|
Name |
Accession |
Description |
Interval |
E-value |
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
83-797 |
0e+00 |
|
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.
Pssm-ID: 462863 [Multi-domain] Cd Length: 717 Bit Score: 1061.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 83 GQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLTSVAQELKEINQNVEIQRGR 162
Cdd:pfam09730 1 GQSVSSHKKVAADGESREESLLQESASKEAYYAQRILELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 163 LRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEE 242
Cdd:pfam09730 81 MRDEIKEYKVREARLLQDYSELEEENISLQKQVSVLKQNQVEFEGLKHEITRKEEETELLNSQLEEAIRLREIAERQLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 243 ALETLKTEREQKNNLRKELSHYMSINDSFYTSHLQVSLDGLKFSDD-TVTAEPNNDAEALvNGFEHS--GLVKSSLDNKT 319
Cdd:pfam09730 161 ALETLKTEREQKNSLRKELSHYMTLNDFDYVSHLSISLDGLKFSEDeGAGTEPNNDGEAM-DGGENGggGLKNSGLDNRT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 320 STPRKDGLAPPSPSLVSDLLSELHISEIQKLKQQLVQMEREKVGLLATLQDTQKQLEQARGTLSEQHEKVNRLTENLSAL 399
Cdd:pfam09730 240 STPRKSEVFPPAPSLVSDLLSELNISEIQKLKQQLIQVEREKVSLLSTLQESQKQLEQAKGALSEQQEKVNRLTENLEAM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 400 RRLQAGKERQTSLDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAE 479
Cdd:pfam09730 320 RGLQASKERQDALDSEKDRDSHEDGDYYEVDINGPEILECKYRVAVEEAGELREELKALKARYNTLEERYKEEKTRWEAE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 480 GQALTEKISLLEKASHQDRELLAHLEKELKKVSDVAGETQGSLNVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYY 559
Cdd:pfam09730 400 AQDLAEKIRQLEKASHQDQERIAHLEKELGKTRKVAGESEGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYY 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 560 REGQGK-AGRTSPEGRGRRSPVLLPKGLLATEVGRADGGtGDNSPSPSSSLPSPLSDPRREPMNIYNLIAIIRDQIKHLQ 638
Cdd:pfam09730 480 REGAGArARKSHQEPRGLRSPRLLTRGLFMGEVGTADTT-SNSPSPCSSCPGSPTSDFRREPMNIYNLVAIIRDQIKHLQ 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 639 AAVDRTTELSRQRIASQELGPAVDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSKYENEKAMV 718
Cdd:pfam09730 559 VAVDRTTELSRQRGAALELSTESDKDKEALMEEILKLKSLLSTKREQIATLRTVLKANKQTAEVALANLKSKYENEKAMV 638
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 85702355 719 TETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLELLEL 797
Cdd:pfam09730 639 TETMMKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLEDLEF 717
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
5-510 |
1.25e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 5 SEEEEYARLVMEAQPEWLRAEVKRLSHELAETTREKIQAAEyglavleEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQ 84
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA-------ELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 85 AHTNHKKVAADGESREESLIQESASKEqyyvrkvlELQTELKQLRNVLTNTQSE----NERLTSVAQELKEINQNVEIQR 160
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLE--------ELEEELAELEEELEELEEEleelEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 161 GRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQL 240
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 241 EEALETLKTEREQKNNLRKELShymSINDSFYTSHLQVSLDGLKFSDDTVTAEPNNDAEALVNGFEHSGLVKSSLDNKTS 320
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLA---ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 321 TPRKDGLAPPSPSLVSDLLSELhiseiqkLKQQLVQMEREKVGLLATLQDTQKQLEQARGT-LSEQHEKVNRLTENLSAL 399
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALEAA-------LAAALQNIVVEDDEVAAAAIEYLKAAKAGRATfLPLDKIRARAALAAALAR 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 400 RRLQAGKERQTSLDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAE 479
Cdd:COG1196 595 GAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL 674
|
490 500 510
....*....|....*....|....*....|.
gi 85702355 480 GQALTEKISLLEKASHQDRELLAHLEKELKK 510
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEE 705
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
23-262 |
6.73e-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: 66.23 E-value: 6.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 23 RAEVKRLSHELAETTrEKIQAAEYGLAVLEEKHQ-LKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGEsREE 101
Cdd:TIGR02168 676 RREIEELEEKIEELE-EKIAELEKALAELRKELEeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA-QLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 102 SLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLTSVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDY 181
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 182 SELEEENISLQKQvsvLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNNLRKEL 261
Cdd:TIGR02168 834 AATERRLEDLEEQ---IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
.
