|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
134-749 |
1.84e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 134 QEFESEAQRREHEFQLraddlsntvltheLKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEA- 212
Cdd:COG1196 216 RELKEELKELEAELLL-------------LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELe 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 213 --MKDARIKDLEKKLHSVQLAKKKAEETFRRKHEELDRQAREKDtVLAAVKGAHAEQLQTLDAKVLELQFRCETLEGQLR 290
Cdd:COG1196 283 leEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA-ELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 291 RAEWRQAEDSKERNSLTDKEFGDRSTcvlsmywhsvitsvpsglpsrfREDAAALKAAWDAQIAQMSKEAVSKDLQIQAL 370
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEE----------------------LLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 371 QEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLgldwqrrcddiecnqIQRSETLIQGLTKARDQVAAKLQ 450
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL---------------LELLAELLEEAALLEAALAELLE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 451 ETERALHKQETLLKAVSLERDQAMETLRTHGLlpgqEAQVPPQPHEGEIRTDSPSSEIQRLQEQNAGLRNAV----SQMR 526
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLL----AGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVveddEVAA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 527 KEMEMLSGHLP----FAQSEERSNANPEPKAGEDSAPPDYVLALEAEMQNLKHELKALEEQLQGtgepvkTSMATADPHH 602
Cdd:COG1196 561 AAIEYLKAAKAgratFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG------RTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 603 GAHNSAEAADAApadqtlitLALRKLGDRVHLLNLLVTQLKKKLRQKPLELVAVQQEIPSEVDQVHLEVLELQKQVAELR 682
Cdd:COG1196 635 ALRRAVTLAGRL--------REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 683 KHLKMTQPQGEPSYIKQLQREGLAD---WHPMGMEDQTESPTFLQEGAQPPQTTSVSHLQRKLKDAARKI 749
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEaerEELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
140-537 |
7.26e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 7.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 140 AQRREHEFQLRA--DDLSN-TVLTHELKVKLLNKELQAlkeagaqateslQKAEsEHIELERKLQDHARELQDLeamkda 216
Cdd:TIGR02168 172 ERRKETERKLERtrENLDRlEDILNELERQLKSLERQA------------EKAE-RYKELKAELRELELALLVL------ 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 217 RIKDLEKKLHSVQLAKKKAEEtfrrKHEELDRQAREKDTVLAAVKGAHAE---QLQTLDAKVLELQFRCETLEGQLRRAE 293
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEE----ELEELTAELQELEEKLEELRLEVSEleeEIEELQKELYALANEISRLEQQKQILR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 294 WRQAEDSKERNSLTDKEFGDRSTcvlsmywhsvitsvpsglpsrfREDAAALKAAWDAQIAQMSKEAVSKDLQIQALQEE 373
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESK----------------------LDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 374 EMKLKAQVAKSQQDIDRYKQ--------------QLSLAVEREQSLEREQVQLGLDWQRRCDDIECNQIQRSETLIQGLT 439
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSkvaqlelqiaslnnEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 440 KARDQVAAKLQETERALHKQETLLKAVSLERDQAMETLRTHGLlpgqeaqvppqphegeiRTDSpsseIQRLQEQNAGLR 519
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA-----------------RLDS----LERLQENLEGFS 505
|
410
....*....|....*...
gi 1958663250 520 NAVSQMRKEMEMLSGHLP 537
Cdd:TIGR02168 506 EGVKALLKNQSGLSGILG 523
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-475 |
1.96e-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: 58.53 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 173 QALKEAGAQATESLQKAESEHIELERKLQDHaRELQDLEAMKDARIKDLEKKLHSVQLAKKKAEETFRRKHEELDRQARE 252
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKEL-EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 253 kDTVLAAVKGAHAEQLQTLDAKVLELQFRCETLEGQLRRAE-----WRQAEDSKE-RNSLTDKEFGDRSTCVLSMywhsv 326
Cdd:TIGR02168 756 -LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKeelkaLREALDELRaELTLLNEEAANLRERLESL----- 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 327 itsvpsglpSRFREDAAALKAAWDAQIAQMSKEAVSKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLE 406
Cdd:TIGR02168 830 ---------ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 407 REQvqlgldwqrrcDDIEcNQIQRSETLIQGLTKARDQVAAKLQETE-RALHKQETLLKAVSLERDQAME 475
Cdd:TIGR02168 901 EEL-----------RELE-SKRSELRRELEELREKLAQLELRLEGLEvRIDNLQERLSEEYSLTLEEAEA 958
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
126-452 |
6.63e-08 |
|
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: 57.05 E-value: 6.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 126 LDSSTELLQEFESEAQRREHeFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHAR 205
Cdd:pfam15921 526 VDLKLQELQHLKNEGDHLRN-VQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRL 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 206 ELQDLEAM---KDARIKDLEKKLHSVQLAKKKAEETFRRKHEELDRQAREKDTVLAAVKGAHAEqLQTL--DAKVLELQF 280
Cdd:pfam15921 605 ELQEFKILkdkKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNE-LNSLseDYEVLKRNF 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 281 RCET---------LEGQLRRAewrQAEDSKERNSLTDKEFGDRSTCVLSMYWHSVITSVPSGLPS-----RFREDAAALK 346
Cdd:pfam15921 684 RNKSeemetttnkLKMQLKSA---QSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDAlqskiQFLEEAMTNA 760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 347 AAWDAQIAQmSKEAVSKDLQIQALQEEEMKLKAQVAKSQQdiDRYKQQLSlavEREQSLEREQVQLGldwqrRCDDIecn 426
Cdd:pfam15921 761 NKEKHFLKE-EKNKLSQELSTVATEKNKMAGELEVLRSQE--RRLKEKVA---NMEVALDKASLQFA-----ECQDI--- 826
|
330 340
....*....|....*....|....*.
