|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
79-391 |
4.25e-138 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 397.75 E-value: 4.25e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 79 NEKETMQSLNDRLASYLDRVRSLETENRRLESKIREHLEKKGPQV-RDWSHYFKIIEDLRAQIFANTVDNARIVLQIDNA 157
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPsRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 158 RLAADDFRVKYETELAMRQSVENDIHGLRKVIDDTNITRLQLETEIEALKEELLFMKKNHEEEVKGLQAQIASSGLTVEV 237
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 238 DAPKSQDLAKIMADIRAQYDELARKNREELDKYWSQQIEESTTVVTTQSAEVGAAETTLTELRRTVQSLEIDLDSMRNLK 317
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40354195 318 ASLENSLREVEARYALQMEQLNGILLHLESELAQTRAEGQRQAQEYEALLNIKVKLEAEIATYRRLLEdGEDFN 391
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLE-GEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
179-386 |
7.23e-10 |
|
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: 7.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 179 ENDIHGLRKVIDDTNITRLQLETEIEALKEELLFMkknhEEEVKGLQAQIASSGLTVEVDAPKSQDLAKIMADIRAQYDE 258
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEELEEELEQLRKELEEL----SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 259 LAR---KNREELdKYWSQQIEESTTVVTTQSAEVGAAETTLTELRRTVQSLEIDLDSMRNLKASLENSLREVEARY---A 332
Cdd:TIGR02168 766 LEErleEAEEEL-AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLedlE 844
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 40354195 333 LQMEQLNGILLHLESELAQTRAEGQRQAQEYEALLNIKVKLEAEIATYRRLLED 386
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
133-386 |
1.19e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 133 IEDLRAQIFANTVDNARIVLQIDNARLAADDFRVKYETELAMRQSVENDIHGLRKVIDDTNITRLQLETEIEALKEE--- 209
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEElae 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 210 LLFMKKNHEEEVKGLQAQIassgltvEVDAPKSQDLAKIMADIRAQYDELARKNREELDKYWSQQIEESttvvtTQSAEV 289
Cdd:COG1196 328 LEEELEELEEELEELEEEL-------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL-----EALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 290 GAAETTLTELRRTVQSLEIDLDSMRNLKASLENSLREVEARyalqmeqlngiLLHLESELAQTRAEGQRQAQEYEALLNI 369
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE-----------EEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250
....*....|....*..
gi 40354195 370 KVKLEAEIATYRRLLED 386
Cdd:COG1196 465 LAELLEEAALLEAALAE 481
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
81-330 |
3.20e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 81 KETMQSLNDRLASYLDRVRSLETenrrLESKIREHLEKKGPQVRDWSHYFKIIEDLRAQifANTVDNARIVLQIDNARLA 160
Cdd:PRK02224 233 RETRDEADEVLEEHEERREELET----LEAEIEDLRETIAETEREREELAEEVRDLRER--LEELEEERDDLLAEAGLDD 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 161 ADDfrvkyETELAMRQSVENDIHGLRKVIDDTNITRLQLETEIEALKEELlfmkKNHEEEVKGLQAQIAssgltvevdap 240
Cdd:PRK02224 307 ADA-----EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA----DDLEERAEELREEAA----------- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 241 ksqDLAKIMADIRAQYDElARKNREELDKywsqQIEESttvvttqSAEVGAAETTLTELRRTVQSLEIDLDSMRNLKASL 320
Cdd:PRK02224 367 ---ELESELEEAREAVED-RREEIEELEE----EIEEL-------RERFGDAPVDLGNAEDFLEELREERDELREREAEL 431
|
250
....*....|
gi 40354195 321 ENSLREVEAR 330
Cdd:PRK02224 432 EATLRTARER 441
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
196-385 |
1.76e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.00 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 196 RLQLETEIEALKEELLFMKKnHEEEVKGLQAQIASsgltvevdapKSQDLAKIMADIRAQYDELARKNREELDKYWSQqi 275
Cdd:smart00787 146 KEGLDENLEGLKEDYKLLMK-ELELLNSIKPKLRD----------RKDALEEELRQLKQLEDELEDCDPTELDRAKEK-- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 276 eesttvVTTQSAEVGAAETTLTELRRTVQSLEIDLDSMRNLKASLENSLREVEARYalqmEQLNGILLHLESELaqtrae 355
Cdd:smart00787 213 ------LKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKL----EQCRGFTFKEIEKL------ 276
|
170 180 190
....*....|....*....|....*....|...
