|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
26-420 |
1.38e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 26 QQLERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQT 105
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 106 EQELQRELDALrgqcQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTTHeellllrrerre 185
Cdd:COG1196 378 EEELEELAEEL----LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE------------ 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 186 hsLELERARSEAGEALSALRRLQRRVSELEEESRLQDADVSAASLQSELAHSLDDGDQGQGADAPGDTPTTRSPKTRKAS 265
Cdd:COG1196 442 --EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 266 SPQPSP-PEEILEPPKKRTSLSPAEILEEKEVEVAKLQDEISLQQAELQS-------LREELQRQKELRAQEDPGEALHS 337
Cdd:COG1196 520 RGLAGAvAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagratfLPLDKIRARAALAAALARGAIGA 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 338 ALSDRDEAVNKALELSLQLNRVSLERDSLSRELLRAIRQKVALTQELEAWQDDMQVVIGQQLRSQRQKELSASASSSTPR 417
Cdd:COG1196 600 AVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA 679
|
...
gi 767986955 418 RAA 420
Cdd:COG1196 680 ELE 682
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
20-231 |
4.44e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 20 QVQKPRQQLERLQQENHELRRGLAARGAE---WEARAVELEGDVEALRAQLGEQRSEQQDSGRERARALSELSEQNLRLS 96
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDLARLEAEveqLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 97 QQLAQASQTEQ---ELQRELDALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTTH 173
Cdd:TIGR02168 793 QLKEELKALREaldELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767986955 174 EELLLLRRERREHSLELERARSEAGEALSALRRLQRRVSELEEESRLQDADVSAASLQ 231
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR 930
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
25-236 |
1.01e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 25 RQQLERLQQENHELRRGLAARgaewEARAVELEGDVEALRAQLGEQRSEQQDSGRERARALSELSeqnlRLSQQLAQASQ 104
Cdd:COG1196 238 EAELEELEAELEELEAELEEL----EAELAELEAELEELRLELEELELELEEAQAEEYELLAELA----RLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 105 TEQELQRELDALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTTHEELLLLRRERR 184
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767986955 185 EHSLELERARSEAGEALSALRRLQRRVSELEEESRLQDADVSAASLQSELAH 236
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
31-390 |
1.15e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 31 LQQENHELRRGLAARGAEW-EARAVELEGDVEALRAQLGEQRSEQqdsgRERARALSELSEQNLRLSQQLAQASQTEQEL 109
Cdd:COG1196 218 LKEELKELEAELLLLKLRElEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 110 QRELDALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTtheeLLLLRRERREHSLE 189
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE----AEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 190 LERARSEAGEALSALRR--LQRRVSELEEESRLQDADVSAASLQSELAHSLDDgdqgqgadapgdtpttrspktrkassp 267
Cdd:COG1196 370 AEAELAEAEEELEELAEelLEALRAAAELAAQLEELEEAEEALLERLERLEEE--------------------------- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 268 qpsppeeileppkKRTSLSPAEILEEKEVEVAKLQDEISLQQAELQSLREELQRQKELRAQEDPGEALHSALSDRDEAVN 347
Cdd:COG1196 423 -------------LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 767986955 348 KALELSLQLNRVSLERDSLSRELLRAIRQKVALTQELEAWQDD 390
Cdd:COG1196 490 AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
25-320 |
6.39e-09 |
|
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: 58.16 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 25 RQQLERLQQENHELRRGLA---ARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQ 101
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSdasRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 102 ASQTE---------------QELQRELDALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQ-------DLEAQIRGLR 159
Cdd:TIGR02169 774 LHKLEealndlearlshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQelqeqriDLKEQIKSIE 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 160 EEVEKGEGRLQTTHEELLLLRRERREHSLELERARSEAGEALSALRRLQRRVSELE-----EESRLQDADVSAASLQSEL 234
Cdd:TIGR02169 854 KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEaqiekKRKRLSELKAKLEALEEEL 933
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 235 AHSLDDGDQGQgadapgdtpttrspktrkaSSPQPSPPEEILEPPKKR-----TSLSPAEILEEKEVE-VAKLQDEISLQ 308
Cdd:TIGR02169 934 SEIEDPKGEDE-------------------EIPEEELSLEDVQAELQRveeeiRALEPVNMLAIQEYEeVLKRLDELKEK 994
|
330
....*....|..