gi 1958663250 427 qIQRSEtliqgltkaRDQVAAKLQET 452
Cdd:pfam15921 827 -IQRQE---------QESVRLKLQHT 842
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
195-584 |
2.07e-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: 55.45 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 195 ELERKLqDHARElqDLEAMKDArIKDLEKKLHSVQLAKKKAEEtFRRKHEELdrqaREKD-TVLAAVKGAHAEQLQTLDA 273
Cdd:TIGR02168 176 ETERKL-ERTRE--NLDRLEDI-LNELERQLKSLERQAEKAER-YKELKAEL----RELElALLVLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 274 KVLELQFRCETLEGQLRRAEwrqaedskernsltdkefgdrstcvlsmywhsvitsvpsglpsrfredaaalkaawdAQI 353
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELE---------------------------------------------------------EKL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 354 AQMSKEAVSKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAverEQSLEREQVQLGLDWQRRCDDIEcnQIQRSET 433
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL---ERQLEELEAQLEELESKLDELAE--ELAELEE 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 434 LIQGLTKARDQVAAKLQETERALHKQETLLKavslERDQAMETLRthgllpgqeaqvppqphegeirtdspsSEIQRLQE 513
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLE----ELEEQLETLR---------------------------SKVAQLEL 393
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958663250 514 QNAGLRNAVSQMRKEMEMLSGHLPfAQSEERSNANPEPKAGEDSAPPDYVLALEAEMQNLKHELKALEEQL 584
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRE-RLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL 463
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
197-586 |
4.20e-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: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 197 ERKLqDHARE----LQDLEAMKDARIKDLEKKlhsvqlaKKKAEetfrrKHEELDRQAREKDTVLAAVKGAHAE-QLQTL 271
Cdd:COG1196 178 ERKL-EATEEnlerLEDILGELERQLEPLERQ-------AEKAE-----RYRELKEELKELEAELLLLKLRELEaELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 272 DAKVLELQFRCETLEGQLRRAEwrqaedskernsltdkefgdrstcvlsmywhsvitsvpsglpsrfredaaalkaawdA 351
Cdd:COG1196 245 EAELEELEAELEELEAELAELE---------------------------------------------------------A 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 352 QIAQMSKEAVSKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLgldwQRRCDDIEcNQIQRS 431
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL----EEELEELE-EELEEL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 432 ETLIQGLTKARDQVAAKLQETERALHKQETLLKAVSLERDQAMETLRTHgllpgqeaqvppqphegEIRTDSPSSEIQRL 511
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-----------------LRAAAELAAQLEEL 405
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958663250 512 QEQNAGLRNAVSQMRKEMEMLsghlpfAQSEERSNANPEPKAGEDSAPPDYVLALEAEMQNLKHELKALEEQLQG 586
Cdd:COG1196 406 EEAEEALLERLERLEEELEEL------EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
170-528 |
7.86e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 170 KELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEAMKDARIKDLEKKLHSVQLAKKKAE-ETFRRKHEELDR 248
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERlEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 249 QAREKDTVLAAVKGAHAE--------------QLQTLDAKVLELQFRCETLEGQLRRAEWRQAEDSKERNSLTDKEFGDR 314
Cdd:COG4717 161 LEEELEELEAELAELQEEleelleqlslateeELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 315 ----------------STCVLSMYWHSVITSVPS---------GLPSRFREDAAALKAAWDAQIAQMSKEAVSKDLQIQA 369
Cdd:COG4717 241 leerlkearlllliaaALLALLGLGGSLLSLILTiagvlflvlGLLALLFLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 370 LQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLgldwqrrcdDIECNQIQRSETLIQGLTKARDQVAAKL 449
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL---------QLEELEQEIAALLAEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958663250 450 QETERAlHKQETLLKAVSLERDQAMETLRtHGLLPGQEAQVPPQPHEGEIRTDSPSSEIQRLQEQNAGLRNAVSQMRKE 528
Cdd:COG4717 392 EQAEEY-QELKEELEELEEQLEELLGELE-ELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-581 |
1.05e-06 |
|
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: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 3 ELRHQHKLMLQEHRLELERVHSDKNSELNHQREQYENLKWKLERKLKELDGELALQRQVHKTLEEIYSLLSEvflnvcyR 82
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA-------E 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 83 LVALQARgcaripvmpvmLALTERRtpwdsslpvdvmkqewvwLDSSTELLQEFESEAQR---REHEFQLRADDLSNTVL 159
Cdd:COG1196 290 EYELLAE-----------LARLEQD------------------IARLEERRRELEERLEEleeELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 160 THELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLE---AMKDARIKDLEKKLHSVQLAKKKAE 236
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALraaAELAAQLEELEEAEEALLERLERLE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 237 ETFRRKHEELDRQAREKDTVLAAVKGA------HAEQLQTLDAKVLELQFRCETLEGQLRRAEWRQAEDSKERNSLTD-- 308