gi 85702355 262 S 262
Cdd:TIGR02168 911 S 911
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6-264 |
4.26e-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: 63.54 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 6 EEEEYARLVMEAQPEWLRAEVKRLSHELAETTREkIQAAEYGLAVLEEKH-QLKLQFEELEVDYEAIRSEMEQLK----- 79
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEE-LEELTAELQELEEKLeELRLEVSELEEEIEELQKELYALAneisr 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 80 -EAFGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLTSVAQELKEINQNVEI 158
Cdd:TIGR02168 300 lEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 159 QRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQ--VEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEIS 236
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeeLLKKLEEAELKELQAELEELEEELEELQEELERL 459
|
250 260
....*....|....*....|....*...
gi 85702355 237 ERQLEEALETLKTEREQKNNLRKELSHY 264
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQL 487
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
38-261 |
5.81e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 5.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 38 REKIQAAEYgLAVLEEKHQLK-----LQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREESLIQESASKEq 112
Cdd:COG1196 207 RQAEKAERY-RELKEELKELEaelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 113 yyvrkvlELQTELKQLRNVLTNTQSENERLTSVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQ 192
Cdd:COG1196 285 -------EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 85702355 193 KQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNNLRKEL 261
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
5-264 |
1.65e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 5 SEEEEYARLVMEAQPEWLRAEVKRLSHELaETTREKIQAAEYGLAVLE-EKHQLKLQFEELEVDYEAIRSEMEQLKeafg 83
Cdd:TIGR02169 204 RREREKAERYQALLKEKREYEGYELLKEK-EALERQKEAIERQLASLEeELEKLTEEISELEKRLEEIEQLLEELN---- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 84 qahtnhKKVAADGESREESL---IQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLTSVAQELKEinqNVEIQR 160
Cdd:TIGR02169 279 ------KKIKDLGEEEQLRVkekIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELER---EIEEER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 161 GRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEI--------------KRLEEETEYLNSQL 226
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREInelkreldrlqeelQRLSEELADLNAAI 429
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 85702355 227 EDAI--------RLKEI------SERQLEEALETLKTEREQKNNLRKELSHY 264
Cdd:TIGR02169 430 AGIEakineleeEKEDKaleikkQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
22-264 |
4.45e-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: 53.92 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 22 LRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREE 101
Cdd:TIGR02169 707 LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 102 SLiqeSASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLTSVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDY 181
Cdd:TIGR02169 787 RL---SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 182 SELEEENISLQKQVSVLRQnqvEFEGLKHEIKRLEEETEYLNSQLEDAirlkeisERQLEEALETLKTEREQKNNLRKEL 261
Cdd:TIGR02169 864 EELEEELEELEAALRDLES---RLGDLKKERDELEAQLRELERKIEEL-------EAQIEKKRKRLSELKAKLEALEEEL 933
|
...
gi 85702355 262 SHY 264
Cdd:TIGR02169 934 SEI 936
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
6-200 |
2.44e-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: 50.53 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 6 EEEEYARLVMEAQPEWLRAEVKRLSHELAETTReKIQAAEYGLAVLEEK-HQLKLQFEELEVDYEAIRSEM-EQLKEAFG 83
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALAR-RIRALEQELAALEAElAELEKEIAELRAELEAQKEELaELLRALYR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 84 QAHTNHKKVAADGESreeslIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLTSVAQELKEINQNVEIQRGRL 163
Cdd:COG4942 116 LGRQPPLALLLSPED-----FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190
....*....|....*....|....*....|....*..
gi 85702355 164 RDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQ 200
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6-247 |
3.58e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 6 EEEEYARLVMEAQPEWLRAEVKRLS-HELAETTREKIQAAEYGLAVLEEKHQ-LKLQFEELEVDYEAIRSEMEQLKEAFG 83
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEElEAQIEQLKEELKALREALDELRAELTlLNEEAANLRERLESLERRIAATERRLE 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 84 QAHTNHKKVAADGESREESLIQESASKEqyyvrkvlELQTELKQLRNVLTNTQSE----NERLTSVAQELKEINQNV--- 156
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELIE--------ELESELEALLNERASLEEAlallRSELEELSEELRELESKRsel 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 157 EIQRGRLRDDIKEYKFREARLLQDYSEL-----EEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAI- 230
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLqerlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIe 993
|
250 260
....*....|....*....|....*.