gi 767986955 309 QAELQSLREELQ 320
Cdd:TIGR02169 995 RAKLEEERKAIL 1006
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
20-217 |
2.90e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 20 QVQKPRQQLERLQQENHELRRGLAARGAEWEARAVELeGDVEALRAQLGEQRSEQQDSGRERARALSELSEQNLRLSQQL 99
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEA-ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 100 AQASQTEQELQRELDALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTTHEELLLL 179
Cdd:TIGR02168 862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
170 180 190
....*....|....*....|....*....|....*....
gi 767986955 180 RRE-RREHSLELERARSEAGEALSALRRLQRRVSELEEE 217
Cdd:TIGR02168 942 QERlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
20-217 |
4.93e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 20 QVQKPRQQLERLQQ--ENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSGRERARAlselseqnlrlsq 97
Cdd:COG4913 243 ALEDAREQIELLEPirELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEA------------- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 98 QLAQASQTEQELQRELDALRGQCQAQALAG-AELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTTHEEL 176
Cdd:COG4913 310 ELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA 389
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767986955 177 LLLRRERREhslELERARSEAGEALSALRRLQRRVSELEEE 217
Cdd:COG4913 390 AALLEALEE---ELEALEEALAEAEAALRDLRRELRELEAE 427
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
25-321 |
2.71e-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: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 25 RQQLERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSGRERARALSELSEQNLRlsqqLAQASQ 104
Cdd:TIGR02169 197 RQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR----LEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 105 TEQELQRELDALRGQCQAQalagaeLRTRLESLQGE--------------NQMLQSRRQDLEAQIRGLREEVEKGEGRLQ 170
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQLR------VKEKIGELEAEiaslersiaekereLEDAEERLAKLEAEIDKLLAEIEELEREIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 171 TTHEELLLLRRERREHSLELERARSEAGEALSALRRLQRRVSELEEEsrLQDADVSAASLQSELAHSLDDGDQ--GQGAD 248
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK--LEKLKREINELKRELDRLQEELQRlsEELAD 424
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767986955 249 APGDTPTTRSPKTRKASSPQpsppEEILEPPKKRTSLSP-AEILEEKEVEVAKLQDEISLQQAELQSLREELQR 321
Cdd:TIGR02169 425 LNAAIAGIEAKINELEEEKE----DKALEIKKQEWKLEQlAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
26-357 |
1.03e-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: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 26 QQLERLQQENHELRRGLAArgaeweARAVELEGDVEALRAQLGEQRSEQQDSGRERARALSELSEQNLRLSqqlaQASQT 105
Cdd:TIGR02168 213 ERYKELKAELRELELALLV------LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS----ELEEE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 106 EQELQRELDALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTTHEELLLLRRERRE 185
Cdd:TIGR02168 283 IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 186 HSLELERARSEAGEALSALRRLQRRVSELEEESRLQDADVS-AASLQSELAHSLDDGDQGQGADAPgdtptTRSPKTRKA 264
Cdd:TIGR02168 363 LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIErLEARLERLEDRRERLQQEIEELLK-----KLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 265 SSPQPSPPEEILEPPKKRtslspaeiLEEKEVEVAKLQDEISLQQAELQSLREELQRqkeLRAQEDPGEALHSALSDRDE 344
Cdd:TIGR02168 438 LQAELEELEEELEELQEE--------LERLEEALEELREELEEAEQALDAAERELAQ---LQARLDSLERLQENLEGFSE 506
|
330
....*....|...
