|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
82-393 |
1.85e-95 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 289.90 E-value: 1.85e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 82 QEKEEMKALNDKFASLIGKVQALEQRNQLLETRWSFLQGQGSATF-DLSHHYETFQGRLQEELRKVSQERGQLEANLLQV 160
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPsRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 161 LEKVEEFRVRYEDEISKRTDLEFTFVQLKKDLDAECLRRTELETKLKGLQGFLELMRTVYEQELKDLTAQVKDVSVTVGL 240
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 241 DSRCHIDLSGIVEEVKAQYDAIAARSLEEAEAYSRSQLEERAARSAEFGNSLQSSRCEIADLNVRIQKLRSQIVSVKSHC 320
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124249090 321 LKLEENIKVAEEQGELAFQDAKDKMAQLENALQKAKQDMARQLREYQDLMNTKLALDIEIATYHKLMEGEESR 393
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
76-370 |
5.04e-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: 55.45 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 76 VQQQKNQEKEEMKALNDKFASLIGKVQALEQRNQLLETRWSFLQGQGSATFDLSHHYETFQGRLQEELRKVSQERGQLEA 155
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 156 NLLQVLEKVEEFRVRYEDEISKRTDLEFTFVQLKKDLDAECLRRTELETKLKGLQGFLelmrTVYEQELKDLTAQVKDVS 235
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA----ANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 236 VTVGLDSRCHIDLSGIVEEVKAQYDaiaarSLEEAEAYSRSQLEeraarsaEFGNSLQSSRCEIADLNVRIQKLRSQIVS 315
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIE-----ELEELIEELESELE-------ALLNERASLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 124249090 316 VKSHCLKLEENIkvaeeqgelafQDAKDKMAQLENALQKAKQDMAR---QLRE-YQDLM 370
Cdd:TIGR02168 906 LESKRSELRREL-----------EELREKLAQLELRLEGLEVRIDNlqeRLSEeYSLTL 953
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
27-78 |
5.32e-08 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 51.96 E-value: 5.32e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 124249090 27 GTSGWGSCGLPGPGFSSRS---LTSCRPAGtIPKVTVNPSLLVPLDLKVDPAVQQ 78
Cdd:pfam16208 102 GGGGYGGGGFGGGGFGGRGgfgGPPCPPGG-IQEVTVNQSLLQPLNLEIDPEIQR 155
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
75-391 |
7.88e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.36 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 75 AVQQQKNQEKEEMKALNDKFASLIGKVQALEQRNQLLETRWSFLQGQG-----------SATFDLSHHYETFQGRLQEEL 143
Cdd:PRK01156 406 AIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgttlgeEKSNHIINHYNEKKSRLEEKI 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 144 RKVSQERGQLEANLLQVL--------EKVEEFRVRYEDEISKRTDLEFTFVQLKKDLDAEcLRRTELETKLKGLQgfLEL 215
Cdd:PRK01156 486 REIEIEVKDIDEKIVDLKkrkeylesEEINKSINEYNKIESARADLEDIKIKINELKDKH-DKYEEIKNRYKSLK--LED 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 216 MRTVYEQELKdLTAQVKDVSVTvGLDSRchidlsgiVEEVKAQYDAIAAR------SLEEAEAYSRSQLEeraaRSAEFG 289
Cdd:PRK01156 563 LDSKRTSWLN-ALAVISLIDIE-TNRSR--------SNEIKKQLNDLESRlqeieiGFPDDKSYIDKSIR----EIENEA 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 290 NSLQSSRCEIADLNVRIQKLRSQIVSVKSHCLKLEENIKvaeEQGELAFQ--DAKDKMAQLENALQKAKQDMARQLREYQ 367
Cdd:PRK01156 629 NNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIP---DLKEITSRinDIEDNLKKSRKALDDAKANRARLESTIE 705
|
330 340
....*....|....*....|....