gi 40354195 356 gQRQAQEYEALLNIK-VKLEAEIA--TYRRLLE 385
Cdd:smart00787 277 -KEQLKLLQSLTGWKiTKLSGNTLsmTYDREIN 308
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
79-391 |
4.25e-138 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 397.75 E-value: 4.25e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 79 NEKETMQSLNDRLASYLDRVRSLETENRRLESKIREHLEKKGPQV-RDWSHYFKIIEDLRAQIFANTVDNARIVLQIDNA 157
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPsRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 158 RLAADDFRVKYETELAMRQSVENDIHGLRKVIDDTNITRLQLETEIEALKEELLFMKKNHEEEVKGLQAQIASSGLTVEV 237
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 238 DAPKSQDLAKIMADIRAQYDELARKNREELDKYWSQQIEESTTVVTTQSAEVGAAETTLTELRRTVQSLEIDLDSMRNLK 317
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40354195 318 ASLENSLREVEARYALQMEQLNGILLHLESELAQTRAEGQRQAQEYEALLNIKVKLEAEIATYRRLLEdGEDFN 391
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLE-GEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
179-386 |
7.23e-10 |
|
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: 7.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 179 ENDIHGLRKVIDDTNITRLQLETEIEALKEELLFMkknhEEEVKGLQAQIASSGLTVEVDAPKSQDLAKIMADIRAQYDE 258
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEELEEELEQLRKELEEL----SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 259 LAR---KNREELdKYWSQQIEESTTVVTTQSAEVGAAETTLTELRRTVQSLEIDLDSMRNLKASLENSLREVEARY---A 332
Cdd:TIGR02168 766 LEErleEAEEEL-AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLedlE 844
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 40354195 333 LQMEQLNGILLHLESELAQTRAEGQRQAQEYEALLNIKVKLEAEIATYRRLLED 386
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
133-386 |
1.19e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 133 IEDLRAQIFANTVDNARIVLQIDNARLAADDFRVKYETELAMRQSVENDIHGLRKVIDDTNITRLQLETEIEALKEE--- 209
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEElae 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 210 LLFMKKNHEEEVKGLQAQIassgltvEVDAPKSQDLAKIMADIRAQYDELARKNREELDKYWSQQIEESttvvtTQSAEV 289
Cdd:COG1196 328 LEEELEELEEELEELEEEL-------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL-----EALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 290 GAAETTLTELRRTVQSLEIDLDSMRNLKASLENSLREVEARyalqmeqlngiLLHLESELAQTRAEGQRQAQEYEALLNI 369
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE-----------EEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250
....*....|....*..