gi 767986955 345 AVNKALELSLQLN 357
Cdd:TIGR02168 507 GVKALLKNQSGLS 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
25-231 |
1.13e-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: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 25 RQQLERLQQENHELRRGLAARGAEWEaravELEGDVEALRAQLGEQRSEQQDSGREraraLSELSEQNLRLSQQLAQASQ 104
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLE----ELRLEVSELEEEIEELQKELYALANE----ISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 105 TEQELQRELDALRGQCQAQALAGAELRTRLESLQGEnqmlqsrRQDLEAQIRGLREEVEKGEGRLQTTHEELLLLRRERR 184
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEE-------LESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767986955 185 EHSLELERARSEAGEALSALRRLQRRVSELEEESRLQDADVSAASLQ 231
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-239 |
2.68e-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: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 47 AEWEARAVELEGDVEALRAQLGEQRSEQ---QDSGRERARALSELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQAQ 123
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELeelEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 124 ALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTTHEELLLLRRERREHSLELERARSEAGEALSA 203
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767986955 204 LRRLQRRVSELEEE-----SRLQDADVSAASLQSELAHSLD 239
Cdd:TIGR02168 840 LEDLEEQIEELSEDieslaAEIEELEELIEELESELEALLN 880
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
25-217 |
2.89e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 25 RQQLERLQQEnhelRRGLAARGAEWEARAVELEGDVEALRAQlgeqrseqqdsgRERARALSELSEQNLRLSQQLAQASQ 104
Cdd:COG4913 609 RAKLAALEAE----LAELEEELAEAEERLEALEAELDALQER------------REALQRLAEYSWDEIDVASAEREIAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 105 TEQELQR------ELDALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTTHEELLL 178
Cdd:COG4913 673 LEAELERldassdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767986955 179 LRRERrehsLELERARSEAGEALSA-LRRLQRRVSELEEE 217
Cdd:COG4913 753 ERFAA----ALGDAVERELRENLEErIDALRARLNRAEEE 788
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
39-385 |
4.09e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 39 RRGLAARGAEwEARAVELEGDVEalRAQLGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQRELDALRG 118
Cdd:TIGR02168 657 PGGVITGGSA-KTNSSILERRRE--IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRK 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 119 QCqaqalagAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTTHEELLLLRRerrehslELERARSEAG 198
Cdd:TIGR02168 734 DL-------ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA-------QIEQLKEELK 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 199 EALSALRRLQRRVSELEEEsrLQDADVSAASLQSELAHslddgdqgqgadapgdtpttrspktrkasspqpsppeeilep 278
Cdd:TIGR02168 800 ALREALDELRAELTLLNEE--AANLRERLESLERRIAA------------------------------------------ 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 279 pKKRTSLSPAEILEEKEVEVAKLQDEISLQQAELQSLREELQRQKELRAQEDpgEALHSALSDRDEAVNKALELSLQLNR 358
Cdd:TIGR02168 836 -TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE--EALALLRSELEELSEELRELESKRSE 912
|
330 340
....*....|....*....|....*..
gi 767986955 359 VSLERDSLSRELLRAIRQKVALTQELE 385
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRID 939
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
128-434 |
1.04e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 128 AELRTRLESLQG------------------ENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTTHEELLLLRRERREHSLE 189
Cdd:COG1196 196 GELERQLEPLERqaekaeryrelkeelkelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 190 LERARSEAGEALSALRRLQRRVSELEEESRLQDADVSAASLQSELAHSLDDGDQGQGADAPGDTPTTRspKTRKASSPQP 269
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE--EELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 270 SPPEEILEPPKKRTSLSPAEILEEKEVEVAKLQDEISLQQAELQSLREELQRQKELRAQEDPGEALHSALSDRDEAVNKA 349
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 350 LELSLQLNRVSLERDS----LSRELLRAIRQKVALTQELEAWQDDMQVVIGQQLRSQRQKELSASASSSTPRRAAPRFSL 425
Cdd:COG1196 434 EEEEEEEEEALEEAAEeeaeLEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
....*....
