|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
32-277 |
2.38e-11 |
|
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: 64.70 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 32 TELNQKIGDLESQNQELARDNDAINRKIESLTAEIEELRGAESKAKRKMGEMEREIDKSDEERKVleAIASRASELETEV 111
Cdd:TIGR02169 226 YELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL--RVKEKIGELEAEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 112 ARLQHELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVKEENEKRMKELESKLGALEVkELDEKNKKFRa 191
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA-ELEEVDKEFA- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 192 eeEMREKIDNKEKEVHDLKEKIKSLESDVAKGKTELQKWITEKMVVEDSLKDSEKKVVALESEIVELQKQLDDAEKMING 271
Cdd:TIGR02169 382 --ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
|
....*.
gi 15221511 272 LKNVVE 277
Cdd:TIGR02169 460 LAADLS 465
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
33-278 |
5.52e-11 |
|
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: 63.54 E-value: 5.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 33 ELNQKIGDLESQNQELARDNDAINRKIESLTAEIEELRGAESKAKRKMGEMEREIDksdEERKVLEAIASRASELETEVA 112
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS---ALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 113 RLQHELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVKEENEKRMKELESKLGALEVKELDEKNKKfrae 192
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL---- 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 193 EEMREKIDNKEKEVHDLKEKIKSLESDVAKGKTELQKWITEKMVVEDSLKDSEKKVVALESEIVELQKQLDDAEKMINGL 272
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
....*.
gi 15221511 273 KNVVEE 278
Cdd:TIGR02168 907 ESKRSE 912
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
21-277 |
1.46e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 21 DSDQQGDDGKSTELNQKIGDLESQNQELARDNDAINRKIESLTAEIEELRGAESKAKRKMGEMEREIDKSDEERkvlEAI 100
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR---REL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 101 ASRASELETEVARLQHELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVKEENEKRMKELESKLGALEVK 180
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 181 ELDEKNKKF---RAEEEMREKIDNKEKEVHDLKEKIKSLESDVAKGKTELQKWITEKMVVEDSLKDSEKKVVALESEIVE 257
Cdd:COG1196 395 AAELAAQLEeleEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250 260
....*....|....*....|
gi 15221511 258 LQKQLDDAEKMINGLKNVVE 277
Cdd:COG1196 475 LEAALAELLEELAEAAARLL 494
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
34-278 |
1.53e-10 |
|
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: 62.39 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 34 LNQKIGDLESQNQELARDNDAINRKIESLTAEIEELRGAESKAKRKMGEMEREIDKSDEERkvlEAIASRASELETEVAR 113
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI---ENVKSELKELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 114 LQHELitARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAglrtvkeENEKRMKELESKLGALEVKeldeknkkfraEE 193
Cdd:TIGR02169 770 LEEDL--HKLEEALNDLEARLSHSRIPEIQAELSKLEEEVS-------RIEARLREIEQKLNRLTLE-----------KE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 194 EMREKIDNKEKEVHDLKEKIKSLESDVAKGKTELQKWITEKMVVEDSLKDSEKKVVALESEIVELQKQLDDAEKMINGLK 273
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
....*
gi 15221511 274 NVVEE 278
Cdd:TIGR02169 910 AQIEK 914
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
32-266 |
1.68e-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: 58.91 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 32 TELNQKIGDLESQNQELARDNDAINRKIESLTAEIEELRgaeskakRKMGEMEREIdksDEERKVLEAIASRASELETEV 111
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELR-------LEVSELEEEI---EELQKELYALANEISRLEQQK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 112 ARLQHELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVKEENEKRMKELESKLGALE--VKELDEKNKKF 189
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELEsrLEELEEQLETL 384
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15221511 190 RAEE-EMREKIDNKEKEVHDLKEKIKSLESDVAKGKTELQKwiTEKMVVEDSLKDSEKKVVALESEIVELQKQLDDAE 266
Cdd:TIGR02168 385 RSKVaQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE--LLKKLEEAELKELQAELEELEEELEELQEELERLE 460
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
71-278 |
3.35e-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: 58.14 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 71 GAESKAKRKMGEMEREIDKSDEE-----------RKVLEAIASRASELETEVARLQHELITARTEGEEATAEAEKLRSEI 139
Cdd:TIGR02168 663 GGSAKTNSSILERRREIEELEEKieeleekiaelEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 140 SQKGGGIEELEKEVAGLRTVKEENEKRMKELESKLGALEVK--ELDEKNKKFRAE-EEMREKIDNKEKEVHDLKEKIKSL 216
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEieELEAQIEQLKEElKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15221511 217 ESDVAKGKTELQKWITEKMVVEDSLKDSEKKVVALESEIVELQKQLDDAEKMINGLKNVVEE 278
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
33-278 |
3.86e-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: 57.77 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 33 ELNQKIGDLESQNQElardndAINRKIESLTAEIEELRGAESKAKRKMGEMEREIDKSDEERkvlEAIASRASELETEVA 112
Cdd:TIGR02169 276 ELNKKIKDLGEEEQL------RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEI---DKLLAEIEELEREIE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 113 RLQHELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVKEENEKRMKELESKLGALevkeLDEKNKKFRAE 192
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL----QEELQRLSEEL 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 193 EEMREKIDNKEKEVHDLKEKIKSLESDVAKGKTELQKWITEKMVVEDSLKDS-------EKKVVALESEIVELQKQLDDA 265
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLkeeydrvEKELSKLQRELAEAEAQARAS 502
|
250
....*....|...