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAaeeeaeLEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEae 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 309 --------------KEFGDRSTCVLSMYWHSVITSVPSGLPSRFREDAAALKAAWDAQIAQMSKEAVSKDL-QIQALQEE 373
Cdd:COG1196 501 adyegflegvkaalLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgRATFLPLD 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 374 EMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQ----LGLDWQRRCDDIECNQIQRSETLIQGLTKARDQVAAKL 449
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLgdtlLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 450 QETERALHKQETLLKAVSLERDQAMETLRTHGLlpgqeaqvppQPHEGEIRTDSPSSEIQRLQEQNAGLRNAVSQMRKEM 529
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEEL----------ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL 730
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1958663250 530 EMLSGHLPFAQSEErsnANPEPKAGEDSAPPDYVLA-LEAEMQNLKHELKALE 581
Cdd:COG1196 731 EAEREELLEELLEE---EELLEEEALEELPEPPDLEeLERELERLEREIEALG 780
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
139-592 |
3.22e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 139 EAQRREHEFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEAMKDARI 218
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 219 KDLEKKLHSVQLAKKKAEetfRRKHEELDRQAREKDTVLAAVKGAHAEQlqtldaKVLELQFRCEtlegQLRRAE--WRQ 296
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAA---KKKADEAKKKAEEKKKADEAKKKAEEAK------KADEAKKKAE----EAKKAEeaKKK 1465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 297 AEDSKERNSLTDKEFGDRSTcvlsmywhsviTSVPSGLPSRFREDAAALKAAWDAQIAQMSKEAVSKDLQIQALQEEEMK 376
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKA-----------DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK 1534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 377 lKAQVAKSQQDIdRYKQQLSLAVEREQSLEREQVQlgldWQRRCDDIECNQIQRSETLIQgLTKARDQVAAKLQETERAL 456
Cdd:PTZ00121 1535 -KADEAKKAEEK-KKADELKKAEELKKAEEKKKAE----EAKKAEEDKNMALRKAEEAKK-AEEARIEEVMKLYEEEKKM 1607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 457 HKQEtlLKAVSLERDQAMETLRTHgllpgQEAQVPPQPHEGEIRTDSPSSEIQRLQEQNAGLRNAVSQMRKEMEMLSGHL 536
Cdd:PTZ00121 1608 KAEE--AKKAEEAKIKAEELKKAE-----EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958663250 537 PFAQSEERSNANPEPKAGEDSAPPDYVLALEAEMQNLKHELKALEEQLQGTGEPVK 592
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-681 |
3.51e-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: 51.21 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 1 MEELRHQHKLMLQEHRLELERV---HSDKNSELNHQREQYENLKwkleRKLKELDGELALQRQVHKTLEEIYSLLSEVFL 77
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELrleVSELEEEIEELQKELYALA----NEISRLEQQKQILRERLANLERQLEELEAQLE 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 78 NVCYRLVALQARgcaripvmpvmLALTERRtpwdsslpVDVMKQEwvwLDSSTELLQEFESEAQ---RREHEFQLRADDL 154
Cdd:TIGR02168 327 ELESKLDELAEE-----------LAELEEK--------LEELKEE---LESLEAELEELEAELEeleSRLEELEEQLETL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 155 SNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLE-AMKDARIKDLEKKLHSVQLAKK 233
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALE 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 234 KAEETFRRKHEELD------RQAREKDTVLAAVKGAHaEQLQTLDAKVLELQFRCETLEGQLR-----RAEWRQA----- 297
Cdd:TIGR02168 465 ELREELEEAEQALDaaerelAQLQARLDSLERLQENL-EGFSEGVKALLKNQSGLSGILGVLSelisvDEGYEAAieaal 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 298 ---------EDS----KERNSLTDKEFGDRSTCVLSMYWHSVITSvpSGLPSRFREDAAALKAAWDAQIAQ--------- 355
Cdd:TIGR02168 544 ggrlqavvvENLnaakKAIAFLKQNELGRVTFLPLDSIKGTEIQG--NDREILKNIEGFLGVAKDLVKFDPklrkalsyl 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 356 MSKEAVSKDLQIQALQEEEMKLKAQVAKSQQDIDR--------YKQQLSLAVEREQSLE--REQVQLGldwQRRCDDIEc 425
Cdd:TIGR02168 622 LGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRpggvitggSAKTNSSILERRREIEelEEKIEEL---EEKIAELE- 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 426 NQIQRSETLIQGLTKARDQVAAKLQETERALHKQETLLKAVSLERDQAMETLRTHGL----LPGQEAQVPPQPHEGEIRT 501
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKelteLEAEIEELEERLEEAEEEL 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 502 DSPSSEIQRLQEQNAGLRNAVSQMRKEMEMLSGHLpFAQSEERSNANPEPKAGEDSAPpdyvlALEAEMQNLKHELKALE 581
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAEL-TLLNEEAANLRERLESLERRIA-----ATERRLEDLEEQIEELS 851
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 582 EQLQGTGEPVKTSMATADPHHGAHNSAEAADAAPADQ-TLITLALRKLGDRVHLLNLLVTQLKKKLRQKPLELVAVQQEI 660
Cdd:TIGR02168 852 EDIESLAAEIEELEELIEELESELEALLNERASLEEAlALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
730 740
....*....|....*....|.
