|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
241-540 |
1.13e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 241 RYAIIKQEIEQLENE----RIDIQNGKEEiNLRNQLADKQSELKRIE------DNNSASNENKIHTLTNELHVENGTVAN 310
Cdd:COG1196 214 RYRELKEELKELEAEllllKLRELEAELE-ELEAELEELEAELEELEaelaelEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 311 LKTRLKQNKQQITHEENRRNQLLENHKGLKSDLEKAKNQKfEYLDDNVCSCCGQQLPAEQVNEAREKALQKFNASKSKEL 390
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL-EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 391 ETIQTSINHIISEGKKikpiIEKLEDDNNNLQIKINEAEERSARIQNKINKLKtthvdvtqtDEYKAVMLEINEINQKRS 470
Cdd:COG1196 372 AELAEAEEELEELAEE----LLEALRAAAELAAQLEELEEAEEALLERLERLE---------EELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487730061 471 NIRKTIQDNVSGIDDKISELTQEKSEI----EVSRSIEKSNKHLDDVISELRNEEDRLLDEKEKYSHDLYILKE 540
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLaellEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
187-523 |
5.65e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 187 FKELNNILGDHE---IETKKKILTDKIKQINKDIKDIPIRINQTQQNKQDVpefdNDRYAIIKQEIEQLeNERIDIQNGK 263
Cdd:TIGR02169 213 YQALLKEKREYEgyeLLKEKEALERQKEAIERQLASLEEELEKLTEEISEL----EKRLEEIEQLLEEL-NKKIKDLGEE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 264 EEINLRNQLADKQSELKRIEDNNSASNEnkihtltnelhvengtvanlktRLKQNKQQITHEENRRNQLLENHKGLKSDL 343
Cdd:TIGR02169 288 EQLRVKEKIGELEAEIASLERSIAEKER----------------------ELEDAEERLAKLEAEIDKLLAEIEELEREI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 344 EKAKNQKfeylddnvcsccgqqlpaEQVNEAREKALQKFNASKSkELETIQTSINHIISEGKKIKPIIEKLEDDNNNLQI 423
Cdd:TIGR02169 346 EEERKRR------------------DKLTEEYAELKEELEDLRA-ELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 424 ----KINEAEERSARIQNKINKLKTTHVDVTQTD-EYKAVMLEINEINQKrsniRKTIQDNVSGIDDKISELTQEKSEIE 498
Cdd:TIGR02169 407 eldrLQEELQRLSEELADLNAAIAGIEAKINELEeEKEDKALEIKKQEWK----LEQLAADLSKYEQELYDLKEEYDRVE 482
|
330 340
....*....|....*....|....*
gi 487730061 499 vsRSIEKSNKHLDDVISELRNEEDR 523
Cdd:TIGR02169 483 --KELSKLQRELAEAEAQARASEER 505
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
87-524 |
1.77e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.97 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 87 EIDGKITTFKKESHPKYTINQKTNRKEYSRSRTKKQYINDESIKVKDY--KARIDELIDEDVFKLITNPQafNLLDWKKR 164
Cdd:PRK01156 260 TAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIenKKQILSNIDAEINKYHAIIK--KLSVLQKD 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 165 RSLLFEIAKPINDEDVIKTNDDFKELNNILGDHEIETKKKiltdKIKQINKDIKDIPIRINQTQQNKQDVPEFDNDRYAI 244
Cdd:PRK01156 338 YNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKK----KIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNE 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 245 IKQEIEQLE------NERIDIQNGKEEINLRN---------------QLADKQSELKRIEDNNSASN-ENKIHTLTNELH 302
Cdd:PRK01156 414 INVKLQDISskvsslNQRIRALRENLDELSRNmemlngqsvcpvcgtTLGEEKSNHIINHYNEKKSRlEEKIREIEIEVK 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 303 VENGTVANLKTRLKQ-NKQQITHEENRRNQLLENHKGLKSDLE-----KAKNQKFEYLDDNVCSCCGQQLPAE------- 369
Cdd:PRK01156 494 DIDEKIVDLKKRKEYlESEEINKSINEYNKIESARADLEDIKIkinelKDKHDKYEEIKNRYKSLKLEDLDSKrtswlna 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 370 --QVNEAREKALQKFNASKSKELETIQTSINHIISEGKKIKPIIE----KLEDDNNNLQIKINEAEERSA---RIQNKIN 440
Cdd:PRK01156 574 laVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDksirEIENEANNLNNKYNEIQENKIlieKLRGKID 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 441 KLKtthvdvTQTDEYKAVMLEINEINQKRSNIRKTIQDNVSGIDDKISELTQEKSEIEVSRSiekSNKHLDDVISELRNE 520
Cdd:PRK01156 654 NYK------KQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRT---RINELSDRINDINET 724
|
....