gi 15221511 266 EKMINGLKNVVEE 278
Cdd:TIGR02169 503 EERVRGGRAVEEV 515
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
58-267 |
4.01e-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: 57.76 E-value: 4.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 58 KIESLTAEIEELRGAESKAKRKMGEMEREIDKSDEErkvLEAIASRASELETEVARLQHELITARTEGEEATAEAEKLRS 137
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEK---LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 138 EISQKGGGIEELEKEVAGLRTVKEENEKRMKELESKLGAL--EVKELDEKNKKFRAE-EEMREKIDNKEKEVHDLKEKIK 214
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELkeELESLEAELEELEAElEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15221511 215 SLESDVAKGKTELQkwitekmVVEDSLKDSEKKVVALESEIVELQKQLDDAEK 267
Cdd:TIGR02168 390 QLELQIASLNNEIE-------RLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
22-253 |
6.21e-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: 57.39 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 22 SDQQGDDGKSTELNQKIGDLESQNQELARDNDAINRKIESLTAEIEELRGAESKAKRKMGEMEREIDKS---------DE 92
Cdd:TIGR02169 723 KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSripeiqaelSK 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 93 ERKVLEAIASRASELETEVARLQHELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVKEENEKRMKELES 172
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 173 KLGALEvKELDEKNKKFRA----EEEMREKIDNKEKEVHDLKEKIKSLESDVA---KGKTELQKWITEKMVVEDSLKDSE 245
Cdd:TIGR02169 883 RLGDLK-KERDELEAQLRElerkIEELEAQIEKKRKRLSELKAKLEALEEELSeieDPKGEDEEIPEEELSLEDVQAELQ 961
|
....*...
gi 15221511 246 KKVVALES 253
Cdd:TIGR02169 962 RVEEEIRA 969
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
33-227 |
3.18e-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: 51.98 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 33 ELNQKIGDLESQNQELARDNDAINRKIESLTAEIEELRGAESKAKRKMGEMEREID----KSDEERKVLEAIASRASELE 108
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEelkeELESLEAELEELEAELEELE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 109 TEVARLQHELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVKEENEKRMKELESKLGALEVKELD-EKNK 187
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEeELEE 451
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15221511 188 KFRAEEEMREKIDNKEKEVHDLKEKIKSLESDVAKGKTEL 227
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
55-278 |
5.46e-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: 51.21 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 55 INRKIESLTAEIEELRGAeSKAKRKMGEMEREIDKSDEERKVLEAIASrasELETEVARLQhelITARTEGEEATAEAEK 134
Cdd:TIGR02168 150 IEAKPEERRAIFEEAAGI-SKYKERRKETERKLERTRENLDRLEDILN---ELERQLKSLE---RQAEKAERYKELKAEL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 135 LRSEISQKGGGIEELEKEVAGLRTVKEENEKRMKELESKLGALEVKeLDEKNKKFRaeeEMREKIDNKEKEVHDLKEKIK 214
Cdd:TIGR02168 223 RELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK-LEELRLEVS---ELEEEIEELQKELYALANEIS 298
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15221511 215 SLESDVAKGKTELQKWITEKMVVEDSLKDSEKKVVALESEIVELQKQLDDAEKMINGLKNVVEE 278
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE 362
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
33-258 |
5.51e-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: 51.21 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 33 ELNQKIGDLESQNQELARDNDAINRKIESLTAEIEELRGAESKAKRKMGEMEREIDksdEERKVLEAIASRASELETEVA 112
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA---ATERRLEDLEEQIEELSEDIE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 113 RLQHELitartegEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVKEENEKRMKELESKLGALEvKELDEKNKKFRAE 192
Cdd:TIGR02168 856 SLAAEI-------EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR-RELEELREKLAQL 927
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15221511 193 EEMREKIDNKEKEvhdLKEKIKslesdvAKGKTELQKWITEKMVVEDSLKDSEKKVVALESEIVEL 258
Cdd:TIGR02168 928 ELRLEGLEVRIDN---LQERLS------EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
53-277 |
7.92e-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: 50.83 E-value: 7.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 53 DAINRKIESLTAEIEELRGAESKAKRKMGEMEREIDKSDEERKV-LEAIASRASELETEVARLQHELITARTEGEEATAE 131
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 132 AEKLRSEISQKGGGIEELEKEVAGLRTVKEENEKRMKELESKLGALEVKELDEKNKKFRAEEEMRE---KIDNKEKEVHD 208
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEElesKLDELAEELAE 341
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15221511 209 LKEKIKSLESDVAKGKTELQKWITEKMVVEDSLKDSEKKVVALESEIVELQKQLDDAEKMINGLKNVVE 277
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
43-267 |
9.21e-07 |
|
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: 49.76 E-value: 9.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 43 SQNQELARDNDAINRKIESLTAEIEELRGAESKAKRKMGEMEREIDKSDEERKVLEAiasRASELETEVARLQHELITAR 122
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ---ELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 123 TEGEEATAEAEKLRSEISQKG-----------GGIEELEKEVAGLRTVKEENEKRMKELESKLGALEvkeldeknkkfRA 191