gi 124249090 368 DLMNTKLALDIEIATYHKLMEGEE 391
Cdd:PRK01156 706 ILRTRINELSDRINDINETLESMK 729
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
75-381 |
3.95e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 75 AVQQQKNQEKEEMKALNDKFASLIGKVQALEQRNQLLETRwsflqgQGSATFDLShhyetfqgRLQEELRKVSQERGQLE 154
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLE------LEELELELE--------EAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 155 ANLLQVLEKVEEFRVRYEDEISKRTDLEFTFVQLKKDLDAECLRRTELETKLKGLqgflelmrtvyEQELKDLTAQvkdv 234
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA-----------EAELAEAEEA---- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 235 svtvgldsrchidlsgiVEEVKAQYDAIAARSLEEAEAYSRSQLEERAARSAefgnsLQSSRCEIADLNVRIQKLRSQIV 314
Cdd:COG1196 367 -----------------LLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-----LEELEEAEEALLERLERLEEELE 424
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124249090 315 SVKSHclklEENIKVAEEQGELAFQDAKDKMAQLENALQKAKQDMARQLREYQDLMNTKLALDIEIA 381
Cdd:COG1196 425 ELEEA----LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
82-393 |
1.85e-95 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 289.90 E-value: 1.85e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 82 QEKEEMKALNDKFASLIGKVQALEQRNQLLETRWSFLQGQGSATF-DLSHHYETFQGRLQEELRKVSQERGQLEANLLQV 160
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPsRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 161 LEKVEEFRVRYEDEISKRTDLEFTFVQLKKDLDAECLRRTELETKLKGLQGFLELMRTVYEQELKDLTAQVKDVSVTVGL 240
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 241 DSRCHIDLSGIVEEVKAQYDAIAARSLEEAEAYSRSQLEERAARSAEFGNSLQSSRCEIADLNVRIQKLRSQIVSVKSHC 320
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124249090 321 LKLEENIKVAEEQGELAFQDAKDKMAQLENALQKAKQDMARQLREYQDLMNTKLALDIEIATYHKLMEGEESR 393
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
76-370 |
5.04e-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: 55.45 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 76 VQQQKNQEKEEMKALNDKFASLIGKVQALEQRNQLLETRWSFLQGQGSATFDLSHHYETFQGRLQEELRKVSQERGQLEA 155
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 156 NLLQVLEKVEEFRVRYEDEISKRTDLEFTFVQLKKDLDAECLRRTELETKLKGLQGFLelmrTVYEQELKDLTAQVKDVS 235
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA----ANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 236 VTVGLDSRCHIDLSGIVEEVKAQYDaiaarSLEEAEAYSRSQLEeraarsaEFGNSLQSSRCEIADLNVRIQKLRSQIVS 315
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIE-----ELEELIEELESELE-------ALLNERASLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 124249090 316 VKSHCLKLEENIkvaeeqgelafQDAKDKMAQLENALQKAKQDMAR---QLRE-YQDLM 370
Cdd:TIGR02168 906 LESKRSELRREL-----------EELREKLAQLELRLEGLEVRIDNlqeRLSEeYSLTL 953
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
27-78 |
5.32e-08 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 51.96 E-value: 5.32e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 124249090 27 GTSGWGSCGLPGPGFSSRS---LTSCRPAGtIPKVTVNPSLLVPLDLKVDPAVQQ 78
Cdd:pfam16208 102 GGGGYGGGGFGGGGFGGRGgfgGPPCPPGG-IQEVTVNQSLLQPLNLEIDPEIQR 155
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
75-391 |
7.88e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.36 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 75 AVQQQKNQEKEEMKALNDKFASLIGKVQALEQRNQLLETRWSFLQGQG-----------SATFDLSHHYETFQGRLQEEL 143
Cdd:PRK01156 406 AIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgttlgeEKSNHIINHYNEKKSRLEEKI 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 144 RKVSQERGQLEANLLQVL--------EKVEEFRVRYEDEISKRTDLEFTFVQLKKDLDAEcLRRTELETKLKGLQgfLEL 215
Cdd:PRK01156 486 REIEIEVKDIDEKIVDLKkrkeylesEEINKSINEYNKIESARADLEDIKIKINELKDKH-DKYEEIKNRYKSLK--LED 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 216 MRTVYEQELKdLTAQVKDVSVTvGLDSRchidlsgiVEEVKAQYDAIAAR------SLEEAEAYSRSQLEeraaRSAEFG 289
Cdd:PRK01156 563 LDSKRTSWLN-ALAVISLIDIE-TNRSR--------SNEIKKQLNDLESRlqeieiGFPDDKSYIDKSIR----EIENEA 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 290 NSLQSSRCEIADLNVRIQKLRSQIVSVKSHCLKLEENIKvaeEQGELAFQ--DAKDKMAQLENALQKAKQDMARQLREYQ 367
Cdd:PRK01156 629 NNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIP---DLKEITSRinDIEDNLKKSRKALDDAKANRARLESTIE 705
|
330 340
....*....|....*....|....