gi 85702355 231 RLKEISERQ---------LEEALETL 247
Cdd:TIGR02168 994 EYEELKERYdfltaqkedLTEAKETL 1019
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
97-539 |
3.65e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 97 ESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLTSVAQELKEINQNVEIQRGRLRDdiKEYKFREAR 176
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK--LEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 177 LLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIR-LKEISERQLEEALETLKTEREQKN 255
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEELQQRLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 256 NLRKELSHYMSINDSFYTSHLQVSLDGLKFSDDTVTAEPNNDAEALVNGFEHSGLVKSSLDNKTSTP------------R 323
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvlgllalL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 324 KDGLAPPSPSLVSDLLSELHISEIQKLKQQLVQMEREKVGLLATLQDTqkQLEQARGTLSEQHEKVNRLTENLSALRRLQ 403
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE--ELLELLDRIEELQELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 404 AGKERQTSLDNEKDRDsheDGDYYEVDINGPEilackYHVAVAEAGELREQLKALRSTHEAREAQHAEEkgRYEAEGQAL 483
Cdd:COG4717 368 LEQEIAALLAEAGVED---EEELRAALEQAEE-----YQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEEL 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 85702355 484 TEKISLLEKASHQDRELLAHLEKELKKVsdvagETQGSLNVAQDELVTFSEELANL 539
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQL-----EEDGELAELLQELEELKAELREL 488
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
20-301 |
8.83e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 49.52 E-value: 8.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 20 EWLRAEVKRLSHELAET-TREKIQAAEYGLAVLEEKHQLKLQfEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGES 98
Cdd:PLN02939 166 EALQGKINILEMRLSETdARIKLAAQEKIHVEILEEQLEKLR-NELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQF 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 99 REESLIQESASKEQYYVrkvLE-----LQTELKQLRNVLTNTQSENERLTSVAQE-LKEINQNVEIQRGRLRDDIKEYkf 172
Cdd:PLN02939 245 LKAELIEVAETEERVFK---LEkerslLDASLRELESKFIVAQEDVSKLSPLQYDcWWEKVENLQDLLDRATNQVEKA-- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 173 reARLLQDYSELEEENISLQ---KQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKT 249
Cdd:PLN02939 320 --ALVLDQNQDLRDKVDKLEaslKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKE 397
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 85702355 250 EREqknnlRKELSHYMSINDSFYTSHLQVSLDGLKFSDDTvtaePNNDAEAL 301
Cdd:PLN02939 398 ESK-----KRSLEHPADDMPSEFWSRILLLIDGWLLEKKI----SNNDAKLL 440
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
20-229 |
9.45e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 9.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 20 EWLRAEVKRLSHELAETtREKIQA--AEYGLAVLEEKHQLKL-QFEELEVDYEAIRSEMEQLKEAFGQAhtnhKKVAADG 96
Cdd:COG3206 178 EFLEEQLPELRKELEEA-EAALEEfrQKNGLVDLSEEAKLLLqQLSELESQLAEARAELAEAEARLAAL----RAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 97 ESREESLIQESAskEQYYVRKVLELQTELKQLRNVLTntqSENERLTSVAQELKEINQNVEIQRGRLRDDIK-EYKFREA 175
Cdd:COG3206 253 PDALPELLQSPV--IQQLRAQLAELEAELAELSARYT---PNHPDVIALRAQIAALRAQLQQEAQRILASLEaELEALQA 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 85702355 176 RLlqdySELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDA 229
Cdd:COG3206 328 RE----ASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
32-261 |
9.97e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.33 E-value: 9.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 32 ELAETTREKIQAAEYGLAVLEEKHQLKL-QFEELEVDYEAIRSEMEQLKEAFGQAHT------NHKKVAADGESREESL- 103
Cdd:pfam05483 363 ELLRTEQQRLEKNEDQLKIITMELQKKSsELEEMTKFKNNKEVELEELKKILAEDEKlldekkQFEKIAEELKGKEQELi 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 104 --------------IQESASK--EQYYVRKVLELQTELKQLRNVLTNTQSENERLTSVAQELKEINQNVEIQRGRLRDDI 167
Cdd:pfam05483 443 fllqarekeihdleIQLTAIKtsEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDI 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 168 KEYKFREARLLQDYSELEEENISLQKQVSVLRQnqvEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETL 247
Cdd:pfam05483 523 INCKKQEERMLKQIENLEEKEMNLRDELESVRE---EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNL 599
|
250
....*....|....
gi 85702355 248 KTEREQKNNLRKEL 261
Cdd:pfam05483 600 KKQIENKNKNIEEL 613
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
346-522 |
1.85e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 346 EIQKLKQQLVQMEREKVGLLATLQDTQKQLEQARGTLSEQHEKVNRLTENLSALRRLQAGKERQTSLDNEKDRDSHEDGD 425
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 426 YYEVDIngpEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAEGQALTEKISLLEKASHQDRELLAHLE 505
Cdd:COG1196 320 ELEEEL---AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170
....*....|....*..