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA-----------AL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15221511 192 EEEMREKIDNKEKEVHDLKEKIKSLESDVAKGKTELQKWITEKMVVEDSLKDSEKKVVALESEIVELQKQLDDAEK 267
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
33-222 |
1.43e-06 |
|
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: 49.38 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 33 ELNQKIGDLESQNQELARDNDAINRKIESLTAEIEELRGAESKAKRKMGEMEREIDKSDEERKVLEA-IASRASELETEV 111
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAeLEAQKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 112 ARLQH-------ELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVKEENEKRMKELESKLGALEVKELD- 183
Cdd:COG4942 111 RALYRlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAl 190
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15221511 184 --EKNKKFRAEEEMREKIDNKEKEVHDLKEKIKSLESDVAK 222
Cdd:COG4942 191 eaLKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
57-261 |
2.32e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 57 RKIESLTaEIEELRGAESKAKRKMGEMEREIDKSD--EERKVLEAIASRASELETEVARLQHELITARTEGEEATAEAEK 134
Cdd:COG4913 249 EQIELLE-PIRELAERYAAARERLAELEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 135 LRSEISQKGGG-IEELEKEVAGLRTVKEENEKRMKELESKLGALEVKELDEknkkfraeeemREKIDNKEKEVHDLKEKI 213
Cdd:COG4913 328 LEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS-----------AEEFAALRAEAAALLEAL 396
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15221511 214 KSLESDVAKGKTELqkwitekmvvEDSLKDSEKKVVALESEIVELQKQ 261
Cdd:COG4913 397 EEELEALEEALAEA----------EAALRDLRRELRELEAEIASLERR 434
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
29-251 |
4.69e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 29 GKSTELNQKIGDLESQ-NQELARDNDAINRKIESLTAEIEELRGAESKAKRKMGEMEREIDKSDEERKVLEAIASRASEL 107
Cdd:COG4717 35 GKSTLLAFIRAMLLERlEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 108 ETEVARLQHELitartEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVKEENEKRMKELESKLGALEVKELDEKNK 187
Cdd:COG4717 115 REELEKLEKLL-----QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15221511 188 KFRAEEEMREKIDNKEKEVHDLKEKIKSLESDVAKGKTELQKWITEKMVVEDSLKDSEKKVVAL 251
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
32-277 |
5.63e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 32 TELNQKIGDLESQNQELARDNDAINRKIESLTAEIEELRGAESKAkrkmgemereIDKSDEERKVLEAIASRASELETEV 111
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDL----------LAEAGLDDADAEAVEARREELEDRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 112 ARLQHELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVKEENEKRMKELESKLGALEvKELDEKNKKF-- 189
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELE-EEIEELRERFgd 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 190 ------RAE---EEMREKIDNKEKEVHDLKEKIKSLESDVAKGKTELQ--KWITEKMVVEDS-----LKDSEKKVVALES 253
Cdd:PRK02224 403 apvdlgNAEdflEELREERDELREREAELEATLRTARERVEEAEALLEagKCPECGQPVEGSphvetIEEDRERVEELEA 482
|
250 260
....*....|....*....|....
gi 15221511 254 EIVELQKQLDDAEKMINGLKNVVE 277
Cdd:PRK02224 483 ELEDLEEEVEEVEERLERAEDLVE 506
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
33-187 |
1.68e-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: 45.91 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 33 ELNQKIGDLESQNQELARDNDAINRKIESLTAEIEELRGAESKAKRKMGEMEREIDK----------------------- 89
Cdd:COG4942 59 ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRlgrqpplalllspedfldavrrl 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 90 ------SDEERKVLEAIASRASELETEVARLQHELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVKEEN 163
Cdd:COG4942 139 qylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
170 180
....*....|....*....|....
gi 15221511 164 EKRMKELESKLGALEVKELDEKNK 187
Cdd:COG4942 219 QQEAEELEALIARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
82-274 |
1.84e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 82 EMEREIDKSDEERKVLEAIASRASELETEVARLQH-ELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVK 160
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAElEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 161 EENEKRMKELESKLGALEVKELDEKNKKFRAEEEMREKIDNKEKEVHDLKEKIKSLESDVAKGKTELQK-WITEKMVVED 239
Cdd:COG4913 319 DALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAeAAALLEALEE 398
|
170 180 190
....*....|....*....|....*....|....*
gi 15221511 240 SLKDSEKKVVALESEIVELQKQLDDAEKMINGLKN 274
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
36-222 |
2.44e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 36 QKIGDLESQNQELARDNDAINRKIESLTAEIEELRGAESKAKRKMGEMEREIDKSDEERKVLEAIASRASELET--EVAR 113
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASsdDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 114 LQHELITARTEGEEATAEAEKLRSEISQkgggieeLEKEVAGLRTVKEENEKRMKELESKLGALEVKELDEKNKKFRAEE 193
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGR-------LEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
170 180
....*....|....*....|....*....