gi 124249090 368 DLMNTKLALDIEIATYHKLMEGEE 391
Cdd:PRK01156 706 ILRTRINELSDRINDINETLESMK 729
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
139-372 |
1.29e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.54 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 139 LQEELRKVSQERGQLEANLLQV-LEKVEEFrvryEDEISKRTDleftfvQLKKDLDAECLRRTELETKLKGLQGFLELMR 217
Cdd:pfam06160 235 VDKEIQQLEEQLEENLALLENLeLDEAEEA----LEEIEERID------QLYDLLEKEVDAKKYVEKNLPEIEDYLEHAE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 218 TVYeQELKDLTAQVK--------DVSVTVGLDSRchidlsgiVEEVKAQYDAIAARSLEEAEAYS---------RSQLEE 280
Cdd:pfam06160 305 EQN-KELKEELERVQqsytlnenELERVRGLEKQ--------LEELEKRYDEIVERLEEKEVAYSelqeeleeiLEQLEE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 281 RAARSAEFGNSLQSSRCEIADLNVRIQKLRSQIVSVKSHCLKLeeNIKVAEEQGELAFQDAKDKMAQLENALQKAKQDM- 359
Cdd:pfam06160 376 IEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKS--NLPGLPESYLDYFFDVSDEIEDLADELNEVPLNMd 453
|
250
....*....|....*
gi 124249090 360 --ARQLREYQDLMNT 372
Cdd:pfam06160 454 evNRLLDEAQDDVDT 468
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
102-372 |
3.69e-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: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 102 QALEQRNQL-LETRWSFLQGQ-----GSATFDlshHYETFQGRL--QEELRKVSQERGQLE---ANLLQVLEKVEEFRVR 170
Cdd:TIGR02168 633 NALELAKKLrPGYRIVTLDGDlvrpgGVITGG---SAKTNSSILerRREIEELEEKIEELEekiAELEKALAELRKELEE 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 171 YEDEISKR----TDLEFTFVQLKKDLD---AECLRRTELETKLKGLQGFLELMRTVYEQELKDLTAQVKDVsvtvgldsr 243
Cdd:TIGR02168 710 LEEELEQLrkelEELSRQISALRKDLArleAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA--------- 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 244 chidlsgivEEVKAQYDAIAARSLEEAEAYSRSQLEERAArsaefgnsLQSSRCEIADLNVRIQKLRSQIVSVKSHCLKL 323
Cdd:TIGR02168 781 ---------EAEIEELEAQIEQLKEELKALREALDELRAE--------LTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 124249090 324 EENIKVAEEQGELA------FQDAKDKM----AQLENALQKAKQDMARQLREYQDLMNT 372
Cdd:TIGR02168 844 EEQIEELSEDIESLaaeieeLEELIEELeselEALLNERASLEEALALLRSELEELSEE 902
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
79-284 |
3.76e-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: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 79 QKNQEKEEMKALNDKFASLIGKVQALEQRNQLLETRWSFLQGQGSATFDLSHHYETFQGRLQEELRKVSQERGQLEANLL 158
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 159 QVLEKVEEFRVRYEDEISKRTDLEF-------TFVQLKKDLDAECLRRTELETKLKGLQGFLELMRTVYEQELKDLT-AQ 230
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEqletlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeAE 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 124249090 231 VKDVSVTVGLDSRCHIDLSGIVEEVKAQYDAIAARS--LEEAEAYSRSQLEERAAR 284
Cdd:TIGR02168 435 LKELQAELEELEEELEELQEELERLEEALEELREELeeAEQALDAAERELAQLQAR 490
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
75-381 |
3.95e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 75 AVQQQKNQEKEEMKALNDKFASLIGKVQALEQRNQLLETRwsflqgQGSATFDLShhyetfqgRLQEELRKVSQERGQLE 154