gi 85702355 506 KELKKVSDVAGETQGSL 522
Cdd:COG1196 397 ELAAQLEELEEAEEALL 413
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
52-809 |
1.86e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 52 EEKHQLKLQFEELEV-----DYEAIRSEMEQLKEAFGQAHTNHKkvaadgesREESLIQESASKEQYYVRKVLELQTELK 126
Cdd:TIGR02168 213 ERYKELKAELRELELallvlRLEELREELEELQEELKEAEEELE--------ELTAELQELEEKLEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 127 QLRNVLTNTQSENERLTSVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKqvsvlrqnqvEFE 206
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE----------ELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 207 GLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNNLRKELshymsindsfytSHLQVSLDGLKfs 286
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL------------ERLEDRRERLQ-- 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 287 ddtvtaepnndaealvngfehsglvkssldnktstprkdglappspSLVSDLLSELHISEIQKLKQQLVQMEREKVGLLA 366
Cdd:TIGR02168 421 ----------------------------------------------QEIEELLKKLEEAELKELQAELEELEEELEELQE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 367 TLQDTQKQLEQARGTLSEQHEKVNRLTENLSALRRLQAGKERQ------------TSLDNEKDRDSHED--GDYYEVDin 432
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLqenlegfsegvkALLKNQSGLSGILGvlSELISVD-- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 433 gpeilaCKYHVAVAEAGELREQLKALRSTHEAREAQhaeekgryEAEGQALTEKISLLEKASHQDRELLAHLEKELKKVS 512
Cdd:TIGR02168 533 ------EGYEAAIEAALGGRLQAVVVENLNAAKKAI--------AFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIE 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 513 DVAGetqgslnvAQDELVTFSEE----LANLYHHVCMCNNETPNRVMLDYYREGQ----------GKAGRTSPEGRGRRS 578
Cdd:TIGR02168 599 GFLG--------VAKDLVKFDPKlrkaLSYLLGGVLVVDDLDNALELAKKLRPGYrivtldgdlvRPGGVITGGSAKTNS 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 579 PVLLPKGLLATEVGRADGGTGD----------------NSPSPSSSLPSPLSDPRREPMNIYNLIAIIRDQIKHLQAAVD 642
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKiaelekalaelrkeleELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 643 RT-----------TELSRQRIASQELGPAVDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSkY 711
Cdd:TIGR02168 751 QLskelteleaeiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES-L 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 712 ENEKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDE-------MQRQLAAAEDEKKTLNSLLRMAIQQ 784
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnerasLEEALALLRSELEELSEELRELESK 909
|
810 820
....*....|....*....|....*
gi 85702355 785 KLALTQRLELLELDHEQTRRGRSKA 809
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGL 934
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
6-271 |
1.90e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 6 EEEEYARLVMEAQPEwLRAEVKRLSHELAETtREKIQAAEyglAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQa 85
Cdd:TIGR02169 781 LNDLEARLSHSRIPE-IQAELSKLEEEVSRI-EARLREIE---QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK- 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 86 htnhkkvaadgesREESLIQESASKEQyyvrKVLELQTELKQLRNVLTNTQSENERLTSVAQELKEINQNVEIQRGRLRD 165
Cdd:TIGR02169 855 -------------EIENLNGKKEELEE----ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 166 DIKEYKFREARLLQDYSELEEENISLQKQVSvlrqNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISER---QLEE 242
Cdd:TIGR02169 918 RLSELKAKLEALEEELSEIEDPKGEDEEIPE----EELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKrldELKE 993
|
250 260 270
....*....|....*....|....*....|....*...
gi 85702355 243 ALETLKTER-------EQKNNLRKE--LSHYMSINDSF 271
Cdd:TIGR02169 994 KRAKLEEERkaileriEEYEKKKREvfMEAFEAINENF 1031
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
22-262 |
2.58e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 22 LRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREE 101
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 102 SLIQESASKEQYYVRKVlELQTELKQLRNVLTNTQSE--NERLTSVAQELKEINQNVEIQRGRLRD---DIKEYKFREAR 176
Cdd:TIGR02169 752 EIENVKSELKELEARIE-ELEEDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREieqKLNRLTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 177 LLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYlnsqledairlkeiSERQLEEALETLKTEREqknN 256
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA--------------ALRDLESRLGDLKKERD---E 893
|
....*.