gi 487730061 521 EDRL 524
Cdd:PRK01156 725 LESM 728
|
|
| DUF3568 |
pfam12092 |
Protein of unknown function (DUF3568); This family of proteins is functionally uncharacterized. ... |
369-441 |
1.89e-04 |
|
Protein of unknown function (DUF3568); This family of proteins is functionally uncharacterized. This protein is found in bacteria. Proteins in this family are about 130 amino acids in length.
Pssm-ID: 403350 Cd Length: 124 Bit Score: 41.53 E-value: 1.89e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487730061 369 EQVNEAREKALQKFNAS-KSKELETIQTSINHIISEGKKIKPIIEKLEDDNNNLQIKINEA--EERSARIQNKINK 441
Cdd:pfam12092 48 RSVYNATLAAIQDLNLSlVEKSKDGSSATITGKDAGDKTVFIRLEKLDDNSTKVSIRVGYFgdEQASRRLLDAIQK 123
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
241-540 |
1.13e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 241 RYAIIKQEIEQLENE----RIDIQNGKEEiNLRNQLADKQSELKRIE------DNNSASNENKIHTLTNELHVENGTVAN 310
Cdd:COG1196 214 RYRELKEELKELEAEllllKLRELEAELE-ELEAELEELEAELEELEaelaelEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 311 LKTRLKQNKQQITHEENRRNQLLENHKGLKSDLEKAKNQKfEYLDDNVCSCCGQQLPAEQVNEAREKALQKFNASKSKEL 390
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL-EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 391 ETIQTSINHIISEGKKikpiIEKLEDDNNNLQIKINEAEERSARIQNKINKLKtthvdvtqtDEYKAVMLEINEINQKRS 470
Cdd:COG1196 372 AELAEAEEELEELAEE----LLEALRAAAELAAQLEELEEAEEALLERLERLE---------EELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487730061 471 NIRKTIQDNVSGIDDKISELTQEKSEI----EVSRSIEKSNKHLDDVISELRNEEDRLLDEKEKYSHDLYILKE 540
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLaellEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
187-523 |
5.65e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 187 FKELNNILGDHE---IETKKKILTDKIKQINKDIKDIPIRINQTQQNKQDVpefdNDRYAIIKQEIEQLeNERIDIQNGK 263
Cdd:TIGR02169 213 YQALLKEKREYEgyeLLKEKEALERQKEAIERQLASLEEELEKLTEEISEL----EKRLEEIEQLLEEL-NKKIKDLGEE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 264 EEINLRNQLADKQSELKRIEDNNSASNEnkihtltnelhvengtvanlktRLKQNKQQITHEENRRNQLLENHKGLKSDL 343
Cdd:TIGR02169 288 EQLRVKEKIGELEAEIASLERSIAEKER----------------------ELEDAEERLAKLEAEIDKLLAEIEELEREI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 344 EKAKNQKfeylddnvcsccgqqlpaEQVNEAREKALQKFNASKSkELETIQTSINHIISEGKKIKPIIEKLEDDNNNLQI 423
Cdd:TIGR02169 346 EEERKRR------------------DKLTEEYAELKEELEDLRA-ELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 424 ----KINEAEERSARIQNKINKLKTTHVDVTQTD-EYKAVMLEINEINQKrsniRKTIQDNVSGIDDKISELTQEKSEIE 498
Cdd:TIGR02169 407 eldrLQEELQRLSEELADLNAAIAGIEAKINELEeEKEDKALEIKKQEWK----LEQLAADLSKYEQELYDLKEEYDRVE 482
|
330 340
....*....|....*....|....*
gi 487730061 499 vsRSIEKSNKHLDDVISELRNEEDR 523
Cdd:TIGR02169 483 --KELSKLQRELAEAEAQARASEER 505
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
248-524 |
5.95e-06 |
|
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: 49.68 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 248 EIEQLENERIDIQNGKEEI-NLRNQLADKQSELKR-IEDNnsasnENKIHTLTNELHVENGTVANLKTRLKQNKQQITHE 325
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIeNRLDELSQELSDASRkIGEI-----EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 326 EnrrnQLLENHKGLKSDLEKAKNQKFEYLDDNVCSCCGQQLPaEQVNEAREKalqkfnaskSKELETIQTSINHIISEGK 405
Cdd:TIGR02169 757 K----SELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP-EIQAELSKL---------EEEVSRIEARLREIEQKLN 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 406 KIKPIIEKLEDDNNNLQIKINEAEERSARIQNKINKLKTTHVDVTQtdEYKAVMLEINEINQKRSNIRKTIQDnvsgIDD 485
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE--ELEELEAALRDLESRLGDLKKERDE----LEA 896
|
250 260 270
....*....|....*....|....*....|....*....