gi 1958663250 661 psevDQVHLEVLELQKQVAEL 681
Cdd:TIGR02168 932 ----EGLEVRIDNLQERLSEE 948
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
126-430 |
4.45e-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: 50.83 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 126 LDSSTELLQEFESEAQRREHEFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHAR 205
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 206 ELQDLEAmkdaRIKDLEKKLhsvqlakKKAEETFRRKHEELDRQAREKDTVlaavkgahAEQLQTLDAKVLELQFRCETL 285
Cdd:TIGR02168 783 EIEELEA----QIEQLKEEL-------KALREALDELRAELTLLNEEAANL--------RERLESLERRIAATERRLEDL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 286 EGQLRRAEWRQAEDSKERNSLTDKEFGDRSTCVLsmywHSVITSVPSGLPSRFREDaaalKAAWDAQIAQMSKEAVSKDL 365
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEA----LLNERASLEEALALLRSE----LEELSEELRELESKRSELRR 915
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958663250 366 QIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVERE----QSLEREQVQLGLDWQRRCDDIEcNQIQR 430
Cdd:TIGR02168 916 ELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTleeaEALENKIEDDEEEARRRLKRLE-NKIKE 983
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
137-744 |
6.11e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 137 ESEAQRREHE-FQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEAMKD 215
Cdd:PTZ00121 1239 AEEAKKAEEErNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 216 ARIKDLEKKLHSVQLAKKKAEETFRRKHEELDRQAREKDTVLAAVKGAHAEQLQTLDA--KVLELQFRCETLEgQLRRAE 293
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkKADAAKKKAEEKK-KADEAK 1397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 294 WRQAEDSKERNSLTDKEFGDRSTcvlsmywhsviTSVPSGLPSRFREDAAALKAAWDAQIAQMSKEAVSKDLQIQALQEE 373
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKA-----------DEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA 1466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 374 EMKLKAQVAKSQQDIDRYKQQLSLAVErEQSLEREQVQLGLDWQRRCDDI-ECNQIQRSETLIQGLTKARDQVAAKLQET 452
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADEAkKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 453 ERA--LHKQETLLKAVSL---------ERDQAMETLRTHGLLPGQEAQVPPQPHEGEIRTDSPSSEIQRLQEQnaglRNA 521
Cdd:PTZ00121 1546 KKAdeLKKAEELKKAEEKkkaeeakkaEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA----KIK 1621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 522 VSQMRKEMEM--LSGHLPFAQSEERSNANPEPKAGEDSAPPDYVLALEAEMQNLK-HELKALEEQLQGTGEPVKTSMATA 598
Cdd:PTZ00121 1622 AEELKKAEEEkkKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKaEEAKKAEEDEKKAAEALKKEAEEA 1701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 599 dphhgahnsaeaadaapadqtlitlalRKlgdrvhllnllVTQLKKKL---RQKPLELVAVQQEIPSEVDQVHLEVLELQ 675
Cdd:PTZ00121 1702 ---------------------------KK-----------AEELKKKEaeeKKKAEELKKAEEENKIKAEEAKKEAEEDK 1743
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958663250 676 KQVAELRKHlkmtqpQGEPSYIKQLQREGladwHPMGMEDQTESPTFLQEGAQPPQTTSVSHLQRKLKD 744
Cdd:PTZ00121 1744 KKAEEAKKD------EEEKKKIAHLKKEE----EKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
214-589 |
7.79e-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: 50.06 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 214 KDARIKDLEKKLHSVQ---LAKKKAEETFRRKHEELDRQAREKDTVLAAVKGAHAEQlqtlDAKVLELQFRCETLEGQLR 290
Cdd:TIGR02168 675 RRREIEELEEKIEELEekiAELEKALAELRKELEELEEELEQLRKELEELSRQISAL----RKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 291 RAEWRQAEDSKERNSLTDKEFGDRSTcvlsmywhsvitsvpsglpsrfREDAAALKAAWDAQIAQMSKEAVSKDLQIQAL 370
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEE----------------------LAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 371 QEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLGLdwqrrcddiecnQIQRSETLIQGLTKARDQVAAKLQ 450
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE------------DIESLAAEIEELEELIEELESELE 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 451 ETERALHKQETLLKAVSLERDQAMETLRTHgllpgqeaqvppqphegeirtdspSSEIQRLQEQNAGLRNAVSQMRKEME 530
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELREL------------------------ESKRSELRRELEELREKLAQLELRLE 932
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958663250 531 MLSGHLpfAQSEERSNANPEPKAGEDSAPPDyvlALEAEMQNLKHELKALEEQLQGTGE 589
Cdd:TIGR02168 933 GLEVRI--DNLQERLSEEYSLTLEEAEALEN---KIEDDEEEARRRLKRLENKIKELGP 986
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
168-309 |
1.93e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.23 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 168 LNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEamkdARIKDLEKKLHSVQLAK-----KKAEETFRRK 242
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE----ARIKKYEEQLGNVRNNKeyealQKEIESLKRR 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958663250 243 HEELDRQAREKDTVLAAVKGAHAEQLQTLDAKVLELQFRCETLEGQLRRAEWRQAEDSKERNSLTDK 309
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
131-308 |
2.89e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 131 ELLQEFESEAQRREHefqLRADDLSNTVLTHELKVKLLNKELQALKEAgaqatesLQKAESEHIELERKLQDHARELQDL 210
Cdd:COG4913 259 ELAERYAAARERLAE---LEYLRAALRLWFAQRRLELLEAELEELRAE-------LARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 211 EAMKDA----RIKDLEKKLHSVQLAKKKAEetfrRKHEELDRQAREKDTVLAAVKGAHAEQLQTLDAKVLELQFRCETLE 286
Cdd:COG4913 329 EAQIRGnggdRLEQLEREIERLERELEERE----RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE 404
|
170 180
....*....|....*....|..