gi 85702355 257 LRKELS 262
Cdd:TIGR02169 894 LEAQLR 899
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
100-262 |
4.82e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.38 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 100 EESLIQESASKEQYYVRKVLELQTELKQLRnvltntqsenerltSVAQELKEINQNVEIQRGRLRDDIKEYKfreaRLLQ 179
Cdd:COG5022 938 NNIDLEEGPSIEYVKLPELNKLHEVESKLK--------------ETSEEYEDLLKKSTILVREGNKANSELK----NFKK 999
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 180 DYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQ--LEDAIRLKEISERQLEEALETLKTEREQKNNL 257
Cdd:COG5022 1000 ELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILkpLQKLKGLLLLENNQLQARYKALKLRRENSLLD 1079
|
....*
gi 85702355 258 RKELS 262
Cdd:COG5022 1080 DKQLY 1084
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6-540 |
5.80e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 6 EEEEYARLVMEAQPEWLRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAfGQA 85
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ-IAS 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 86 HTNH----KKVAADGESREESLIQESASKEQYYVR-KVLELQTELKQLRNVLTNTQSENERLTSVAQELKEINQNVEIQR 160
Cdd:TIGR02168 398 LNNEierlEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 161 GRLRDDIKEYKFREARLlqdySELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIR-----LKEI 235
Cdd:TIGR02168 478 DAAERELAQLQARLDSL----ERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGgrlqaVVVE 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 236 SERQLEEALETLKTEREQKNNLRKELSHYMSINDSFYTSHLQVSLDGLKFSDDTVTAEPnnDAEALVNGFEHSGLVKSSL 315
Cdd:TIGR02168 554 NLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDP--KLRKALSYLLGGVLVVDDL 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 316 DNKTSTPRK----------DG--------LAPPSPSLVSDLLS-----ELHISEIQKLKQQLVQMEREKVGLLATLQDTQ 372
Cdd:TIGR02168 632 DNALELAKKlrpgyrivtlDGdlvrpggvITGGSAKTNSSILErrreiEELEEKIEELEEKIAELEKALAELRKELEELE 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 373 KQLEQARGTLSEQHEKVNRLTENLSALR-RLQAGKERQTSLDNE-KDRDSHEDGDYYEVDINGPEILACKYHVAVAEA-- 448
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEaEVEQLEERIAQLSKElTELEAEIEELEERLEEAEEELAEAEAEIEELEAqi 791
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 449 GELREQLKALRSTHEAREAQHAEEKGRYeaegQALTEKISLLEKASHQDRELLAHLEKELKKVSDVAGETQGSLNVAQDE 528
Cdd:TIGR02168 792 EQLKEELKALREALDELRAELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL 867
|
570
....*....|..
gi 85702355 529 LVTFSEELANLY 540
Cdd:TIGR02168 868 IEELESELEALL 879
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
116-253 |
6.63e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 6.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 116 RKVLELQTELKQLRNVLTNTQSENERLTSVAQELKeinqnveiQRGRLRDDIKEYKFREarllQDYSELEEENISLQKQV 195
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQ--------ERREALQRLAEYSWDE----IDVASAEREIAELEAEL 677
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 85702355 196 SVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQ 253
Cdd:COG4913 678 ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
345-510 |
8.87e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 8.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 345 SEIQKLKQQLVQMEREKVGLLATLQDTQKQLEQARGTLSEQHEKVNRLTENLSALR-RLQAGKERQTSLDNEKDRDSHED 423
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEaRIKKYEEQLGNVRNNKEYEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 424 gdyyEVDINGPEILACKYHV--AVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAEGQALTEKISLLEKAShqdRELL 501
Cdd:COG1579 97 ----EIESLKRRISDLEDEIleLMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER---EELA 169
|
....*....
gi 85702355 502 AHLEKELKK 510
Cdd:COG1579 170 AKIPPELLA 178
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
60-507 |
2.26e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 60 QFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAAdGESREESLIQESASKEQyyVRKVLELQTELKQLRNVLtntQSEN 139
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEE-LEAELEELREELEKLEK--LLQLLPLYQELEALEAEL---AELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 140 ERLTSVAQELKEInQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENIS-LQKQVSVLRQNQVEfegLKHEIKRLEEE 218
Cdd:COG4717 146 ERLEELEERLEEL-RELEEELEELEAELAELQEELEELLEQLSLATEEELQdLAEELEELQQRLAE---LEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 219 TEYLNSQLEDAIRLKEIS--ERQLEEALETLKTEREQKNNLRKELSHYMSINDSFYTSHLQVSLDGLKFSDDT-VTAEPN 295
Cdd:COG4717 222 LEELEEELEQLENELEAAalEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLArEKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 296 NDAEALVNGFEHSGLVKSSLDNKTStpRKDGLAPPSPSLVSDLLSelHISEIQKLKQQLVQMEREKvgLLATLQDTQKQL 375
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLA--ALGLPPDLSPEELLELLD--RIEELQELLREAEELEEEL--QLEELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 376 EQARGTLSE--------QHEKVNRLTENLSALRR--LQAGKERQTSLDNEKDRDSHEDGDYYEVDIngpEILACKYHVAV 445
Cdd:COG4717 376 LAEAGVEDEeelraaleQAEEYQELKEELEELEEqlEELLGELEELLEALDEEELEEELEELEEEL---EELEEELEELR 452
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 85702355 446 AEAGELREQLKALRSTHEAREAQHAEEkgRYEAEGQALTEKISLLEKASHQDRELLAHLEKE 507
Cdd:COG4717 453 EELAELEAELEQLEEDGELAELLQELE--ELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