gi 487730061 486 KISELTQEKSEIEVsrSIEKSNKHLDDVISELRNEEDRL 524
Cdd:TIGR02169 897 QLRELERKIEELEA--QIEKKRKRLSELKAKLEALEEEL 933
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
87-524 |
1.77e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.97 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 87 EIDGKITTFKKESHPKYTINQKTNRKEYSRSRTKKQYINDESIKVKDY--KARIDELIDEDVFKLITNPQafNLLDWKKR 164
Cdd:PRK01156 260 TAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIenKKQILSNIDAEINKYHAIIK--KLSVLQKD 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 165 RSLLFEIAKPINDEDVIKTNDDFKELNNILGDHEIETKKKiltdKIKQINKDIKDIPIRINQTQQNKQDVPEFDNDRYAI 244
Cdd:PRK01156 338 YNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKK----KIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNE 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 245 IKQEIEQLE------NERIDIQNGKEEINLRN---------------QLADKQSELKRIEDNNSASN-ENKIHTLTNELH 302
Cdd:PRK01156 414 INVKLQDISskvsslNQRIRALRENLDELSRNmemlngqsvcpvcgtTLGEEKSNHIINHYNEKKSRlEEKIREIEIEVK 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 303 VENGTVANLKTRLKQ-NKQQITHEENRRNQLLENHKGLKSDLE-----KAKNQKFEYLDDNVCSCCGQQLPAE------- 369
Cdd:PRK01156 494 DIDEKIVDLKKRKEYlESEEINKSINEYNKIESARADLEDIKIkinelKDKHDKYEEIKNRYKSLKLEDLDSKrtswlna 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 370 --QVNEAREKALQKFNASKSKELETIQTSINHIISEGKKIKPIIE----KLEDDNNNLQIKINEAEERSA---RIQNKIN 440
Cdd:PRK01156 574 laVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDksirEIENEANNLNNKYNEIQENKIlieKLRGKID 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 441 KLKtthvdvTQTDEYKAVMLEINEINQKRSNIRKTIQDNVSGIDDKISELTQEKSEIEVSRSiekSNKHLDDVISELRNE 520
Cdd:PRK01156 654 NYK------KQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRT---RINELSDRINDINET 724
|
....
gi 487730061 521 EDRL 524
Cdd:PRK01156 725 LESM 728
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
388-531 |
3.55e-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: 45.69 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 388 KELETIQTSINHIISEGKKIKPIIEKLEDDNNNLQIKINEAEERSARIQNKINKLKTThvdvtqtDEYKAVMLEINEINQ 467
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-------KEYEALQKEIESLKR 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487730061 468 KRSNIRKTIQDNVSGIDDKISELTQEKSEIE-VSRSIEKSNKHLDDVISELRNEEDRLLDEKEKY 531
Cdd:COG1579 104 RISDLEDEILELMERIEELEEELAELEAELAeLEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
247-498 |
3.91e-05 |
|
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: 46.30 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 247 QEIEQLENERIDIQNGKEEinLRNQLADKQSELKRIEDNNSASnENKIHTLTNELHVENGTVANLKTRLKQNKQQITHEE 326
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAE--LEKELAALKKEEKALLKQLAAL-ERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 327 NRRNQllenhkglksdlekaknQKFEYlddnvcsccGQQLPAEQVNEAREKALQKFNASKSKELETIQTSINHIISEGKK 406
Cdd:COG4942 97 AELEA-----------------QKEEL---------AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 407 ikpIIEKLEDDNNNLQIKINEAEERSARIQNKINKLKTTHVDVTQTDEYKAVMLeiNEINQKRSNIRKTI---QDNVSGI 483
Cdd:COG4942 151 ---QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL--ARLEKELAELAAELaelQQEAEEL 225
|
250
....*....|....*
gi 487730061 484 DDKISELTQEKSEIE 498
Cdd:COG4942 226 EALIARLEAEAAAAA 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
237-513 |
9.85e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 9.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 237 FDNDRY-AIIKQEIEQLENERIDIQNGKEEIN-LRNQLADKQSELKRI-----EDNNSASNENKIHTLTNELH---VENG 306
Cdd:COG4913 606 FDNRAKlAALEAELAELEEELAEAEERLEALEaELDALQERREALQRLaeyswDEIDVASAEREIAELEAELErldASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 307 TVANLKTRLKQNKQQITHEENRRNQLLENHKGLKSDLEKAKNQKFEYLDDNvcsccgQQLPAEQVNEAREKALQKFNASK 386