gi 15221511 194 EMREKIDNKEKEVHDLKEKIKSLESDVAK 222
Cdd:COG4913 763 VERELRENLEERIDALRARLNRAEEELER 791
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
37-264 |
2.75e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 37 KIGDLESQNQELARDNDAINRKIESLTAEIEELRgaeSKAKRKMGEMEREIDKSDEErkvleaiasrASELETEVARLQH 116
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQR---KKNGENIARKQNKYDELVEE----------AKTIKAEIEELTD 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 117 ELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLR------TVK---EENEKRMKELESKLgalevkelDEKNK 187
Cdd:PHA02562 242 ELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcpTCTqqiSEGPDRITKIKDKL--------KELQH 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221511 188 KFRAEEEMREKIDNKEKEVHDLKEKIKSLESDVAKGKTELQKWITEKMVVEDSLKDSEKKVVALESEIVELQKQLDD 264
Cdd:PHA02562 314 SLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDK 390
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
89-267 |
9.66e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 9.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 89 KSDEERKVLEAIASRASELETEVARLQHELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVKEENEKRMK 168
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 169 ELESKLGALEVKELDEKnkkfRAEEEMREKIDNKEKEVHDLKEKIKSLESDVAKGKTELQKWITEKMVVEDSLKDSEKKV 248
Cdd:COG1196 299 RLEQDIARLEERRRELE----ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170
....*....|....*....
gi 15221511 249 VALESEIVELQKQLDDAEK 267
Cdd:COG1196 375 AEAEEELEELAEELLEALR 393
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
120-225 |
1.06e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 120 TARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVKEENEKRMKELESKLgaleVKELDEKNKKFRAEEE---MR 196
Cdd:COG2433 396 EAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLEREL----SEARSEERREIRKDREisrLD 471
|
90 100
....*....|....*....|....*....
gi 15221511 197 EKIDNKEKEVHDLKEKIKSLESDVAKGKT 225
Cdd:COG2433 472 REIERLERELEEERERIEELKRKLERLKE 500
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
33-284 |
1.33e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 33 ELNQKIGDLESQNQELARDNDAINRKIESLTAEIEELRGAES---KAKRKMGEMEREIDKSDEE-------------RKV 96
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEelkKAKGKCPVCGRELTEEHRKelleeytaelkriEKE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 97 LEAIASRASELETEVARLQHELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVKEENEKRMKELESKLGA 176
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 177 LEVKELDEKNKkfraeEEMREKIDNKEKEVHDLKEKIKSLESDVAKGKTELQKWITEKMVVEDSLKDSEKKVVALESEIV 256
Cdd:PRK03918 548 LEKLEELKKKL-----AELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK 622
|
250 260
....*....|....*....|....*...
gi 15221511 257 ELQKQLDDAEKMINGLKNVVEEPLNGIE 284
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLEELRKELE 650
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
74-278 |
1.52e-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: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 74 SKAKRKMGEMEREIDksdEERKVLEAIASRASELETEVARLQHELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEV 153
Cdd:COG4942 23 AEAEAELEQLQQEIA---ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 154 AGLRTV---------KEENEKRMKEL---ESKLGALEVKELDEKNKKFRAE--EEMREKIDNKEKEVHDLKEKIKSLESD 219
Cdd:COG4942 100 EAQKEElaellralyRLGRQPPLALLlspEDFLDAVRRLQYLKYLAPARREqaEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15221511 220 VAKGKTELQKWITEKMVVEDSLKDSEKKVVALESEIVELQKQLDDAEKMINGLKNVVEE 278
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
58-169 |
1.64e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 58 KIESLTAEIEELRgaeskakRKMGEMEREIDKSDEERKvlEAIASRASELETEVARLQHELITAR---TEGEEATAEAEK 134
Cdd:COG0542 405 EIDSKPEELDELE-------RRLEQLEIEKEALKKEQD--EASFERLAELRDELAELEEELEALKarwEAEKELIEEIQE 475
|
90 100 110
....*....|....*....|....*....|....*
gi 15221511 135 LRSEISQKGGGIEELEKEVAGLRTVKEENEKRMKE 169
Cdd:COG0542 476 LKEELEQRYGKIPELEKELAELEEELAELAPLLRE 510
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
24-267 |
1.99e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 24 QQGDDGKSTELNQKIGDLESQNQElARDNDAINRKIESLTAEIEELRGAESKAKRKMGEMEREIDKSDEERKVLEAIAsR 103
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA-E 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 104 ASELETEVARLQHELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVKEENEKRMKELESKLGALEVKELD 183
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAD 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 184 EKNKKF---RAEEEMREKIDNKEKEVHDLKEKIKSLESDVAKGKTElqkwiTEKMVVEDSLKDSEKKVVALESEIVELQK 260
Cdd:PTZ00121 1448 EAKKKAeeaKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE-----EAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
....*..