62-261 |
2.30e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 62 EELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREESLIQESaskeqyyvRKVLELQTELKQLRNVLTNTQSENER 141
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA--------RRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 142 LTSVAQELKE--INQNVEIQRGRLRDDIK--------EYKFREARLLQDYSELEEENI-SLQKQVSVLRQNQVEFEGLKH 210
Cdd:COG4942 95 LRAELEAQKEelAELLRALYRLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAeELRADLAELAALRAELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 85702355 211 EIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNNLRKEL 261
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-494 |
2.45e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 173 REARLLQDYSELEEENISLQKQVSVLRqnqvefeglkheIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTERE 252
Cdd:TIGR02168 207 RQAEKAERYKELKAELRELELALLVLR------------LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 253 QKNNLRKELSHYMSINDSFYT--SHLQVSLDGLKFSDDTVTAEPNNDAEALVNGFehsglvkssldnktstprkdglapp 330
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANeiSRLEQQKQILRERLANLERQLEELEAQLEELE------------------------- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 331 spslvsdllselhiSEIQKLKQQLVQMEREKVGLLATLQDTQKQLEQARGTLSEQHEKVNRLTENLSALRRLQAGKERQ- 409
Cdd:TIGR02168 330 --------------SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQi 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 410 TSLDNE--------KDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAEGQ 481
Cdd:TIGR02168 396 ASLNNEierlearlERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
330
....*....|...
gi 85702355 482 ALTEKISLLEKAS 494
Cdd:TIGR02168 476 ALDAAERELAQLQ 488
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
110-262 |
3.59e-04 |
|
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: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 110 KEQYYVRKVLELQTELKQLRNVLTNTQSENERLTSVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENI 189
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 85702355 190 SLQKQVSVLRQnqvefeglkhEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNNLRKELS 262
Cdd:COG1196 299 RLEQDIARLEE----------RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
345-540 |
3.88e-04 |
|
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: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 345 SEIQKLKQQLVQMEREKVGLLATLQDTQKQLEQARGTLSEQHEKVNRLTENLSALRRLQAGKERQTSLDNEKDRDSHEDG 424
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 425 DYYEVDINGPEilackyhVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAEGQALTEKISLLEKASHQDRELLAHL 504
Cdd:COG1196 347 EEAEEELEEAE-------AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
170 180 190
....*....|....*....|....*....|....*.
gi 85702355 505 EKELKKVSDVAGETQGSLNVAQDELVTFSEELANLY 540
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
22-205 |
5.54e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 22 LRAEVKRLS-----HELAETTREKIQAAEYGLAVL------EEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTN-- 88
Cdd:COG4913 247 AREQIELLEpirelAERYAAARERLAELEYLRAALrlwfaqRRLELLEAELEELRAELARLEAELERLEARLDALREEld 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 89 --HKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNV-LTNTQSEnERLTSVAQELKEINQNVEIQRGRLRD 165
Cdd:COG4913 327 elEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALgLPLPASA-EEFAALRAEAAALLEALEEELEALEE 405
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 85702355 166 DIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEF 205
Cdd:COG4913 406 ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
60-263 |
6.27e-04 |
|
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: 43.58 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 60 QFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREESLIQESASKEQyyvrKVLELQTELKQLRNVLTNTQSEN 139
Cdd:pfam05557 59 LLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKN----ELSELRRQIQRAELELQSTNSEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 140 ERLTSVAQELKEINQNVEIQRGRLRDDIKEYKFREARLlqdySELEEEnISLQKQ----VSVLRQNQVEFEGLKHEIKRL 215
Cdd:pfam05557 135 EELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRI----KELEFE-IQSQEQdseiVKNSKSELARIPELEKELERL 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 85702355 216 EEETEYLNSQLEDAIRLKEISErQLEEALETLKTEREQKNNLRKELSH 263
Cdd:pfam05557 210 REHNKHLNENIENKLLLKEEVE-DLKRKLEREEKYREEAATLELEKEK 256
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
22-261 |
7.15e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 22 LRAEVKRLS--HELAETTREKIQAaeygLAVLEEKHQlklQFEELEVDYEAIRSEMEQLKEAFGQahtnhkKVAADGESR 99
Cdd:COG4913 230 LVEHFDDLEraHEALEDAREQIEL----LEPIRELAE---RYAAARERLAELEYLRAALRLWFAQ------RRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 100 EESLIQESASKEQyyvrKVLELQTELKQLRNVLTNTqsENERLTSVAQELKEINQnveiQRGRLRDDIKEYKFREARLLQ 179
Cdd:COG4913 297 LEELRAELARLEA----ELERLEARLDALREELDEL--EAQIRGNGGDRLEQLER----EIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 180 DYSELEEEnislqkqvsvLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTERE----QKN 255
Cdd:COG4913 367 LLAALGLP----------LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslerRKS 436
|
....*.