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLE------LEELELELE--------EAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 155 ANLLQVLEKVEEFRVRYEDEISKRTDLEFTFVQLKKDLDAECLRRTELETKLKGLqgflelmrtvyEQELKDLTAQvkdv 234
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA-----------EAELAEAEEA---- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 235 svtvgldsrchidlsgiVEEVKAQYDAIAARSLEEAEAYSRSQLEERAARSAefgnsLQSSRCEIADLNVRIQKLRSQIV 314
Cdd:COG1196 367 -----------------LLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-----LEELEEAEEALLERLERLEEELE 424
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124249090 315 SVKSHclklEENIKVAEEQGELAFQDAKDKMAQLENALQKAKQDMARQLREYQDLMNTKLALDIEIA 381
Cdd:COG1196 425 ELEEA----LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
136-381 |
1.33e-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: 44.66 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 136 QGRLQEELRKVSQERGQLEANLL-----QVLEKVEEFRVRYEDEISKRTDLEFTFVQLKKDLDAECLRRTELETKLKGLQ 210
Cdd:TIGR02168 208 QAEKAERYKELKAELRELELALLvlrleELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 211 GFL----------ELMRTVYEQELKDLTAQVKDVSVTVGLDSRCHIDLSGIVEEVKAQYDAIAAR--SLEEAEAYSRSQL 278
Cdd:TIGR02168 288 KELyalaneisrlEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEleSLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 279 EERAARSAEFGNSLQSSRCEIADLNVRIQKLRSQIVSVKSHCLKLEENI-KVAEEQGELAFQDAKDKMAQLENALQKAKQ 357
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRReRLQQEIEELLKKLEEAELKELQAELEELEE 447
|
250 260
....*....|....*....|....
gi 124249090 358 DMARQLREYQDLMNTKLALDIEIA 381
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELE 471
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
252-393 |
4.19e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 252 VEEVKAQYDAIAARSLEEAEAYSRSQLEERAARS--AEFGNSLQSSRCEIADLNVRIQKLRSQIVSVKSHCLKLEENIKV 329
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAelARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124249090 330 AEEQGELA---FQDAKDKMAQLENALQKAKQDMARQLREYQDLMNTKLALDIEIATYHKLMEGEESR 393
Cdd:COG1196 342 LEEELEEAeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
75-371 |
9.46e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 75 AVQQQKNQEKEEMKALNDKFASLIGKVQALEQRNQLLETRWSFLQGQGS----ATFDLSHHY-ETFQGRLQEELRKVSQE 149
Cdd:TIGR02169 727 QLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHkleeALNDLEARLsHSRIPEIQAELSKLEEE 806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 150 RGQLEANLL---QVLEKVEEFRVRYEDEI----SKRTDLEFTFVQLKKDLDAECLRRTELETKLKGLQGFLElmrtVYEQ 222
Cdd:TIGR02169 807 VSRIEARLReieQKLNRLTLEKEYLEKEIqelqEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR----DLES 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 223 ELKDLTAQvkdvsvtvgldsrchidlsgiVEEVKAQYDAiAARSLEEAEAySRSQLEERAARSAEFGNSLQSSRCEIADL 302
Cdd:TIGR02169 883 RLGDLKKE---------------------RDELEAQLRE-LERKIEELEA-QIEKKRKRLSELKAKLEALEEELSEIEDP 939
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124249090 303 NVRIQKLRSQIVS---VKSHCLKLEENIKVAEEQGELAFQDAKDKMAQLeNALQKAKQDMARQLREYQDLMN 371