gi 40354195 370 KVKLEAEIATYRRLLED 386
Cdd:COG1196 465 LAELLEEAALLEAALAE 481
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
250-388 |
3.24e-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: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 250 ADIRAQYDELARKNREELDkywsQQIEESTTVVTTQSAEVGAAETTLTELRRTVQSLEIDLDSMRNLKASLENSLREVEA 329
Cdd:COG1196 227 AELLLLKLRELEAELEELE----AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40354195 330 RYALQMEQLNGI---LLHLESELAQTRAEGQRQAQEYEALLNIKVKLEAEIATYRRLLEDGE 388
Cdd:COG1196 303 DIARLEERRRELeerLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
62-389 |
3.76e-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: 46.26 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 62 GLATGIAGGLAGMGGIQNEKETMQ-SLNDRLASYLDRVRSLETENRRLESKIREHLEKkgpqvrdwshYFKIIEDLRAQ- 139
Cdd:pfam15921 282 GLTEKASSARSQANSIQSQLEIIQeQARNQNSMYMRQLSDLESTVSQLRSELREAKRM----------YEDKIEELEKQl 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 140 IFANTvdnarivlQIDNARLAADDFRV-----------------KYETELAMRQSVEN-----------DIHGLRKVIDD 191
Cdd:pfam15921 352 VLANS--------ELTEARTERDQFSQesgnlddqlqklladlhKREKELSLEKEQNKrlwdrdtgnsiTIDHLRRELDD 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 192 TNITRLQLETEIEALKEELlfmKKNHEEEVKGLQAQIAS----SGLTVEVDAPKSQdLAKIMADIRAQYDELARKNReel 267
Cdd:pfam15921 424 RNMEVQRLEALLKAMKSEC---QGQMERQMAAIQGKNESlekvSSLTAQLESTKEM-LRKVVEELTAKKMTLESSER--- 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 268 dkywsqQIEESTTVVTTQSAEVGAAETTLTELRRTVQSLEIDLDSMRNLKASLENSLREVEArYALQMEQLNGILLHLES 347
Cdd:pfam15921 497 ------TVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEA-LKLQMAEKDKVIEILRQ 569
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 40354195 348 ELAQTRAEGQRQAQEYEALLNIKVKLEAEIATYR------RLLEDGED 389
Cdd:pfam15921 570 QIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRlelqefKILKDKKD 617
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
81-330 |
3.20e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 81 KETMQSLNDRLASYLDRVRSLETenrrLESKIREHLEKKGPQVRDWSHYFKIIEDLRAQifANTVDNARIVLQIDNARLA 160
Cdd:PRK02224 233 RETRDEADEVLEEHEERREELET----LEAEIEDLRETIAETEREREELAEEVRDLRER--LEELEEERDDLLAEAGLDD 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 161 ADDfrvkyETELAMRQSVENDIHGLRKVIDDTNITRLQLETEIEALKEELlfmkKNHEEEVKGLQAQIAssgltvevdap 240
Cdd:PRK02224 307 ADA-----EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA----DDLEERAEELREEAA----------- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 241 ksqDLAKIMADIRAQYDElARKNREELDKywsqQIEESttvvttqSAEVGAAETTLTELRRTVQSLEIDLDSMRNLKASL 320
Cdd:PRK02224 367 ---ELESELEEAREAVED-RREEIEELEE----EIEEL-------RERFGDAPVDLGNAEDFLEELREERDELREREAEL 431
|
250
....*....|
gi 40354195 321 ENSLREVEAR 330
Cdd:PRK02224 432 EATLRTARER 441
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
74-391 |
6.35e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 74 MGGIQNEKETMQSLNDRLASYLDRVRSLETENRRLESKIREhLEKKGPQVRdwshyfKIIEDLRaqifantvDNARIVLQ 153
Cdd:PRK03918 223 LEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRE-LEERIEELK------KEIEELE--------EKVKELKE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 154 ID---NARLAADDFRVKYETELA----MRQSVENDIHGLRKVIDDTN--ITRL-QLETEIEALKEELLFMKKNHE--EEV 221
Cdd:PRK03918 288 LKekaEEYIKLSEFYEEYLDELReiekRLSRLEEEINGIEERIKELEekEERLeELKKKLKELEKRLEELEERHElyEEA 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 222 KGLQAQIAS-----SGLTVEVDAPKSQDLAKIMADIRAQYDELARKnREELDKywsQQIEESTTVVTTQSAE----VGAA 292
Cdd:PRK03918 368 KAKKEELERlkkrlTGLTPEKLEKELEELEKAKEEIEEEISKITAR-IGELKK---EIKELKKAIEELKKAKgkcpVCGR 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 293 ETT-------LTELRRTVQSLEIDLDSMRNLKASLENSLREVE-----ARYALQMEQLNGILLHLESELAQTRAEG-QRQ 359
Cdd:PRK03918 444 ELTeehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEkvlkkESELIKLKELAEQLKELEEKLKKYNLEElEKK 523
|
330 340 350
....*....|....*....|....*....|..