gi 1958663250 287 GQLRRAEWRQAEDSKERNSLTD 308
Cdd:COG4913 405 EALAEAEAALRDLRRELRELEA 426
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-261 |
4.43e-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: 47.74 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 2 EELRHQHKLM---LQEHRLELERVhSDKNSELNHQREQYENLKWKLERKLKELDGELA--------LQRQV--------- 61
Cdd:TIGR02168 722 EELSRQISALrkdLARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLEEAEEELAeaeaeieeLEAQIeqlkeelka 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 62 ----HKTLEEIYSLLSEVFLNVCYRLVALQARgCARIPVMPVMLALTERRTPWDSSLPVDVMKQEWVWLDSSTELLQEFE 137
Cdd:TIGR02168 801 lreaLDELRAELTLLNEEAANLRERLESLERR-IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 138 ---SEAQRREHEFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHAR-ELQDLEAM 213
Cdd:TIGR02168 880 nerASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEAL 959
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958663250 214 K----------DARIKDLEKKLHS---VQLAkkkAEETFRRKHEELDRQAREKDTVLAAVK 261
Cdd:TIGR02168 960 EnkieddeeeaRRRLKRLENKIKElgpVNLA---AIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
10-316 |
5.10e-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: 47.37 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 10 LMLQEHRLELERVHSDKNSELNHQ--------REQYENLKWK--LERKLKELDGELALQRQVhktLEEIYSLLSEVFLnv 79
Cdd:TIGR02169 191 LIIDEKRQQLERLRREREKAERYQallkekreYEGYELLKEKeaLERQKEAIERQLASLEEE---LEKLTEEISELEK-- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 80 cyRLVALQARgcaripvmpvmlalterrtpwdsslpvdvmkqewvwLDSSTELLQEFESEAQRReheFQLRADDLSNTVL 159
Cdd:TIGR02169 266 --RLEEIEQL------------------------------------LEELNKKIKDLGEEEQLR---VKEKIGELEAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 160 THELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEAMKDARIKDLEKKLHSVQLAKKKAEETF 239
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 240 R-------------RKHEELDRQAREKDTVLAAVKGAHAE---QLQTLDAKVLELQFRCETLEGQLRRAEWRQAEDSKER 303
Cdd:TIGR02169 385 DelkdyrekleklkREINELKRELDRLQEELQRLSEELADlnaAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
330
....*....|...
gi 1958663250 304 NSLTDKEFGDRST 316
Cdd:TIGR02169 465 SKYEQELYDLKEE 477
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
170-247 |
1.24e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 44.13 E-value: 1.24e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958663250 170 KELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEAMKdARIKDLEKKLHSVQLAKKKAEETFRRKHEELD 247
Cdd:pfam13851 47 KLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLK-ARLKVLEKELKDLKWEHEVLEQRFEKVERERD 123
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-518 |
1.44e-04 |
|
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: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 2 EELRHQHKLMLQEHRLELERVhSDKNSELNHQREQYENLKWKLER---KLKELDGELALQRQVHKTLEEIYSLLSEVFLN 78
Cdd:COG1196 277 EELELELEEAQAEEYELLAEL-ARLEQDIARLEERRRELEERLEEleeELAELEEELEELEEELEELEEELEEAEEELEE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 79 VCYRLVALQARgcaripvmpvMLALTERRTPWDSSLpvDVMKQEWVWLDSSTELLQEFESEAQRREHEFQLRADDLSNTV 158
Cdd:COG1196 356 AEAELAEAEEA----------LLEAEAELAEAEEEL--EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 159 LTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEAmKDARIKDLEKKLHSVQLAKKKAEEt 238
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA-ALAELLEELAEAAARLLLLLEAEA- 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 239 frrKHEELDRQAREKDTVLAAVKGAHAEQLQTLDAKVLELQFRCETLEGQLRRAEWRQAEDSKERNSLTDKEFGDRSTCV 318
Cdd:COG1196 502 ---DYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLP 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 319 LSMYWHSVITSVP-SGLPSRFREDAAALKAAWDAQIAQMSKEAVSKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSL 397
Cdd:COG1196 579 LDKIRARAALAAAlARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 398 AVEREQSLEREQVQLGLDWQRRCDDIECNQIQRSETLIQGLTKARDQVAAKLQETERALHKQETLLKAVSLERDQAMETL 477
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1958663250 478 RTHGLLPGQEAQVPPQPHEGEIRTDSPSSEIQRLQEQNAGL 518
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
126-407 |
1.55e-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: 45.83 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 126 LDSSTELLQEFESEAQRREHEFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHAR 205
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 206 ELQ--------------DLEAMK----------------------DARIKDLEKKLHSVQLAKKKAEETFRRKHEEL--- 246
Cdd:TIGR02169 766 RIEeleedlhkleealnDLEARLshsripeiqaelskleeevsriEARLREIEQKLNRLTLEKEYLEKEIQELQEQRidl 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 247 -DRQAREKDTV--LAAVKGAHAEQLQTLDAKVLELQFRCETLEGQLRRAEWRQAEDSKERNSLTDKEFGDRSTCVLSMYW 323
Cdd:TIGR02169 846 kEQIKSIEKEIenLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 324 HSVITSVPSGLPSRFREDAAALKAAWDAQIAQMSKEAVSKDlqIQALQEEEMKLKAQVAKSQQDIDRYKQQLS-LAVERE 402
Cdd:TIGR02169 926 LEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEE--IRALEPVNMLAIQEYEEVLKRLDELKEKRAkLEEERK 1003
|
....*
gi 1958663250 403 QSLER 407
Cdd:TIGR02169 1004 AILER 1008
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
486-582 |
1.90e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.23 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 486 QEAQVPPQPHEGEIRtdSPSSEIQRLQEQNAGLRNAVSQMRKEMEMLSGHLPFAQSEERSNANPEPKagedsappdyVLA 565
Cdd:COG2433 402 EHEERELTEEEEEIR--RLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDRE----------ISR 469
|
90
....*....|....*..