gi 767986955 426 RLGPGPAGG 434
Cdd:COG1196 514 LLLAGLRGL 522
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
29-392 |
1.37e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 29 ERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQrSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQE 108
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA-DEVLEEHEERREELETLEAEIEDLRETIAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 109 LQRELDALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTTHEELLLLRRERREHSL 188
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 189 ELERARSEAGE-------ALSALRRLQRRVSELEEESRLQDADVSAASLQSELAHSLDDGDQGQGADAPGDTPTTRSpkT 261
Cdd:PRK02224 357 RAEELREEAAEleseleeAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEA--T 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 262 RKASSPQPSPPEEILEPPKKRTSLSP------AEILEEKEVEVAKLQDEISLQQAELQSLREELQRQKELRAQEDPGEal 335
Cdd:PRK02224 435 LRTARERVEEAEALLEAGKCPECGQPvegsphVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIE-- 512
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 767986955 336 hsALSDRDEAVNKALElslqLNRVSLERDSLSRELLRAirQKVALTQELEAWQDDMQ 392
Cdd:PRK02224 513 --RLEERREDLEELIA----ERRETIEEKRERAEELRE--RAAELEAEAEEKREAAA 561
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
26-158 |
6.10e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.96 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 26 QQLERLQQENHELRRGLAARgaewEARAVELEGDVEALRAQLGEQRSEQ---QDSGRERARALSELSEQNLRLSQQLAQA 102
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLE----RQGNQDLQDSVANLRASLSAAEAERsrlQALLAELAGAGAAAEGRAGELAQELDSE 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 767986955 103 SQTEQELQRELDALRGQCqaqalagAELRTRLESLQGENQMLQSRRQDLEAQIRGL 158
Cdd:PRK09039 129 KQVSARALAQVELLNQQI-------AALRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
22-163 |
1.07e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 22 QKPRQQLERLQQENHELRRGLAARGAEWEA-RAVELEGDVEALRAQLGEQRSEQQDSGRERARALSELSEQNLRLSQQLA 100
Cdd:COG3096 495 QTARELLRRYRSQQALAQRLQQLRAQLAELeQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA 574
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767986955 101 QASQTEQELQRELDALRGQCQ---AQALAGAELRTRLESLQGE-NQMLQSRRQDLEAQIRGLREEVE 163
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKelaARAPAWLAAQDALERLREQsGEALADSQEVTAAMQQLLERERE 641
|
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
212-386 |
1.23e-04 |
|
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.
Pssm-ID: 411439 [Multi-domain] Cd Length: 1306 Bit Score: 44.70 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 212 SELEEESRLQDADVSAASLQSELAHSLDDGDQGQGAdaPGDTPTTRSPKTRKASSPQPSP---PEEILEPPKKRTSLSPA 288
Cdd:NF033875 71 TAVSEEATVQKDTTSQPTKVEEVASEKNGAEQSSAT--PNDTTNAQQPTVGAEKSAQEQPvvsPETTNEPLGQPTEVAPA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 289 EILEEKEVEVAKlqdeiSLQQAELQSLREELQRQKELRAQEDPGEALHSaLSDRDEAVNKAlelslqlnrvslERDSLSR 368
Cdd:NF033875 149 ENEANKSTSIPK-----EFETPDVDKAVDEAKKDPNITVVEKPAEDLGN-VSSKDLAAKEK------------EVDQLQK 210
|
170
....*....|....*...
gi 767986955 369 ELLRAIRQKVAltqELEA 386
Cdd:NF033875 211 EQAKKIAQQAA---ELKA 225
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
20-171 |
1.99e-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: 43.21 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 20 QVQKPRQQLERLQQENHELRRGLAARGAEWEARAVELE-----------------GDVEALRAQLGEQRSEQQDSGRERA 82
Cdd:COG4942 77 ELAALEAELAELEKEIAELRAELEAQKEELAELLRALYrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 83 RALSELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEV 162
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
....*....
gi 767986955 163 EKGEGRLQT 171
Cdd:COG4942 237 AAAAERTPA 245
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
80-384 |
2.92e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 80 ERARALSELSEQNLRLSQQ----LAQASQTEQELQRELDALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQI 155
Cdd:pfam10174 447 EKERIIERLKEQREREDRErleeLESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAV 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 156 RGLREEVEKGEGRLQTTHEELLLLRR----ERREHSLELE--RARSEAGEALSALRRLQRRVSELEEESRLQDADVSAAS 229
Cdd:pfam10174 527 EQKKEECSKLENQLKKAHNAEEAVRTnpeiNDRIRLLEQEvaRYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELE 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 230 L--------QSELAHSLDDGDQGQGADAPGDTPTTRSPKTRKASSPQPSPPEEILEPPKKRTSlspaeILEEKEVEVAKL 301
Cdd:pfam10174 607 SltlrqmkeQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQ-----ELDATKARLSST 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 302 QDEISLQQAELQSLREELQRQKElRAQEDPGEALHSALSDRDEAVnKALELSlqlnrvSLERDSLSRELLRAIRQKVALT 381
Cdd:pfam10174 682 QQSLAEKDGHLTNLRAERRKQLE-EILEMKQEALLAAISEKDANI-ALLELS------SSKKKKTQEEVMALKREKDRLV 753
|
...