gi 85702355 256 NLRKEL 261
Cdd:COG4913 437 NIPARL 442
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
346-513 |
8.18e-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: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 346 EIQKLKQQLVQMEREKVGLLATLQDTQKQLEQARGTLSEQHEKVNRLTENLSALRRLQAgkERQTSLDNEKDR------- 418
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA--ELRAELEAQKEElaellra 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 419 --------------------DSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEA 478
Cdd:COG4942 113 lyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190
....*....|....*....|....*....|....*
gi 85702355 479 EGQALTEKISLLEKASHQDRELLAHLEKELKKVSD 513
Cdd:COG4942 193 LKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
23-260 |
1.47e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 23 RAEVKRLSHELAETTREKIQAAEYGLAVLEEK--HQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESRE 100
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 101 ESLIQESASKEQYyVRKVLELQT--ELK---QLRNVLTNTQSENERLTSV--AQELKEINQNVEIQRGRLRDDIKEYKFR 173
Cdd:PTZ00121 1532 EAKKADEAKKAEE-KKKADELKKaeELKkaeEKKKAEEAKKAEEDKNMALrkAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 174 EARLLQDYSELEEE---NISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEdaiRLKEISERQLEEALETLKTE 250
Cdd:PTZ00121 1611 EAKKAEEAKIKAEElkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA---KKAEEDKKKAEEAKKAEEDE 1687
|
250
....*....|
gi 85702355 251 REQKNNLRKE 260
Cdd:PTZ00121 1688 KKAAEALKKE 1697
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
120-261 |
1.64e-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: 41.93 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 120 ELQTELKQLRNVLTNTQSENERLTSVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLR 199
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 85702355 200 QnqvEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNNLRKEL 261
Cdd:TIGR04523 433 E---TIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
22-502 |
1.73e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 22 LRAEVKRLSHELAETTREKIQAAEY---GLAVLEEKHQLKLQFEELEVDYEAIR---SEMEQLKEAFGQAHTNHKKVAAD 95
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETrdeADEVLEEHEERREELETLEAEIEDLRetiAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 96 GESREESLIQE----SASKEQYYVRKVlELQTELKQLRnvltntqsenERLTSVAQELKEINQNVEiqrgRLRDDIKEYK 171
Cdd:PRK02224 291 LEEERDDLLAEagldDADAEAVEARRE-ELEDRDEELR----------DRLEECRVAAQAHNEEAE----SLREDADDLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 172 FREARLLQDYSELEEEnisLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAirlkeisERQLEEALETLKTER 251
Cdd:PRK02224 356 ERAEELREEAAELESE---LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA-------EDFLEELREERDELR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 252 EQKNNLRKELShymsindsfytshlqvsldglkfsddtvTAEPN-NDAEALVNgfehsglvkssldnktstprkdglAPP 330
Cdd:PRK02224 426 EREAELEATLR----------------------------TARERvEEAEALLE------------------------AGK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 331 SPSLVSDLLSELHISEIQKLKQQLVQMEREKVGLLATLQDTQKQLEQARgTLSEQHEKVNRLTENLSALRRLQAGKERQT 410
Cdd:PRK02224 454 CPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETI 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 411 SLDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEA----GELREQLKALRSTHEA--REAQHAEEKGRYEAEGQALT 484
Cdd:PRK02224 533 EEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAreevAELNSKLAELKERIESleRIRTLLAAIADAEDEIERLR 612
|
490
....*....|....*...