Cdd:TIGR02169 940 KGEDEEIPEEELSledVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKRAKLEEERKAILERIE 1010
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
210-365 |
1.41e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 210 QGFLELMRTVYEQELKDLTAQVKDVSVTVGLDSRCHIDLSGIVEEVKAQYDAIAA-----RSLEEAEAYSRSQLEERAAR 284
Cdd:PRK09039 41 QFFLSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAersrlQALLAELAGAGAAAEGRAGE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 285 -SAEFGNSLQSS---RCEIADLNVRIQKLRSQIVSVKShCLKLEENiKVAEEQGELAfqdakDKMAQLENALQKAKQDMA 360
Cdd:PRK09039 121 lAQELDSEKQVSaraLAQVELLNQQIAALRRQLAALEA-ALDASEK-RDRESQAKIA-----DLGRRLNVALAQRVQELN 193
|
170
....*....|..
gi 124249090 361 R-------QLRE 365
Cdd:PRK09039 194 RyrseffgRLRE 205
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
133-372 |
1.85e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.59 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 133 ETFQgRLQEELRKVSQERGQLEanllqvLEKVEEfrvrYEDEISKRTDleftfvQLKKDLDAECLRRTELETKLKGLQGF 212
Cdd:PRK04778 256 KEIQ-DLKEQIDENLALLEELD------LDEAEE----KNEEIQERID------QLYDILEREVKARKYVEKNSDTLPDF 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 213 LELMRTVYeQELKDLTAQVK--------DVSVTVGLDSRchidlsgiVEEVKAQYDAIAARSLEEAEAYS---------R 275
Cdd:PRK04778 319 LEHAKEQN-KELKEEIDRVKqsytlnesELESVRQLEKQ--------LESLEKQYDEITERIAEQEIAYSelqeeleeiL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 276 SQLEERAARSAEFGNSLQSSRCEIADLNVRIQKLRSQIVSVKSHCLKLeeNIKVAEEQGELAFQDAKDKMAQLENALQKA 355
Cdd:PRK04778 390 KQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEKS--NLPGLPEDYLEMFFEVSDEIEALAEELEEK 467
|
250 260
....*....|....*....|
gi 124249090 356 KQDM---ARQLREYQDLMNT 372
Cdd:PRK04778 468 PINMeavNRLLEEATEDVET 487
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
199-395 |
3.07e-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: 40.04 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 199 RTELETKLKGLQGFLELMrtvyeQELKDLTAQVKDVSVTVGLDSrchidlsgiVEEVKAQYDAiaarsLEEAEAYSRSQL 278
Cdd:TIGR02168 195 LNELERQLKSLERQAEKA-----ERYKELKAELRELELALLVLR---------LEELREELEE-----LQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 279 EERAARSAEFGNSLQSSRCEIADLNVRIQKLRSQIVSVKSHCLKLEENIKVAEEQGELAFQDAKDKMAQLENALQK---A 355
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKldeL 335
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 124249090 356 KQDMARQLREYQDLMNTKLALDIEIATYHKLMEGEESRMD 395
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
135-367 |
3.11e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 135 FQGRLQEELRKVSQERGQLEANLLQVLEKVEEFRVRYEDEISKRTDLEFTFVQLKKDLDAECLRRTELETKLKGLQGFLE 214
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 215 LMRtvYEQELKDLTAQVKDvsvtvgLDSRchidlsgiVEEVKAQYDAIAARsLEEAEAYSRSQLEERAARSAEFGNSLQS 294
Cdd:COG4717 127 LLP--LYQELEALEAELAE------LPER--------LEELEERLEELREL-EEELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124249090 295 SRCEIADLNVRIQKLRSQIVsvkshclKLEENIKVAEEQGElafqDAKDKMAQLENALQkaKQDMARQLREYQ 367