gi 767986955 382 QEL 384
Cdd:pfam10174 754 HQL 756
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
84-231 |
3.01e-04 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 43.30 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 84 ALSELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQAqalagaeLRTRLESLQGENQMLQSRRQDLEAQIRGLREEVE 163
Cdd:pfam09726 396 ALVRLEQDIKKLKAELQASRQTEQELRSQISSLTSLERS-------LKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQ 468
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767986955 164 KGEGRLQTT--HEELLLLRRERREHSLELERARSEAGEALSALRR------LQRRVSELEEESRLQDADVSAASLQ 231
Cdd:pfam09726 469 QLEKRLKAEqeARASAEKQLAEEKKRKKEEEATAARAVALAAASRgectesLKQRKRELESEIKKLTHDIKLKEEQ 544
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
20-229 |
3.40e-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: 42.83 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 20 QVQKPRQQLERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSGRERARALSELSEQNLRLSQQL 99
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 100 AQASQTEQELQRELDALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTTHEELLLL 179
Cdd:COG4942 111 RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767986955 180 RRERREHSLELERARSEAGEALSALRRLQRRVSELEEESRLQDADVSAAS 229
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
50-389 |
4.49e-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: 42.74 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 50 EARAVELEGDVEALRAQLGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQAQALAGAE 129
Cdd:TIGR02168 644 GYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 130 LRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTTHEELLLLRRERREHSLELERARSEAGEALSALRRLQR 209
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 210 RVSELEEEsrLQDADVSAASLQSELAHSLDDgdqgqgadapgdtpttrspktrkasspqpsppeeileppkkrtslspae 289
Cdd:TIGR02168 804 ALDELRAE--LTLLNEEAANLRERLESLERR------------------------------------------------- 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 290 iLEEKEVEVAKLQDEISLQQAELQSLreelqrQKELRAQEDPGEALHSALsdrDEAVNKALELSLQLNRVSLERDSLSRE 369
Cdd:TIGR02168 833 -IAATERRLEDLEEQIEELSEDIESL------AAEIEELEELIEELESEL---EALLNERASLEEALALLRSELEELSEE 902
|
330 340
....*....|....*....|
gi 767986955 370 LLRAIRQKVALTQELEAWQD 389
Cdd:TIGR02168 903 LRELESKRSELRRELEELRE 922
|
|
| Nucleoporin_FG2 |
pfam15967 |
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ... |
59-171 |
1.13e-03 |
|
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of chordate nucleoporins. The proteins carry many repeats of the FG sequence motif.
Pssm-ID: 435043 [Multi-domain] Cd Length: 586 Bit Score: 41.19 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 59 DVEALRAQLGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQRELDALRgQCQAQALAGAELRTRLES-- 136
Cdd:pfam15967 252 DVENFQKFVKEQKQVQEEISRMSSKAMLKVQDDIKALKQLLSVAASGLQRNSLAIDKLK-IETAQELKNADIALRTQKtp 330
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 767986955 137 --LQGEN----QMLQSRRQDLEAQIRGLREEVEKGEGRLQT 171
Cdd:pfam15967 331 pgLQHENtapaDYFRSLVEQFEVQLQQYRQQIEELENHLTT 371
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
79-247 |
1.49e-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: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 79 RERARALSELSEQNlrlsQQLAQASQTEQELQRELDALRGQCQAQALAgaELRTRLESLQGENQMLQSRRQDLEAQIRGL 158
Cdd:COG4913 248 REQIELLEPIRELA----ERYAAARERLAELEYLRAALRLWFAQRRLE--LLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 159 REEVEKGEGRLQTTHEELLLLRRErrehslELERARSEAGEALSALRRLQRRVSELEEESRLQDADVsaASLQSELAHSL 238
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLER------EIERLERELEERERRRARLEALLAALGLPLPASAEEF--AALRAEAAALL 393
|
....*....