gi 40354195 360 AQEYEALLNIKVKLEAEIATYRRLLEDGEDFN 391
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEELK 555
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
196-385 |
1.76e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.00 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 196 RLQLETEIEALKEELLFMKKnHEEEVKGLQAQIASsgltvevdapKSQDLAKIMADIRAQYDELARKNREELDKYWSQqi 275
Cdd:smart00787 146 KEGLDENLEGLKEDYKLLMK-ELELLNSIKPKLRD----------RKDALEEELRQLKQLEDELEDCDPTELDRAKEK-- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 276 eesttvVTTQSAEVGAAETTLTELRRTVQSLEIDLDSMRNLKASLENSLREVEARYalqmEQLNGILLHLESELaqtrae 355
Cdd:smart00787 213 ------LKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKL----EQCRGFTFKEIEKL------ 276
|
170 180 190
....*....|....*....|....*....|...
gi 40354195 356 gQRQAQEYEALLNIK-VKLEAEIA--TYRRLLE 385
Cdd:smart00787 277 -KEQLKLLQSLTGWKiTKLSGNTLsmTYDREIN 308
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
153-386 |
2.33e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 153 QIDNARLAADDFRVKYETELAMRQSVENDIHGLRKVIDDTNITRLQLETEIEALKEELLFMKKNHEEEVKGLQAQIASSG 232
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 233 LTVEVDAPK---SQDLAKIMADIRAQYDELARKNREELDKYwsqqieesttvvttqsaevgaaETTLTELRRTVQSLEID 309
Cdd:COG4942 115 RLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQAEEL----------------------RADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40354195 310 LDSMRNLKASLENSLREVEARYALQmeqlngillhlESELAQTRAEGQRQAQEYEALLNIKVKLEAEIATYRRLLED 386
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAER-----------QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
77-355 |
2.44e-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: 40.43 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 77 IQNEKETMQSLNDRLASYLDRVRSLETENRRLESKIREHLEKkgpqvrdwshyfkiIEDLRAQIfantvdnARIVLQIDN 156
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE--------------IEELEAQI-------EQLKEELKA 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 157 ARLAADDFRVKYETELAMRQSVENDIHGLRKVIDDTNITRLQLETEIEALKEELLFMKKNHEEEVKGLQAqiASSGLTVE 236
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE--LESELEAL 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 237 VDAPKSQDLAkiMADIRAQYDELARKNREELDKywsqqieesttvvttqsaeVGAAETTLTELRRTVQSLEIDLDSMRNL 316
Cdd:TIGR02168 879 LNERASLEEA--LALLRSELEELSEELRELESK-------------------RSELRRELEELREKLAQLELRLEGLEVR 937
|
250 260 270
....*....|....*....|....*....|....*....
gi 40354195 317 KASLENSLREveaRYALQMEQLNGILLHLESELAQTRAE 355
Cdd:TIGR02168 938 IDNLQERLSE---EYSLTLEEAEALENKIEDDEEEARRR 973
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
76-362 |
2.75e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.05 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 76 GIQNEKETMQSLNDRLAsylDRVRSLETENRRLESKIREHLEKKGPQVRdwshyfKIIEDLRAQIfantvdnARIVLQID 155
Cdd:TIGR02169 248 SLEEELEKLTEEISELE---KRLEEIEQLLEELNKKIKDLGEEEQLRVK------EKIGELEAEI-------ASLERSIA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 156 NARLAADDF---RVKYETElamRQSVENDIHGLRKVIDDTNITRLQLETEIEALKEELlfmkknhEEEVKGLQAQIASSG 232
Cdd:TIGR02169 312 EKERELEDAeerLAKLEAE---IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL-------EDLRAELEEVDKEFA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 233 LTVEvdapKSQDLAKIMADIRAQYDELARKNREELD--KYWSQQIEESTTVVTTQSAEVGAAETTLTELRRTVQSLEIDL 310
