361 ELRNTKSE 368
Cdd:TIGR04523 392 QINDLESK 399
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
88-178 |
5.31e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 38.90 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 88 KIVRTNEKEQLQGLNDR-FAMFIEKVRNLEQHNKVLETELVSLRQRQNEPSRL-AELYQQ--EIRDLRAQVDELNNEKSH 163
Cdd:PRK05431 5 KLIRENPEAVKEALAKRgFPLDVDELLELDEERRELQTELEELQAERNALSKEiGQAKRKgeDAEALIAEVKELKEEIKA 84
|
90
....*....|....*
gi 221307553 164 ILIERDSIEEDLQKL 178
Cdd:PRK05431 85 LEAELDELEAELEEL 99
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
84-369 |
5.64e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.23 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 84 NNEFKIVRTNEKEQLQGLNDRFAMFIEKVRNLEQHNKVLETELVSLRQRQNEPSRLAELYQQEIRDLRAQVDELNNEKSH 163
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 164 ILIERDSIEEDLQKLRGKFEEEIRAREEAEQTLRSYKKDVDDATMVRVDLERKVESLLDEINFLRKVHDE---EVTELTN 240
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKlesEKKEKES 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 241 MIqaAQISVEVELSKPDLTsalkdiRGQYETLASKNLQSAEEWYKSKFASLNEQaTRTNEAMRATREEVNDYRRQLQSKT 320
Cdd:TIGR04523 539 KI--SDLEDELNKDDFELK------KENLEKEIDEKNKEIEELKQTQKSLKKKQ-EEKQELIDQKEKEKKDLIKEIEEKE 609
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 221307553 321 I-------EIETLRGTNESLERQIREMEEAHNA---EVAGYQETIgqldLELRNTKSEM 369
Cdd:TIGR04523 610 KkisslekELEKAKKENEKLSSIIKNIKSKKNKlkqEVKQIKETI----KEIRNKWPEI 664
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
161-380 |
7.59e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 161 KSHILiERDSIEEDLQKLRGKFeeeirareeaeQTLRSYKKDVDDAtmvrvdlERKVESLldeinflrkvhdEEVTELTN 240
Cdd:COG4913 214 REYML-EEPDTFEAADALVEHF-----------DDLERAHEALEDA-------REQIELL------------EPIRELAE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307553 241 MIQAAQISVEVelskpdltsaLKDIRgqyETLASKNLQSAEEWYKSKFASLNEQATRTNEAMRATREEVNDYRRQLQSKT 320
Cdd:COG4913 263 RYAAARERLAE----------LEYLR---AALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELE 329
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221307553 321 IEIETLRGTN-ESLERQIREMEEAHN---AEVAGYQETIGQLDLELRNTKSEMARHLREYQDLL 380
Cdd:COG4913 330 AQIRGNGGDRlEQLEREIERLERELEereRRRARLEALLAALGLPLPASAEEFAALRAEAAALL 393
|
|
| |