gi 15221511 261 QLDDAEK 267
Cdd:PTZ00121 1523 KADEAKK 1529
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
106-267 |
3.07e-04 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 41.61 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 106 ELETEVARLQHELITARTEGEEATAEAEKLrsEISQKGGGIEELEKEVAGLrtvKEENEK---RMKELESKLGALevkeL 182
Cdd:pfam15294 90 ELLEQIAEFEEREFTSSNKKPNFELNKPKL--EPLNEGGGSALLHMEIERL---KEENEKlkeRLKTLESQATQA----L 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 183 DEKNKKFRAEEEMREKIDNKEKEVHDLKEkIKSLESDVAKGKTELQKWITEKMVVEDSLkdsEKKVVALESEIVELQKQL 262
Cdd:pfam15294 161 DEKSKLEKALKDLQKEQGAKKDVKSNLKE-ISDLEEKMAALKSDLEKTLNASTALQKSL---EEDLASTKHELLKVQEQL 236
|
....*
gi 15221511 263 DDAEK 267
Cdd:pfam15294 237 EMAEK 241
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
28-268 |
3.78e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 28 DGKSTELNQKIGDLESQNQELARDNDAINRKIESLTAEIEELRGAESKAKRKMGEMEreiDKSDEERKVLEAIASRASEL 107
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE---DFLEELREERDELREREAEL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 108 ETEVARLQHELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVKEENEKRMKELESKLGALE--VKELDEK 185
Cdd:PRK02224 432 EATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEdlVEAEDRI 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 186 NKKFRAEEEMREKIDNKEKEVHDLKEKIKSLESDVAKGKTELQKWITEKMVVEDSLKDSEKKVVALESEIVELQKQLDDA 265
Cdd:PRK02224 512 ERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL 591
|
...
gi 15221511 266 EKM 268
Cdd:PRK02224 592 ERI 594
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
29-222 |
3.89e-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: 42.35 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 29 GKSTELNQKIGDLESQNQELARDNDAINRKIESLTAEIEELRGAESKAKRKMGEMEREIDKSDEERKVLEAIASRAS--- 105
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRsel 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 106 --------ELETEVARLQHELITARTEGEEATAEAEKLRSEISQKGGGI--------EELEKEVAGLRTVKEENEKRMKE 169
Cdd:TIGR02168 897 eelseelrELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeysltlEEAEALENKIEDDEEEARRRLKR 976
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15221511 170 LESKLgalevKELDEKNkkFRAEEEMR---EKIDNKEKEVHDLKEKIKSLESDVAK 222
Cdd:TIGR02168 977 LENKI-----KELGPVN--LAAIEEYEelkERYDFLTAQKEDLTEAKETLEEAIEE 1025
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
30-274 |
3.90e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 30 KSTELNQKIGDLESQNQELARDNDAINRKIESLTAEIEELRGAESKAKRKMGEMEREIDKSDEERKVLEAIAS----RAS 105
Cdd:TIGR04523 392 QINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTREsletQLK 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 106 ELETEVARLQHELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVKEENEKRMKELESKLGALE--VKELD 183
Cdd:TIGR04523 472 VLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEdeLNKDD 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 184 EKNKKFRAEEEmrekIDNKEKEVHDLKEKIKSLESDVAKGKTELQKWITEKMVVEDSLKDSEKKVVALESEIVELQKQLD 263
Cdd:TIGR04523 552 FELKKENLEKE----IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENE 627
|
250
....*....|.