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL------EAAEDLARLELRALLEERFAAAL 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 387 SKELEtiqtsinhiisegkkiKPIIEKLEDDNNNLQIKINEAEERSARIQNKINK---LKTTHVDVT--QTDEYKAVM-- 459
Cdd:COG4913 760 GDAVE----------------RELRENLEERIDALRARLNRAEEELERAMRAFNRewpAETADLDADleSLPEYLALLdr 823
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 487730061 460 LEINEINQKRSNIRKTIQDNVSG-IDDKISELTQEKSEIEvsRSIEKSNKHLDDV 513
Cdd:COG4913 824 LEEDGLPEYEERFKELLNENSIEfVADLLSKLRRAIREIK--ERIDPLNDSLKRI 876
|
|
| DUF3568 |
pfam12092 |
Protein of unknown function (DUF3568); This family of proteins is functionally uncharacterized. ... |
369-441 |
1.89e-04 |
|
Protein of unknown function (DUF3568); This family of proteins is functionally uncharacterized. This protein is found in bacteria. Proteins in this family are about 130 amino acids in length.
Pssm-ID: 403350 Cd Length: 124 Bit Score: 41.53 E-value: 1.89e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487730061 369 EQVNEAREKALQKFNAS-KSKELETIQTSINHIISEGKKIKPIIEKLEDDNNNLQIKINEA--EERSARIQNKINK 441
Cdd:pfam12092 48 RSVYNATLAAIQDLNLSlVEKSKDGSSATITGKDAGDKTVFIRLEKLDDNSTKVSIRVGYFgdEQASRRLLDAIQK 123
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
243-532 |
5.75e-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: 43.13 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 243 AIIKQEIEQLENERI------DIQNGKEEINLRNQLADKQSELKRIE--DNNSASNENKIHTLTNELHVENGTVANLKTR 314
Cdd:TIGR02169 194 DEKRQQLERLRREREkaeryqALLKEKREYEGYELLKEKEALERQKEaiERQLASLEEELEKLTEEISELEKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 315 LKQNKQQITHE-ENRRNQLLENHKGLKSDLEKAKNQKFEYLDDnvcsccgqqlpAEQVNEAREKALQKFNASKSkELETI 393
Cdd:TIGR02169 274 LEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERE-----------LEDAEERLAKLEAEIDKLLA-EIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 394 QTSINHIISEGKKIKPIIEKLEDDNNNLQIKINEAEERSARIQNKINKLKTTHVDVT-QTDEYKAVMLEINEINQKRSNI 472
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKrEINELKRELDRLQEELQRLSEE 421
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 473 RKTIQDNVSGIDDKISELTQEKSEIEvsRSIEKSNKHLDDVISELRNEEDRLLDEKEKYS 532
Cdd:TIGR02169 422 LADLNAAIAGIEAKINELEEEKEDKA--LEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
400-575 |
6.18e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.99 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 400 IISEGKKIKPIIEKL--------EDDNNNLQI-KINEAEERSARIQNKINKLKTtHVDVTQTDEY---KAVMLEINEINQ 467
Cdd:PRK05771 11 IVTLKSYKDEVLEALhelgvvhiEDLKEELSNeRLRKLRSLLTKLSEALDKLRS-YLPKLNPLREekkKVSVKSLEELIK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 468 KRSNIRKTIQDNVSGIDDKISELTQEKSEIEVSRSIEKSNKHLDDVISELRNEE---------DRLLDEKEKYSHDLYIL 538
Cdd:PRK05771 90 DVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPWGNFDLDLSLLLGFKyvsvfvgtvPEDKLEELKLESDVENV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 487730061 539 KEFTTTK---------VKMLTENINNEFEIAEFKLFNTLVNGELEE 575
Cdd:PRK05771 170 EYISTDKgyvyvvvvvLKELSDEVEEELKKLGFERLELEEEGTPSE 215
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
188-438 |
1.41e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 188 KELNNIlgDHEIETKKKILTD---KIKQINKDIKDIPIRINQTQQNKQDVpefdNDRYAIIKQEIEQLEneridiqngKE 264
Cdd:COG4942 27 AELEQL--QQEIAELEKELAAlkkEEKALLKQLAALERRIAALARRIRAL----EQELAALEAELAELE---------KE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 265 EINLRNQLADKQSELKRIedNNSASNENKIHTLTNELHVENGT-----VANLKTRLKQNKQQITHEENRRNQLLEnhkgL 339
Cdd:COG4942 92 IAELRAELEAQKEELAEL--LRALYRLGRQPPLALLLSPEDFLdavrrLQYLKYLAPARREQAEELRADLAELAA----L 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 340 KSDLEKAKNQKfeylddnvcsccgQQLPAEQvnEAREKALQKFNASKSKELETIQTSInhiisegKKIKPIIEKLEDDNN 419
Cdd:COG4942 166 RAELEAERAEL-------------EALLAEL--EEERAALEALKAERQKLLARLEKEL-------AELAAELAELQQEAE 223
|
250
....*....|....*....