Cdd:COG4717 190 TEEELQDLAEELEELQQRLA-------ELEEELEEAQEELE----ELEEELEQLENELE--AAALEERLKEAR 249
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
107-350 |
7.14e-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: 38.93 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 107 RNQLLETRWSFLQGQGSATFDLSHHYETFQGRLQEELRKVSQERgqLEANLLQVLEKVEEFRVRYEDEISKRTD-LEFTF 185
Cdd:pfam05483 547 RDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMK--ILENKCNNLKKQIENKNKNIEELHQENKaLKKKG 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 186 VQLKKDLDAECLRRTELETKLKGLQGFLELMRTVYEQELKD-------LTAQVKDVSVTVG--------LDSRCH---ID 247
Cdd:pfam05483 625 SAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDkkiseekLLEEVEKAKAIADeavklqkeIDKRCQhkiAE 704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 248 LSGIVEEVKAQYDAIAARSLEEAEAYSRSQLEERAARSAefgnslqssrceiadLNVRIQKLRSQIVSVKshclkleENI 327
Cdd:pfam05483 705 MVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAA---------------LEIELSNIKAELLSLK-------KQL 762
|
250 260
....*....|....*....|...
gi 124249090 328 KVAEEQGELAFQDAKDKMAQLEN 350
Cdd:pfam05483 763 EIEKEEKEKLKMEAKENTAILKD 785
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
139-370 |
7.20e-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: 39.00 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 139 LQEELRKVSQERGQLEANLLQVLEKVEEFRVRYEDEISKRTDLEFTFVQLKKDLDAECLRRTELETKLKGLQgflelmrt 218
Cdd:pfam01576 389 LQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLS-------- 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 219 vyeQELKDLTAQVKDVSVTVGLDSRCHIDLSGIVeevkaqydaiaaRSLEEAEAYSRSQLEERAARSAEFGNSLQSSRCE 298
Cdd:pfam01576 461 ---KDVSSLESQLQDTQELLQEETRQKLNLSTRL------------RQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQ 525
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124249090 299 IADLNVRIQKLRSQIVSvkshclkLEENIKVAEEQGELAFQDAKDKMAQLENaLQKAKQdmaRQLREYQDLM 370
Cdd:pfam01576 526 LSDMKKKLEEDAGTLEA-------LEEGKKRLQRELEALTQQLEEKAAAYDK-LEKTKN---RLQQELDDLL 586
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
85-346 |
8.42e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 38.76 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 85 EEMK-----ALNDKFASLI------GKVQaLEQRNQLLET----RWSFLQGQGSATFDLSHHYETFQGRLQEELRKVS-Q 148
Cdd:PRK05771 4 VRMKkvlivTLKSYKDEVLealhelGVVH-IEDLKEELSNerlrKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSvK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 149 ERGQLEANLLQVLEKVEEfrvRYEDEISKRTDLEftfvQLKKDLDAECLRrteletkLKGLQGF-LELmrtVYEQELKDL 227
Cdd:PRK05771 83 SLEELIKDVEEELEKIEK---EIKELEEEISELE----NEIKELEQEIER-------LEPWGNFdLDL---SLLLGFKYV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249090 228 TAQVKDVSVTVGLDSRCHIDLSGIVEEVKA-QYDAIAARSLEEAEAYSRSQLEERAARSAEFGNS------LQSSRCEIA 300
Cdd:PRK05771 146 SVFVGTVPEDKLEELKLESDVENVEYISTDkGYVYVVVVVLKELSDEVEEELKKLGFERLELEEEgtpselIREIKEELE 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 124249090 301 DLNVRIQKLRSQIVSVKShclKLEENIKVAEEQ--GELAFQDAKDKMA 346
Cdd:PRK05771 226 EIEKERESLLEELKELAK---KYLEELLALYEYleIELERAEALSKFL 270
|
|
| |