gi 15221511 264 DAEKMINGLKN 274
Cdd:TIGR04523 628 KLSSIIKNIKS 638
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
33-158 |
3.95e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 33 ELNQKIGDLESQNQELArdndAINRKIESLTAEIEELRGAESKAKRKMGEMEREIDKSDEERKVLEAIASRASELETEVa 112
Cdd:COG4913 672 ELEAELERLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE- 746
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 15221511 113 rlQHELITARTEGEEATAEAEKLRSEISQKgggIEELEKEVAGLRT 158
Cdd:COG4913 747 --LRALLEERFAAALGDAVERELRENLEER---IDALRARLNRAEE 787
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
28-205 |
5.67e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 28 DGKSTELNQKIGDLESQNQELARDNDAINRKIESLTAEIEELRGAESKAKRKMGEMEREIDKSDEE----RKVLEAIA-- 101
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEieerREELGERAra 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 102 ------------------------SRASELETEVARLQHELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLR 157
Cdd:COG3883 95 lyrsggsvsyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15221511 158 TVKEENEKRMKELESKLGALEVKELDEKNKKFRAEEEMREKIDNKEKE 205
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
54-266 |
5.81e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 54 AINRKIESLTAEIEELRGAESKAKRKMGEMEREIDKSDEERKVLEAIASRASELETEVARLQHELITARTEGEEATAEAE 133
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 134 KLRSEISqkgGGIEELEKEVAGLRTVKEENEKRMKELESKLGALEVKELDEKNKKFRAEEEmREKIDNKEKEVHDLKEKI 213
Cdd:PRK02224 290 ELEEERD---DLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL-REDADDLEERAEELREEA 365
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15221511 214 KSLESDVAKGKTELQkwitekmvvedslkDSEKKVVALESEIVELQKQLDDAE 266
Cdd:PRK02224 366 AELESELEEAREAVE--------------DRREEIEELEEEIEELRERFGDAP 404
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
30-224 |
6.35e-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: 41.29 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 30 KSTELNQKIGDLESQNQELARDNDAINRKIESLTAEIEELRGAESKAKRKMGEMEREIDK---------SDEERKVL--- 97
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlgRQPPLALLlsp 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 98 ---EAIASRASELETEVARLQHELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVKEENEKRMKELESKL 174
Cdd:COG4942 129 edfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15221511 175 GALEvKELDEKNKKfraEEEMREKIDNKEKEVHDLKEKIKSLESDVAKGK 224
Cdd:COG4942 209 AELA-AELAELQQE---AEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
91-264 |
6.46e-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: 40.68 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 91 DEERKVLEAIASRASELETEVARLQHELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVKEEN--EKRMK 168
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEalQKEIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 169 ELESKLGALEVKELdeknkkfraeeEMREKIDNKEKEVHDLKEKIKSLESDVAKGKTELqkwitekmvvEDSLKDSEKKV 248
Cdd:COG1579 100 SLKRRISDLEDEIL-----------ELMERIEELEEELAELEAELAELEAELEEKKAEL----------DEELAELEAEL 158
|
170
....*....|....*.
gi 15221511 249 VALESEIVELQKQLDD 264
Cdd:COG1579 159 EELEAEREELAAKIPP 174
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
146-281 |
9.08e-04 |
|
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: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 146 IEELEKEVAGLRTVKEENEKRMKELESKLGALEvkELDEKNKKFRAEEEMREKIDNKEKEVHDLKEKIKSLE---SDVAK 222
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQ--ERREALQRLAEYSWDEIDVASAEREIAELEAELERLDassDDLAA 689
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 15221511 223 GKTELQKWITEKMVVEDSLKDSEKKVVALESEIVELQKQLDDAEKMINGLKNVVEEPLN 281
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
32-267 |
1.00e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 32 TELNQKIGDLESQNQELARDNDAINRKIESLTAEIEELRGAESKAKRKMGEMEREIDKSDEERKVLEAIASRASELETEV 111
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 112 ARLqhelitarTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVKEENEKRMKELESKLGALE-----VKELDEKN 186
Cdd:PRK03918 283 KEL--------KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEelkkkLKELEKRL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 187 KKFRAEEEMREKIDNKEKEVHDLKEKIKSLESDvaKGKTELQKWITEKMVVEDSLKDSEKKVVALESEIVELQKQLDDAE 266
Cdd:PRK03918 355 EELEERHELYEEAKAKKEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
.
gi 15221511 267 K 267
Cdd:PRK03918 433 K 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
57-264 |
1.33e-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: 40.44 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 57 RKIESLTAEIEELRGAESKAKRKMGEMEREIDKSDEER-KVLEAIASRASELETEVARLQHELitartegeeataeaEKL 135
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREReKAERYQALLKEKREYEGYELLKEK--------------EAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 136 RSEISQKGGGIEELEKEVAGLRTVKEENEKRMKELESKLGALEVK---ELDEKNKKFRAE-EEMREKIDNKEKEVHDLKE 211
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKikdLGEEEQLRVKEKiGELEAEIASLERSIAEKER 315
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15221511 212 KIKSLESDVAKGKTELQKWITEKMVVEDSLKDSEKKVVALESEIVELQKQLDD 264
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED 368
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
33-273 |
1.94e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 39.67 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 33 ELNQKIGDLESQNQELARDNDAINRKIESLTAEIEELRGAESKAKRKMGEMEREIDKSDEERKVLE----AIASRASELE 108
Cdd:pfam19220 73 GLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEeenkALREEAQAAE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 109 TEVARLQHELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAglrtvkeENEKRMKELESKLGALEVKELDEKNKK 188
Cdd:pfam19220 153 KALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLA-------ELETQLDATRARLRALEGQLAAEQAER 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 189 FRAEEEMREKIDNKEKEVHDLKEKIKSL-------ESDVAKGKTELQKWITEKMVVEDSLKDSEKKVVALESEIVELQKQ 261
Cdd:pfam19220 226 ERAEAQLEEAVEAHRAERASLRMKLEALtaraaatEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEAD 305
|
250
....*....|..