gi 487730061 420 NLQIKINEAEERSARIQNK 438
Cdd:COG4942 224 ELEALIARLEAEAAAAAER 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
178-540 |
1.73e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 178 EDVIKTNDDFKELnnilgdheIETKKKILTDKIKQINKDIKDIPIRINQTQQNKQDVPEFDNdryaiIKQEIEQLENERI 257
Cdd:PRK03918 182 EKFIKRTENIEEL--------IKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE-----LKEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 258 DIQNGKEEI-----NLRNQLADKQSELKRIEDNNSASNENKihtltnELHVENGTVANLKTRLKQNKQQITHEENRRNQL 332
Cdd:PRK03918 249 SLEGSKRKLeekirELEERIEELKKEIEELEEKVKELKELK------EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 333 LENHKGLKSDLEKaKNQKFEYLDDNVCSCCGQQLPAEQVNEAREKALQKFNASKSKELETIQTSINHIISEGKKIKPIIE 412
Cdd:PRK03918 323 INGIEERIKELEE-KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 413 KLEDDNNNLQIKINEAEERSARIQNKINKLKTTHVDVTQ-----TDEYKAVMLEinEINQKRSNIRKTIQDnvsgIDDKI 487
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVcgrelTEEHRKELLE--EYTAELKRIEKELKE----IEEKE 475
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 487730061 488 SELTQEKSEIEVSRSIEKSNKHLDDVISELRNEEDRL----LDEKEKYSHDLYILKE 540
Cdd:PRK03918 476 RKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLkkynLEELEKKAEEYEKLKE 532
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
359-540 |
1.79e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 359 CSCCGQQLPAEQVNEAREKALQKFNASKsKELETIQTSINHIISEGKKIKPIIEKLEDDNNNLQIKINEAEERSARIQNK 438
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELE-KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 439 INKLKTTHvdVTQTDEYKAVMLE----------------------------INEINQKRSNIRKTIQDNVSGIDDKISEL 490
Cdd:COG4942 92 IAELRAEL--EAQKEELAELLRAlyrlgrqpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 487730061 491 TQEKSEIEVSRS-IEKSNKHLDDVISELRNEEDRLLDEKEKYSHDLYILKE 540
Cdd:COG4942 170 EAERAELEALLAeLEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
198-376 |
1.83e-03 |
|
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: 40.29 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 198 EIETKKKILTDKIKQINKDIKDIPIRINQTQQNKQDVpeFDNDRYAIIKQEIEQLENERIDIQngKEEINLRNQLADKQS 277
Cdd:COG1579 49 AAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV--RNNKEYEALQKEIESLKRRISDLE--DEILELMERIEELEE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 278 ELKRIEDnnsasnenKIHTLTNELHVEngtVANLKTRLKQNKQQITHEENRRNQLLenhKGLKSDL----EKAKNQK--- 350
Cdd:COG1579 125 ELAELEA--------ELAELEAELEEK---KAELDEELAELEAELEELEAEREELA---AKIPPELlalyERIRKRKngl 190
|
170 180
....*....|....*....|....*..