Cdd:TIGR02169 382 ETRD----ELKDYREKLEKLKREINELKRELDRLQEelQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 40354195 311 DSMRNLKASLENSLREVEARYalqmEQLNGILLHLESELAqtRAEGQRQAQE 362
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEY----DRVEKELSKLQRELA--EAEAQARASE 503
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
77-329 |
3.66e-03 |
|
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: 39.70 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 77 IQNEKETMQSLNDRLASYLDRVRSLETENRRLESKIREHLEKKGPQVRDWSHYFKIIE----DLRAQIfANTVDNARIVL 152
Cdd:pfam05483 536 IENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEnkcnNLKKQI-ENKNKNIEELH 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 153 Q----------IDNARLAADDFRV-KYETELA-MRQSVENDIHGLRKVIDDTNITRLQLETEIEALKEELLFMKKNHEEE 220
Cdd:pfam05483 615 QenkalkkkgsAENKQLNAYEIKVnKLELELAsAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEI 694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 221 VKGLQAQIAssgltvevdapksqDLAKIMADIRAQYDELARKNREELDKYWSQQIEESTTVVttqsaevgAAETTLTELR 300
Cdd:pfam05483 695 DKRCQHKIA--------------EMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKA--------ALEIELSNIK 752
|
250 260
....*....|....*....|....*....
gi 40354195 301 RTVQSLEIDLDSMRNLKASLENSLREVEA 329
Cdd:pfam05483 753 AELLSLKKQLEIEKEEKEKLKMEAKENTA 781
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
185-368 |
3.99e-03 |
|
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: 39.72 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 185 LRKVIDDTNITRLQLETEiEALKEELLFMKKNHEEEVKGLQAQIASSGLTVEVDAPKSQDLAKIMADIRAQYDE-----L 259
Cdd:pfam15921 477 LRKVVEELTAKKMTLESS-ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEcealkL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 260 ARKNREELDKYWSQQIEESTTVVTTQSAEVGAAETTLTELRRTVQSLEIDLDSMRNLKASLENSLREVEARYA-LQMEQL 338
Cdd:pfam15921 556 QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSdLELEKV 635
|
170 180 190
....*....|....*....|....*....|
gi 40354195 339 NgiLLHLESElaQTRAEGQRQaQEYEALLN 368
Cdd:pfam15921 636 K--LVNAGSE--RLRAVKDIK-QERDQLLN 660
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
162-386 |
5.25e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.28 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 162 DDFRVKYETELAMRQSVENDIHGLRKVIDD--TNITRLQLETE----IEALKEE--------LLFMKKNHEEEVKGLQAQ 227
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEkrQQLERLRREREkaerYQALLKEkreyegyeLLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 228 IAS-----SGLTVEVdapksQDLAKIMADIRAQYDELARKNREEldkywsqqIEESTTVVTTQSAEVGAaettltELRRT 302
Cdd:TIGR02169 246 LASleeelEKLTEEI-----SELEKRLEEIEQLLEELNKKIKDL--------GEEEQLRVKEKIGELEA------EIASL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 303 VQSLEIDLDSMRNLKASLENSLREVEaRYALQMEQLNGILLHLESELAQTRAEGQRQAQEYEALLNIKVKLEAEIATYRR 382
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEID-KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD 385
|
....
gi 40354195 383 LLED 386
Cdd:TIGR02169 386 ELKD 389
|
|
| PRK10361 |
PRK10361 |
DNA recombination protein RmuC; Provisional |
268-368 |
5.79e-03 |
|
DNA recombination protein RmuC; Provisional
Pssm-ID: 182409 [Multi-domain] Cd Length: 475 Bit Score: 38.81 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 268 DKYWSQQIEESTTVVttqsAEVGAAETTLTE---LRRTVQSLEIDLDSMRNLKASLENSLREVEARyalqmeqLNGILLH 344
Cdd:PRK10361 28 AQQKAEQLAEREEMV----AELSAAKQQITQsehWRAECELLNNEVRSLQSINTSLEADLREVTTR-------MEAAQQH 96
|
90 100
....*....|....*....|....