gi 15221511 262 LDDAEKMINGLK 273
Cdd:pfam19220 306 LERRTQQFQEMQ 317
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-267 |
2.04e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 2 AEERSLNGEATGQDDESFFDSDQQGDDGKSTELNQKIGDL----ESQNQELARDNDAINRKIESLTAEieELRGAESKAK 77
Cdd:PTZ00121 1124 AEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDArkaeEARKAEDAKKAEAARKAEEVRKAE--ELRKAEDARK 1201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 78 RKMGEMEREIDKSDEERKVLEAIASRASELETEVARLQHELITA-RTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGL 156
Cdd:PTZ00121 1202 AEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAeEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAD 1281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 157 RTVKEENEKRMKELESKLGALEVKELDEKNKKFRAEEEMREKIDNKEKEVHDLKEKiksleSDVAKGKTELQKWITEKmv 236
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKK-----AEEAKKAAEAAKAEAEA-- 1354
|
250 260 270
....*....|....*....|....*....|.
gi 15221511 237 VEDSLKDSEKKVVALESEIVELQKQLDDAEK 267
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
197-278 |
2.12e-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: 39.36 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 197 EKIDNKEKEVHDLKEKIKSLESDVAKGKTELQKWITEKMVVEDSLKDSEKKVVALESEIVELQKQLDDAEKMINGLKNVV 276
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
..
gi 15221511 277 EE 278
Cdd:COG4942 100 EA 101
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
43-261 |
2.29e-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: 39.72 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 43 SQNQELARDNDAINRKIESLTAEIEELRGA---ESKAKRKMGEMEREIDKSDEERKvlEAIASRASELETEVARlqhELI 119
Cdd:pfam17380 375 SRMRELERLQMERQQKNERVRQELEAARKVkilEEERQRKIQQQKVEMEQIRAEQE--EARQREVRRLEEERAR---EME 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 120 TARTEGEEATAEAEKLRSEISQKGGGIEELEKEVaglRTVKEENEKRMKELESKLGALEVKELDEKNKKFRAEEEMREki 199
Cdd:pfam17380 450 RVRLEEQERQQQVERLRQQEEERKRKKLELEKEK---RDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEE-- 524
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15221511 200 dnKEKEVHDLKEKIKSLESDVAKGKTELQKWITEKMVV---EDSLKDSEKKVVALESEIVELQKQ 261
Cdd:pfam17380 525 --RQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKateERSRLEAMEREREMMRQIVESEKA 587
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
53-184 |
2.42e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.46 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 53 DAINRKIESLTAEIEELRGAESKAK-RKMGEMEREIDKSDEERKVLEAIAS----RASELETEVARLQHELITARTEGEE 127
Cdd:COG2433 380 EALEELIEKELPEEEPEAEREKEHEeRELTEEEEEIRRLEEQVERLEAEVEeleaELEEKDERIERLERELSEARSEERR 459
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15221511 128 ATAEaeklRSEISQKGGGIEELEKEVAGLRTVKEENE------KRMKELESKLGALEVKELDE 184
Cdd:COG2433 460 EIRK----DREISRLDREIERLERELEEERERIEELKrklerlKELWKLEHSGELVPVKVVEK 518
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
30-278 |
3.05e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 30 KSTELNQKIGDLESQNQELARDNDAInRKIESLTAEIEELRGAESKAKRKMGEMEREIDKSDEERKVLEAIASRASELET 109
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEA-KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 110 EVARLQHELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVKEENEKRMKELESKLGALEVKELDEKNKKF 189
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV 1635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 190 RAEEEMREKIDNKEKEVHDLKEKIKSLESDVAKGKTELQKWITEKMVVEDSLKDSEKKVVALESE---IVELQKQLDDAE 266
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEakkAEELKKKEAEEK 1715
|
250
....*....|..
gi 15221511 267 KMINGLKNVVEE 278
Cdd:PTZ00121 1716 KKAEELKKAEEE 1727
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
32-277 |
3.13e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 39.34 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 32 TELNQKIGDLESQNQELARDNDAINRKIESLTAEIEELRGAESKAKrkmgEMEREIDKSDEERKVLEAIAS---RASELE 108
Cdd:pfam05557 128 QSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIK----ELEFEIQSQEQDSEIVKNSKSelaRIPELE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 109 TEVARLQHElitartegeeataeAEKLRSEIsqkgGGIEELEKEVAGLRTVKEENEKRMKE---LESKLGALEvKELDEK 185
Cdd:pfam05557 204 KELERLREH--------------NKHLNENI----ENKLLLKEEVEDLKRKLEREEKYREEaatLELEKEKLE-QELQSW 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 186 NKKF-------RAEEEMREKIDNKEKEVHDLKEKIKSLESDVAKGKTELQKWITEKMVVEDSLKDSEKKVVALESEIVEL 258
Cdd:pfam05557 265 VKLAqdtglnlRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRL 344
|
250
....*....|....*....