gi 487730061 351 -FEYLDDNVCSCCGQQLPAEQVNEARE 376
Cdd:COG1579 191 aVVPVEGGACGGCFMELPPQELNEIRA 217
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
186-349 |
2.23e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 186 DFKELNNILgdhEIETKKKILTDKIKQINKDIKDIPIRINQTQ-----------QNKQDVPE-FDNDRYAIIKQEIEQLE 253
Cdd:COG3206 200 EFRQKNGLV---DLSEEAKLLLQQLSELESQLAEARAELAEAEarlaalraqlgSGPDALPElLQSPVIQQLRAQLAELE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 254 NERIDI-QNGKEE----INLRNQLADKQSELKRIEDNNSASNENKIHTLTNElhvengtVANLKTRLKQNKQQITHEENR 328
Cdd:COG3206 277 AELAELsARYTPNhpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAR-------EASLQAQLAQLEARLAELPEL 349
|
170 180
....*....|....*....|.
gi 487730061 329 RNQLLEnhkgLKSDLEKAKNQ 349
Cdd:COG3206 350 EAELRR----LEREVEVAREL 366
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
196-437 |
7.70e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 196 DHEIETKKKILTDKIKQINKDIKDIpIRINQTQQNKQdvpefdnDRYAIIKQEIEQLENERIDIQngKEEINLRNQLADK 275
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDI-ARLEERRRELE-------ERLEELEEELAELEEELEELE--EELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 276 QSELKRIEDNNSASNEnKIHTLTNELHVENGTVANLKTRLKQNKQQITHEENRRNQLLENHKGLKSDLEKAKNQKFEYLD 355
Cdd:COG1196 350 EEELEEAEAELAEAEE-ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 356 DnvcsccgqqlpAEQVNEAREKALQKFNASKSKELETIQTSINHIISEGKKIKpIIEKLEDDNNNLQIKINEAEERSARI 435
Cdd:COG1196 429 A-----------LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE-EAALLEAALAELLEELAEAAARLLLL 496
|
..
gi 487730061 436 QN 437
Cdd:COG1196 497 LE 498
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
244-524 |
9.10e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 39.07 E-value: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 244 IIKQEIEQLENE-RIDIQNGKEEINLRNQLADKQSELKRIEDNNSASNEN---KIHTLTNELHV---ENGTVANLK---- 312
Cdd:PLN03229 459 ALNEMIEKLKKEiDLEYTEAVIAMGLQERLENLREEFSKANSQDQLMHPVlmeKIEKLKDEFNKrlsRAPNYLSLKykld 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 313 ------------------TRLKQNKQQITHEENRRNQLLENHKGLKSDLEKAKNQKFEYLDDNVcsccgqqlpAEQVNEA 374
Cdd:PLN03229 539 mlnefsrakalsekkskaEKLKAEINKKFKEVMDRPEIKEKMEALKAEVASSGASSGDELDDDL---------KEKVEKM 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 375 R-EKALQKFNASKSKELETIQTSINHIISEGKKIKP-IIEKLEDDNNNLQIKINEAeERSARIQNKINKLKTTHVDVTQT 452
Cdd:PLN03229 610 KkEIELELAGVLKSMGLEVIGVTKKNKDTAEQTPPPnLQEKIESLNEEINKKIERV-IRSSDLKSKIELLKLEVAKASKT 688
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487730061 453 DEykavMLEINEINQKRSNIRKTIQD--NVSGIDDKISELTQE-KSEIEVSRSIEKSNKHLDDVISELRNEEDRL 524
Cdd:PLN03229 689 PD----VTEKEKIEALEQQIKQKIAEalNSSELKEKFEELEAElAAARETAAESNGSLKNDDDKEEDSKEDGSRV 759
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
316-538 |
9.95e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 38.84 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 316 KQNKQQITHEENRRNQLLENHKGLKSDLEKAKNQKFEYLDDNvcsccgqqlpaeqvnEAREKALQKFN---ASKSKELET 392
Cdd:PHA02562 209 KKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDI---------------EDPSAALNKLNtaaAKIKSKIEQ 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487730061 393 IQtSINHIISEGKKIKPIIEKLEDDNNnlqiKINEAEERSARIQNKINKLKTTHVDVTQ-TDEYKAVMLEINEINQKRSN 471
Cdd:PHA02562 274 FQ-KVIKMYEKGGVCPTCTQQISEGPD----RITKIKDKLKELQHSLEKLDTAIDELEEiMDEFNEQSKKLLELKNKIST 348
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487730061 472 IRKTIqdnvSGIDDKISELTQEKSEIEVSRSIEKSNkhlddvISELRNEEDRLLDEKEKYSHDLYIL 538
Cdd:PHA02562 349 NKQSL----ITLVDKAKKVKAAIEELQAEFVDNAEE------LAKLQDELDKIVKTKSELVKEKYHR 405
|
|
|