gi 1958663250 566 LEAEMQNLKHELKALEE 582
Cdd:COG2433 470 LDREIERLERELEEERE 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-310 |
2.67e-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: 45.05 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 2 EELRHQHK----LMLQEHRLELERVHSDKNsELNHQREQYENLKWKLERKLKELDGElalQRQVHKTLEEIYSLLsevfl 77
Cdd:TIGR02168 220 AELRELELallvLRLEELREELEELQEELK-EAEEELEELTAELQELEEKLEELRLE---VSELEEEIEELQKEL----- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 78 nvcYRLVALQARgcaripvmpvmlalterrtpwdsslpVDVMKQEwvwLDSSTELLQEFESEAQRREHEFQLRADDLsnt 157
Cdd:TIGR02168 291 ---YALANEISR--------------------------LEQQKQI---LRERLANLERQLEELEAQLEELESKLDEL--- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 158 vlthELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEamkdARIKDLEKKLHS----VQLAKK 233
Cdd:TIGR02168 336 ----AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR----SKVAQLELQIASlnneIERLEA 407
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958663250 234 KAEETFRRKHEELDRQAREKDTVLAAVKGAHAEQLQTLDAKVLELQFRCETLEGQLRRAEWRQAEDSKERNSLTDKE 310
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
138-306 |
2.70e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 138 SEAQRREHEFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEAMKDAR 217
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 218 IKDLEKKLHSVQLAKKKAEETFRRKHEELDRQAReKDTVLAAVKGAHAEQLQTLDAKVLELQFRCETLEGQLRRAEWRQA 297
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLSPEDFLDAVR-RLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
....*....
gi 1958663250 298 EDSKERNSL 306
Cdd:COG4942 182 ELEEERAAL 190
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
352-530 |
2.73e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 352 QIAQMSKEAVSKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLGLDWQRRCDDI-------- 423
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaellraly 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 424 ---------------ECNQIQRSETLIQGLTKARDQVAAKLQETERALHKQETLLKAVSLERDQAMETLRT-HGLLPGQE 487
Cdd:COG4942 115 rlgrqpplalllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEeRAALEALK 194
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958663250 488 AQVPPQPHEGEIRTDSPSSEIQRLQEQNAGLRNAVSQMRKEME 530
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-302 |
2.93e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 1 MEELRHQHKLMLQEHRLELERVHSDKNSELNHQREQYENLKWKLERKLKELDgELALQRQVHKTLEEIYSLLSEVFLN-- 78
Cdd:COG4717 179 LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE-QLENELEAAALEERLKEARLLLLIAaa 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 79 VCYRLVALQARGCARIPVMPVMLALTErrtpwdsslpvdVMKQEWVWLDSSTELLQEFESEAQRREHEFQLRADDLSNTV 158
Cdd:COG4717 258 LLALLGLGGSLLSLILTIAGVLFLVLG------------LLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 159 LTHELKVKLLNKELQALKEAGAQATESLQKAESEhiELERKLQDHARELQDLEAMKDAR-IKDLEKKLHSVQlAKKKAEE 237
Cdd:COG4717 326 AALGLPPDLSPEELLELLDRIEELQELLREAEEL--EEELQLEELEQEIAALLAEAGVEdEEELRAALEQAE-EYQELKE 402
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958663250 238 TFRRKHEELDRQAREKDTVLAAV-KGAHAEQLQTLDAKVLELQFRCETLEGQLRRAEWR--QAEDSKE 302
Cdd:COG4717 403 ELEELEEQLEELLGELEELLEALdEEELEEELEELEEELEELEEELEELREELAELEAEleQLEEDGE 470
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
778-1002 |
3.39e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.78 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 778 TPCPGPPTSEP---QDPREVPERPLDRGPPLGQLQPHSTTQDPRHTKRKcvseyagknqPHSAQVVNKNSTPQGHKAG-- 852
Cdd:PHA03307 183 ARAPSSPPAEPppsTPPAAASPRPPRRSSPISASASSPAPAPGRSAADD----------AGASSSDSSSSESSGCGWGpe 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 853 -MASRPVQKQHRIPTETWKSVYQKENRTPKLPQAQEVPEESDH------HTHRSSSLASSSLLDTWRlLDLGSSLSGVPS 925
Cdd:PHA03307 253 nECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSpspspsSPGSGPAPSSPRASSSSS-SSRESSSSSTSS 331
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958663250 926 QDNSAAECPAPLGPSCfqkvSRSPVP--TQRVSRSPVPTQRAFAVKGLKMEAQPKASHPRPSKSHPAKPANCQPQRHPR 1002
Cdd:PHA03307 332 SSESSRGAAVSPGPSP----SRSPSPsrPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGR 406
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
13-310 |
3.73e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 13 QEHRLELERVHSDKNSELNHQREQYENLKWKLERKLKELDGELALQRQV---HKTLEEIYSLLSEvfLNVcYRLVALQAr 89
Cdd:PRK03918 447 EEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELiklKELAEQLKELEEK--LKK-YNLEELEK- 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 90 gcaripvmpvmlALTERRTPWDSSLPVdvmKQEWVWLDSSTELLQEFESEAQRREHEFQLRADDLSntvlthELKVKLLN 169