gi 40354195 345 LESELAQTRAEGQRQAQEYEALLN 368
Cdd:PRK10361 97 ADDKIRQMINSEQRLSEQFENLAN 120
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
79-379 |
6.73e-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: 38.85 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 79 NEKET-MQSLNDRLASYLDRVRSLETENRRLESKIREHLEKKgpqvrdwshyfkiiEDLRAQIFANTVDNARIVLQIDNA 157
Cdd:TIGR04523 366 EEKQNeIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLN--------------QQKDEQIKKLQQEKELLEKEIERL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 158 RlaadDFRVKYETELamrQSVENDIHGLRKVIDDTNITRLQLETEIEALKEELlfmkKNHEEEVKGLQAQIASsgltvev 237
Cdd:TIGR04523 432 K----ETIIKNNSEI---KDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI----NKIKQNLEQKQKELKS------- 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 238 dapKSQDLAKIMADIraqydelarKNREELDKYWSQQIEESTTVVTTQSAEVGAAETTLTELRRTVQSLEIDLDSmRNLK 317
Cdd:TIGR04523 494 ---KEKELKKLNEEK---------KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK-ENLE 560
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40354195 318 ASLENSLREVEaryalQMEQLNGILLHLESELaqtraegQRQAQEYEA-LLNIKVKLEAEIAT 379
Cdd:TIGR04523 561 KEIDEKNKEIE-----ELKQTQKSLKKKQEEK-------QELIDQKEKeKKDLIKEIEEKEKK 611
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
198-389 |
6.92e-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: 38.88 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 198 QLETEIEALKEELLFMkknhEEEVKGLQAQIASSGLTVEVDAPKSQDLAKIMADIRAQYDEL-ARKNREELDKywsQQIE 276
Cdd:TIGR02168 236 ELREELEELQEELKEA----EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALaNEISRLEQQK---QILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 277 ESTTVVTTQSAEVgaaETTLTELRRTVQSLEIDLDSMRNLKASLENSLREVEAryalQMEQLNGILLHLESELAQTRAEG 356
Cdd:TIGR02168 309 ERLANLERQLEEL---EAQLEELESKLDELAEELAELEEKLEELKEELESLEA----ELEELEAELEELESRLEELEEQL 381
|
170 180 190
....*....|....*....|....*....|...
gi 40354195 357 QRQAQEYEALLNIKVKLEAEIATYRRLLEDGED 389
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
226-381 |
9.12e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 37.79 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 226 AQIASSGLTVEVDAPKSQdLAKIMADIRAQYDELARKNREELDKYWSQQIEESTTvvttqsAEVGAAETTLTELRRTVQS 305
Cdd:pfam00529 49 FQLDPTDYQAALDSAEAQ-LAKAQAQVARLQAELDRLQALESELAISRQDYDGAT------AQLRAAQAAVKAAQAQLAQ 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40354195 306 LEIDLDSMRNL-KASLENSLREVEARYALQmeQLNGILLHLESELAQTRAEGQRQAQEYEALL-NIKVKLEAEIATYR 381
Cdd:pfam00529 122 AQIDLARRRVLaPIGGISRESLVTAGALVA--QAQANLLATVAQLDQIYVQITQSAAENQAEVrSELSGAQLQIAEAE 197
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
280-381 |
9.54e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 38.46 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40354195 280 TVVTTQSAEVgAAETTLTELRRTVQ-SLEIDLDSMRNlKASLENSLREVEARYAL---------QMEQLNGILLHLESEL 349
Cdd:PTZ00491 631 TNVDVQSVEP-VDERTRDSLQKSVQlAIEITTKSQEA-AARHQAELLEQEARGRLerqkmhdkaKAEEQRTKLLELQAES 708
|
90 100 110
....*....|....*....|....*....|....*
gi 40354195 350 AQTRAEGQRQAQ---EYEALLnIKVKLEAEIATYR 381
Cdd:PTZ00491 709 AAVESSGQSRAEalaEAEARL-IEAEAEVEQAELR 742
|
|
| |