gi 767986955 239 DDGDQGQGA 247
Cdd:COG4913 394 EALEEELEA 402
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
20-392 |
1.92e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 20 QVQKPRQQLERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSGRERARALSELseQNLRLSQQL 99
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL--EKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 100 AQASQTEQELQRELDALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTTHEELLLL 179
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 180 RRERREhslELERARSEAGEALSALRRLQRRVSELEEESRLQDADVSAASLQSELAHSLDDGDQGQGADAPGDTPTTRSP 259
Cdd:COG4717 208 LAELEE---ELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 260 KTRKASSPQPSPPEEILEPPKKRTSLSPAEILEEKEVE--VAKLQDEISLQQAELQSLREELQRQKELRAQEDpgEALHS 337
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEELQALPALEELEEEELEelLAALGLPPDLSPEELLELLDRIEELQELLREAE--ELEEE 362
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 767986955 338 ALSDRDEAVNKALelslqLNRVSLERDSLSRELLRAIRQKVALTQELEAWQDDMQ 392
Cdd:COG4717 363 LQLEELEQEIAAL-----LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLE 412
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
20-164 |
3.37e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 20 QVQKPRQQLERLQQENHELRRG--LAARGAEWEARAVELEGDVEALRAQLGEQR---SEQQDSGRERARALSELSEQNLR 94
Cdd:PRK04863 514 QLQQLRMRLSELEQRLRQQQRAerLLAEFCKRLGKNLDDEDELEQLQEELEARLeslSESVSEARERRMALRQQLEQLQA 593
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 95 LSQQLAQASQTEQELQRELDALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEK 164
Cdd:PRK04863 594 RIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIER 663
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
20-364 |
3.85e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 20 QVQKPRQQLERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSGRERARALSELSEqnlrLSQQL 99
Cdd:COG4372 7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ----LEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 100 AQASQTEQELQRELDALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTTHEELLLL 179
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 180 RRERRehSLELERARSEAGEALSALRRLQRRVSELEEESRLQDADVSAASLQSELAHSLDDGDQGQGADAPGDTPTTRSP 259
Cdd:COG4372 163 QEELA--ALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 260 KTR-KASSPQPSPPEEILEPPKKRTSLSPAEILEEKEVEVAKLQDEISLQQAELQSLREELQRQKELRAQEDPGEALHSA 338
Cdd:COG4372 241 ALElEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
|
330 340
....*....|....*....|....*.
gi 767986955 339 LSDRDEAVNKALELSLQLNRVSLERD 364
Cdd:COG4372 321 LLELAKKLELALAILLAELADLLQLL 346
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
28-235 |
4.19e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 28 LERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEqrseqqdsgreraraLSELSEQNLRLSQQLAQASQTEQ 107
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEE---------------YAELQEELEELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 108 ELQRELDALRGQCQAQALAG--AELRTRLESLQGENQMLQSR---RQDLEAQIRGLREEVEKGEGRLQTTHEELLLLRRE 182
Cdd:COG4717 113 ELREELEKLEKLLQLLPLYQelEALEAELAELPERLEELEERleeLRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767986955 183 RREHSLE-LERARSEAGEALSALRRLQRRVSELEEESRLQDADVSAASLQSELA 235
Cdd:COG4717 193 ELQDLAEeLEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
20-102 |
4.57e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 39.55 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 20 QVQKPRQQLERLQQE---NHELRRGLAARGAEWEARAVELEGDVEALRA---QLGEQRSEQQDSGRERARALSELSEQNL 93
Cdd:PRK11448 150 EVLTLKQQLELQAREkaqSQALAEAQQQELVALEGLAAELEEKQQELEAqleQLQEKAAETSQERKQKRKEITDQAAKRL 229
|
90
....*....|....*...