Cdd:PRK03918 523 ------------KAEEYEKLKEKLIKL---KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELA------ELLKELEE 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 170 KELQALKEAGAQATEsLQKAESEHIEL---ERKLQDHARELQDLEAMKDARIKDLEKKLHSVQLAKKKAEETFRRKHEEL 246
Cdd:PRK03918 582 LGFESVEELEERLKE-LEPFYNEYLELkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE 660
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958663250 247 DRQAREKDTVLaavkgahAEQLQTLDAKVLELQFRCETLEGQLRRAEWRQAEDSKERNSLTDKE 310
Cdd:PRK03918 661 YEELREEYLEL-------SRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-279 |
8.29e-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: 43.52 E-value: 8.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 1 MEELRHQHKLM--LQEHRLELERVHSDKNSELNHQREQYENLKWKLE---RKLKELDGELALQRQVHKTLEEIYSLLSEV 75
Cdd:TIGR02169 694 QSELRRIENRLdeLSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEeleEDLSSLEQEIENVKSELKELEARIEELEED 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 76 FLNVCYRLVALQARgcaripvmpvmLALTERRTPWDSSLPVDVMKQEWVwldsstELLQEFESEAQRREHEFQLrADDLS 155
Cdd:TIGR02169 774 LHKLEEALNDLEAR-----------LSHSRIPEIQAELSKLEEEVSRIE------ARLREIEQKLNRLTLEKEY-LEKEI 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 156 NtvlthELKVKLLnkELQALKEAGAQATESLQKaesEHIELERKLQDHARELQDLEAmkdaRIKDLEKKLHSVQLAKKKA 235
Cdd:TIGR02169 836 Q-----ELQEQRI--DLKEQIKSIEKEIENLNG---KKEELEEELEELEAALRDLES----RLGDLKKERDELEAQLREL 901
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1958663250 236 EETFRRKHEELDrQAREKDTVLAAVKGAHAEQLQTLDAKVLELQ 279
Cdd:TIGR02169 902 ERKIEELEAQIE-KKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
352-478 |
8.88e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 8.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 352 QIAQMSKEAVSKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAV-ERE-QSLEREQVQLGLdwqrrcddiecnQIQ 429
Cdd:COG1579 39 ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnNKEyEALQKEIESLKR------------RIS 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958663250 430 RSETLIQGLTKARDQVAAKLQETERALHKQETLLKAVSLERDQAMETLR 478
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
133-245 |
1.64e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 40.69 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 133 LQEFESEAQRREHEFQLRaddlsntvlthelkVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDlea 212
Cdd:pfam08614 62 LREELAELYRSRGELAQR--------------LVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELRE--- 124
|
90 100 110
....*....|....*....|....*....|...
gi 1958663250 213 mKDARIKDLEKKLHSVQLAKKKAEETFRRKHEE 245
Cdd:pfam08614 125 -KRKLNQDLQDELVALQLQLNMAEEKLRKLEKE 156
|
|
| BBP1_C |
pfam15272 |
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole ... |
126-255 |
4.38e-03 |
|
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole body component, carries coiled-coils that are necessary for the localization of BBP1 to the spindle pole body (SPB). Although not a membrane protein itself, BBP1 binds to Mps2 as well as to Spc29 and the half-bridge protein Kar1, thus providing a model for how the SPB core is tethered within the nuclear envelope and to the half-bridge
Pssm-ID: 405864 [Multi-domain] Cd Length: 183 Bit Score: 39.30 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 126 LDSSTELLQEFESEAQRREHEFQLRADDLSNTVLthELKVKLLNKELQALKEAGA-----QATESLQKAESEHIELERKL 200
Cdd:pfam15272 13 LDKNNRALHLLNKDVRERDEHYQLQETSYKKKYL--QTRNELINELKQSKKLYDNyyklySKYQQLKKISNESLDLQSTI 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958663250 201 QDHARELQDLEAMKDARIKDLEKKLHSVQLAKKKAEETFRR-------KHEELDRQAREKDT 255
Cdd:pfam15272 91 TNLESQLVDQAIDKDREIHNLNEKILSLELRNQELETKREIdkmkyesRIDELERQLKEQEY 152
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
134-301 |
4.59e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 134 QEFESEAQRREHEF-QLRADDLSNTVLTHELKVKLLNKELQALKEAGAQAtESLQKAESEHIELERKLQDHARELQDLEA 212
Cdd:PTZ00121 1573 EEDKNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-EELKKAEEEKKKVEQLKKKEAEEKKKAEE 1651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 213 MKDArikDLEKKLHSVQLAKK------------KAEETFRRKHEELDRQAREKDTVlAAVKGAHAEQLQTLDAKVLELQF 280
Cdd:PTZ00121 1652 LKKA---EEENKIKAAEEAKKaeedkkkaeeakKAEEDEKKAAEALKKEAEEAKKA-EELKKKEAEEKKKAEELKKAEEE 1727
|
170 180
....*....|....*....|...
gi 1958663250 281 RCETLEGQLRRAEW--RQAEDSK 301
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEdkKKAEEAK 1750
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
365-458 |
4.60e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 365 LQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLGLDwqrrcddiecnQIQRSETLIQGLTKARDQ 444
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD-----------RLEQLEREIERLERELEE 356
|
90
....*....|....