gi 15221511 259 QKQLDDAEKMINGLKNVVE 277
Cdd:pfam05557 345 QRRVLLLTKERDGYRAILE 363
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
76-272 |
3.74e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 76 AKRKMGEMEREIDKSDEErkvLEAIASRASELETEVARL--QHELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEV 153
Cdd:COG4913 608 NRAKLAALEAELAELEEE---LAEAEERLEALEAELDALqeRREALQRLAEYSWDEIDVASAEREIAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 154 AGLRTVKEenekRMKELESKLGALEvkelDEKNKKFRAEEEMREKIDNKEKEVHDLKEKIKSLESDVAKGKTELqkwiTE 233
Cdd:COG4913 685 DDLAALEE----QLEELEAELEELE----EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL----LE 752
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15221511 234 KMVVEDSLKDSEKKVVA-LESEIVELQKQLDDAEKMINGL 272
Cdd:COG4913 753 ERFAAALGDAVERELREnLEERIDALRARLNRAEEELERA 792
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
144-292 |
5.05e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 38.07 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 144 GGIEELEKEVAGLRTVKEENEKRMKELESKLGALeVKELDEKNKKFRAEEEM-REKIDNKEKEVHDLKEKIKSLESDVAK 222
Cdd:smart00787 144 GLKEGLDENLEGLKEDYKLLMKELELLNSIKPKL-RDRKDALEEELRQLKQLeDELEDCDPTELDRAKEKLKKLLQEIMI 222
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15221511 223 GKTELQKWITEKMVVEDSLKDSEKKVVALESEIVELQKQLDDAEKM----INGLKNVVE--EPLNGIEFKSWSPNV 292
Cdd:smart00787 223 KVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFtfkeIEKLKEQLKllQSLTGWKITKLSGNT 298
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
46-222 |
5.80e-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: 37.60 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 46 QELARDNDAINRKIESLTAEIEELRGAESKAKRKMGEMEREIDKSDEERKVLEaiaSRASELETEVARLQHELITARTEG 125
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLE---LEIEEVEARIKKYEEQLGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 126 EeataeaeklrseisqkgggIEELEKEVAGLRTVKEENEKRMKELESKLGALEVKELDEKNKKFRAEEEMREKIDNKEKE 205
Cdd:COG1579 90 E-------------------YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170
....*....|....*..
gi 15221511 206 VHDLKEKIKSLESDVAK 222
Cdd:COG1579 151 LAELEAELEELEAEREE 167
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
99-278 |
9.17e-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: 37.44 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 99 AIASRASELETEVARLQHELITARTEGEEATAEAEKLRSEISQKGGGIEELEKEVAGLRTVKEENEKRMKELESKLGALE 178
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 179 vKELDEKNKKFRA------------------------------------EEEMREKIDNKEKEVHDLKEKIKSLESDVAK 222
Cdd:COG4942 97 -AELEAQKEELAEllralyrlgrqpplalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15221511 223 GKTELQKWITEKMVVEDSLKDSEKKVVALESEIVELQKQLDDAEKMINGLKNVVEE 278
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
30-274 |
9.48e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 37.69 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 30 KSTELNQKIGDLESQNQELARDNDAINRKIESLTAEIEElrgAESKAKRKMGEMEREIDKSDEERKVLEAIASRASELET 109
Cdd:TIGR04523 212 KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN---TQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 110 EVARLQHELITARTEGEEATAEAEK------------LRSEISQKGGGIEELEKEVAGLRTVKE----ENEKRMKELESK 173
Cdd:TIGR04523 289 QLNQLKSEISDLNNQKEQDWNKELKselknqekkleeIQNQISQNNKIISQLNEQISQLKKELTnsesENSEKQRELEEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 174 LGALEV------KELDEKNKKFRAEEEMREKIDNKEKEVHDLKEKIKSLESDVAKGKTELQKWITEKMVVEDSLKDSEKK 247
Cdd:TIGR04523 369 QNEIEKlkkenqSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ 448
|
250 260
....*....|....*....|....*..
gi 15221511 248 VVALESEIVELQKQLDDAEKMINGLKN 274
Cdd:TIGR04523 449 DSVKELIIKNLDNTRESLETQLKVLSR 475
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
33-278 |
9.79e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 37.60 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 33 ELNQKIGDLesQNQELARDNDAINRKIESLTAEIEELRGAESKAKRKMGEMEREIDKSDEER-----KVLEAIASRASEL 107
Cdd:PRK05771 35 DLKEELSNE--RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEElekieKEIKELEEEISEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 108 ETEVARLQHELITARTEGEEATAEAEKLRSE-ISQKGGGIEE-------LEKEVAGLRTVKEENEKR------MKELESK 173
Cdd:PRK05771 113 ENEIKELEQEIERLEPWGNFDLDLSLLLGFKyVSVFVGTVPEdkleelkLESDVENVEYISTDKGYVyvvvvvLKELSDE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221511 174 LGAlEVKELDEKNKKFRAEEEMREKIDNKEKEVHDLKEKIKSLESDVAKGKTELQKWI----------TEKMVVEDSLKD 243
Cdd:PRK05771 193 VEE-ELKKLGFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELlalyeyleieLERAEALSKFLK 271
|
250 260 270
....*....|....*....|....*....|....*
gi 15221511 244 SEkKVVALESEIVElqkqlDDAEKMINGLKNVVEE 278
Cdd:PRK05771 272 TD-KTFAIEGWVPE-----DRVKKLKELIDKATGG 300
|
|
| |