gi 767986955 94 RLS---------QQLAQA 102
Cdd:PRK11448 230 ELSeeetrilidQQLRKA 247
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
29-217 |
5.06e-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: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 29 ERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQE 108
Cdd:COG1196 615 YYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 109 LQRELDALRgqcqAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTTHEELLLLRRERREHSL 188
Cdd:COG1196 695 LEEALLAEE----EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE 770
|
170 180 190
....*....|....*....|....*....|...
gi 767986955 189 ELERARSEAGE----ALSALRRLQRRVSELEEE 217
Cdd:COG1196 771 RLEREIEALGPvnllAIEEYEELEERYDFLSEQ 803
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
74-164 |
5.49e-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: 38.98 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 74 QQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEA 153
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90
....*....|.
gi 767986955 154 QIRGLREEVEK 164
Cdd:COG4942 98 ELEAQKEELAE 108
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
22-154 |
8.50e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 38.57 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 22 QKPRQQLERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSGRERARALSELSE-QNLRLSQQLA 100
Cdd:pfam17380 456 QERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEErQKAIYEEERR 535
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 767986955 101 QASQTEQELQRELDAlRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQ 154
Cdd:pfam17380 536 REAEEERRKQQEMEE-RRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKAR 588
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
25-163 |
8.90e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 25 RQQLERLQQENHELrrglaargaewEARAVELEGDVEALRAQLGEQRSEQQDS-GRERARALSELSEQN---LRLSQQLA 100
Cdd:COG4913 301 RAELARLEAELERL-----------EARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERErrrARLEALLA 369
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767986955 101 QASQTEQELQRELDALRGQCQAQALAGAELRTRLESLQGEnqmLQSRRQDLEAQIRGLREEVE 163
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAE---AEAALRDLRRELRELEAEIA 429
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
25-151 |
9.06e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 38.50 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 25 RQQLERLQQENHElrrglaargaeweARAVELEGDVEALRAQLGEQRSEQQDSGRERARALSELS-----------EQNL 93
Cdd:PRK10929 202 RQELARLRSELAK-------------KRSQQLDAYLQALRNQLNSQRQREAERALESTELLAEQSgdlpksivaqfKINR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 94 RLSQQLAQASQ------------TEQELQ--RELDALRGQCQ---AQALAGAELRTRLESL-------QGENQMLQSRRQ 149
Cdd:PRK10929 269 ELSQALNQQAQrmdliasqqrqaASQTLQvrQALNTLREQSQwlgVSNALGEALRAQVARLpempkpqQLDTEMAQLRVQ 348
|
..
gi 767986955 150 DL 151
Cdd:PRK10929 349 RL 350
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
26-235 |
9.20e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 38.56 E-value: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 26 QQLERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQ----QDSG-------------RERARALSEL 88
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERdqfsQESGnlddqlqklladlHKREKELSLE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 89 SEQNLRLSQQLAQASQTEQELQRELD--------------ALRGQCQAQalagaeLRTRLESLQGENQMLQ---SRRQDL 151
Cdd:pfam15921 397 KEQNKRLWDRDTGNSITIDHLRRELDdrnmevqrleallkAMKSECQGQ------MERQMAAIQGKNESLEkvsSLTAQL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 152 EAQIRGLREEVEKGEGRLQTTHEELLLLRRERREHSlELERARSEAGEALSALR-RLQRRVSELE----EESRLQDADVS 226
Cdd:pfam15921 471 ESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ-EKERAIEATNAEITKLRsRVDLKLQELQhlknEGDHLRNVQTE 549
|
....*....
gi 767986955 227 AASLQSELA 235
Cdd:pfam15921 550 CEALKLQMA 558
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
26-171 |
9.20e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 38.46 E-value: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767986955 26 QQLERLQQENHELRRGLAARGAEWEARAVELEGDVEALRA-----QLGEQRSEQQDSGRERARALSELSEQNLRLSQQLA 100
Cdd:COG3206 219 QQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEllqspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRA 298
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767986955 101 QASQTEQELQRELDALRGQCQAQAlagAELRTRLESLQGENQMLQSRRQDL---EAQIRGLREEVEKGEGRLQT 171
Cdd:COG3206 299 QIAALRAQLQQEAQRILASLEAEL---EALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYES 369
|
|
|