gi 1958663250 445 VAAKLQETERALHK 458
Cdd:COG4913 357 RERRRARLEALLAA 370
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-303 |
5.47e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 1 MEELRHQHKLMLQEHRLELERVHSDKNsELNHQREQYENLKWKLERKLKELDGELALQRQVHKTLEEIYSLLSEVFLNVc 80
Cdd:COG4717 183 LEQLSLATEEELQDLAEELEELQQRLA-ELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLA- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 81 yrLVALQARGCARIPVMPVMLALTerrtpwdsslpVDVMKQEWVWLDSSTELLQEFESEAQRREHEFQLRADDLSNTVLT 160
Cdd:COG4717 261 --LLGLGGSLLSLILTIAGVLFLV-----------LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAA 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 161 HELKVKLLNKELQALKEAGAQATESLQKAESEhiELERKLQDHARELQDLEAMKDAR-IKDLEKKLHSVQlAKKKAEETF 239
Cdd:COG4717 328 LGLPPDLSPEELLELLDRIEELQELLREAEEL--EEELQLEELEQEIAALLAEAGVEdEEELRAALEQAE-EYQELKEEL 404
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958663250 240 RRKHEELDRQAREKDTVLAAV-KGAHAEQLQTLDAKVLELQFRCETLEGQLRRAEWR--------------QAEDSKER 303
Cdd:COG4717 405 EELEEQLEELLGELEELLEALdEEELEEELEELEEELEELEEELEELREELAELEAEleqleedgelaellQELEELKA 483
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
126-296 |
5.64e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 126 LDSSTELLQEFESEAQRREHEfqlrADDLSNTVLTHELKVKLLNKELQALK---EAGAQATESLQKAESEHIELERkLQD 202
Cdd:PRK02224 539 AEELRERAAELEAEAEEKREA----AAEAEEEAEEAREEVAELNSKLAELKeriESLERIRTLLAAIADAEDEIER-LRE 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 203 HARELQDLE-------AMKDARIKDLEKKLHSVQLA-----KKKAEETFRRKHEELDRQAREKDTVLAAVKGAHAE--QL 268
Cdd:PRK02224 614 KREALAELNderrerlAEKRERKRELEAEFDEARIEearedKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEleEL 693
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958663250 269 QTLDAKVLELQFRCETLE-------------GQLrRAEWRQ 296
Cdd:PRK02224 694 EELRERREALENRVEALEalydeaeelesmyGDL-RAELRQ 733
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
366-593 |
5.72e-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: 40.82 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 366 QIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLGLDWQRRCDDiECNQIQRSETLIQG-LTKARDQ 444
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE-EQLRVKEKIGELEAeIASLERS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 445 VAAKLQETERAlhkQETLLKAVSLERDQA--METLRTH-GLLPGQEAQVPPQPHEGEIRTDSPSSEIQRLQEQNAGLRNA 521
Cdd:TIGR02169 310 IAEKERELEDA---EERLAKLEAEIDKLLaeIEELEREiEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 522 VSQMRKEMEMLS-------------GHLPFAQSEERSNANPEPKAGEDSappdyVLALEAEMQNLKHELKALEEQLQGTG 588
Cdd:TIGR02169 387 LKDYREKLEKLKreinelkreldrlQEELQRLSEELADLNAAIAGIEAK-----INELEEEKEDKALEIKKQEWKLEQLA 461
|
....*
gi 1958663250 589 EPVKT 593
Cdd:TIGR02169 462 ADLSK 466
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
179-308 |
7.02e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 179 GAQATESLQKAESEHIELERKLQDHARELQDLEamkdARIKDLEKKLHSVQLAKKKAEEtfRRKHEELDRQAREKDTVLA 258
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEAEERLEALE----AELDALQERREALQRLAEYSWD--EIDVASAEREIAELEAELE 678
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1958663250 259 AVKGAHAEqLQTLDAKVLELQFRCETLEGQLRRAEWRQAEDSKERNSLTD 308
Cdd:COG4913 679 RLDASSDD-LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
131-310 |
8.34e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.52 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 131 ELLQEFESEAQRR---EHEFQLRADDLSNTVLTH---ELKVKLLNKELQALKeagaqateslqkaeSEHIELERKLQDHA 204
Cdd:pfam00038 86 DFRQKYEDELNLRtsaENDLVGLRKDLDEATLARvdlEAKIESLKEELAFLK--------------KNHEEEVRELQAQV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 205 RELQDLEAMKDARIKDLEKKLHSV--------QLAKKKAEETFRRKHEELDRQAREKDTVLAAVKGAHAE---QLQTLDA 273
Cdd:pfam00038 152 SDTQVNVEMDAARKLDLTSALAEIraqyeeiaAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITElrrTIQSLEI 231
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958663250 274 KVLELQFRCETLEGQLRRAEWRQAEDSKE-RNSLTDKE 310
Cdd:pfam00038 232 ELQSLKKQKASLERQLAETEERYELQLADyQELISELE 269
|
|
| PRK13460 |
PRK13460 |
F0F1 ATP synthase subunit B; Provisional |
169-295 |
8.84e-03 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 139585 [Multi-domain] Cd Length: 173 Bit Score: 38.47 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 169 NKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQdlEAMKDARIKDLEKKLHSVQLAKKKAEETfrrkHEELDR 248
Cdd:PRK13460 39 DVILKALDERASGVQNDINKASELRLEAEALLKDYEARLN--SAKDEANAIVAEAKSDALKLKNKLLEET----NNEVKA 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958663250 249 QareKDTVLAAVKGAHAEQLQTLDAKVLELQ--FRCETLEGQLRRAEWR 295
Cdd:PRK13460 113 Q---KDQAVKEIELAKGKALSQLQNQIVEMTitIASKVLEKQLKKEDYK 158
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
131-252 |
9.04e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663250 131 ELLQEFESEAQRREHEFQlradDLSNTVLTHEL----KVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARE 206
Cdd:PRK12704 68 KLRNEFEKELRERRNELQ----KLEKRLLQKEEnldrKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1958663250 207 LQDLEAM--KDAR---IKDLEKKlhsvqlAKKKAEETFRRKHEEL----DRQARE 252
Cdd:PRK12704 144 LERISGLtaEEAKeilLEKVEEE------ARHEAAVLIKEIEEEAkeeaDKKAKE 192
|
|
| |