gi 85702355 485 EKISLLEKASHQDRELLA 502
Cdd:PRK02224 613 EKREALAELNDERRERLA 630
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
113-265 |
1.89e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 113 YYVRKVLeLQTELKQLRNVLTNTQSENERLTSVAQELKEINQNVEIQRGR------LRDDIKEYKFREARLLQDYSELEE 186
Cdd:PRK12704 22 YFVRKKI-AEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRnefekeLRERRNELQKLEKRLLQKEENLDR 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 85702355 187 ENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDaiRLKEISERQLEEALETLKTEREQKnnLRKELSHYM 265
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ--ELERISGLTAEEAKEILLEKVEEE--ARHEAAVLI 175
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
22-256 |
2.38e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 22 LRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAhtnhkkvaadgESREE 101
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL-----------EKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 102 SLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLTSVAQELKEINQNVEIQRGRLRDDIKEykfrearLLQDY 181
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-------LAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 85702355 182 SELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNN 256
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
109-425 |
2.50e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.58 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 109 SKEQYYVRKVLELQTELKQLRNVLTNTQSEneRLTSVAQELKEINQNV------EIQRGrLRDDIKEYKFREARLLQDYS 182
Cdd:TIGR01612 489 SKQDNTVKLILMRMKDFKDIIDFMELYKPD--EVPSKNIIGFDIDQNIkaklykEIEAG-LKESYELAKNWKKLIHEIKK 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 183 ELEEEN---ISLQKQVSVLRQ------------NQVEFEgLKHEIKRLEEETEYLnsqlEDAIRLKEISERQLEEALETL 247
Cdd:TIGR01612 566 ELEEENedsIHLEKEIKDLFDkyleiddeiiyiNKLKLE-LKEKIKNISDKNEYI----KKAIDLKKIIENNNAYIDELA 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 248 KTEREQknnlrkeLSHYMSINDSFYTshlqvsldglkfsddTVTAEPN----NDAEALVNgfEHSGLVK-SSLDNKTSTP 322
Cdd:TIGR01612 641 KISPYQ-------VPEHLKNKDKIYS---------------TIKSELSkiyeDDIDALYN--ELSSIVKeNAIDNTEDKA 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 323 RKDGLAPPSPSLVSDLLS------ELHISEIQKLKQQL----VQMEREKVGLLA-----TLQD---TQKQLEQARGTLSE 384
Cdd:TIGR01612 697 KLDDLKSKIDKEYDKIQNmetatvELHLSNIENKKNELldiiVEIKKHIHGEINkdlnkILEDfknKEKELSNKINDYAK 776
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 85702355 385 QHEKVNRLTENLSALRrlqAGKERQTSLDNEKDRDSHEDGD 425
Cdd:TIGR01612 777 EKDELNKYKSKISEIK---NHYNDQINIDNIKDEDAKQNYD 814
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
22-261 |
2.69e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 22 LRAEVKRLSHELA--ETTREKIQAAEYGLA-VLEEKHQLKLQFEELEVDYEAIRSEMEQLKEafgqahtnHKKVAADGES 98
Cdd:PRK03918 174 IKRRIERLEKFIKrtENIEELIKEKEKELEeVLREINEISSELPELREELEKLEKEVKELEE--------LKEEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 99 REESLIQESASkeqyyvrkvleLQTELKQLRNVLTNTQSENERLTSVAQELKEINQNVE--IQRGRLRDDIKEYKFREAR 176
Cdd:PRK03918 246 ELESLEGSKRK-----------LEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEeyIKLSEFYEEYLDELREIEK 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 177 LLQDYSE----LEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTERE 252
Cdd:PRK03918 315 RLSRLEEeingIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE 394
|
....*....
gi 85702355 253 QKNNLRKEL 261
Cdd:PRK03918 395 ELEKAKEEI 403
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
5-353 |
4.27e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.98 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 5 SEEEEYARLVMEAQPEWLR---AEVKRLSHELAETTREKIQAAEYGLAVLEekHQLKLQFEELEVDYEAIRsemEQLKEA 81
Cdd:pfam12128 638 SREETFARTALKNARLDLRrlfDEKQSEKDKKNKALAERKDSANERLNSLE--AQLKQLDKKHQAWLEEQK---EQKREA 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 82 FGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKqlrNVLTNTQSENERLTSVAQELKEINQNVEIQRG 161
Cdd:pfam12128 713 RTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYK---RDLASLGVDPDVIAKLKREIRTLERKIERIAV 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 162 RlRDDIKEY-KFREARLLQdyseleeENISLQKQVSVLRQNQVEfegLKHEIKRLEEETEYLNSQLEDAIRLKEISERQL 240
Cdd:pfam12128 790 R-RQEVLRYfDWYQETWLQ-------RRPRLATQLSNIERAISE---LQQQLARLIADTKLRRAKLEMERKASEKQQVRL 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 241 EEALETLKTEREQKNNLRK---------ELSHYMSINDSFYTSHLQVSLDGLKFSDDTVTAEPNNDAEALVNGFEhsglv 311
Cdd:pfam12128 859 SENLRGLRCEMSKLATLKEdanseqaqgSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWE----- 933
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 85702355 312 kSSLDNKTSTPRKDGLAPPSPSLV---SDLLSELHISEIQKLKQQ 353
Cdd:pfam12128 934 -SLREEDHYQNDKGIRLLDYRKLVpylEQWFDVRVPQSIMVLREQ 977
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
16-198 |
5.76e-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: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 16 EAQPEWLRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVaad 95
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY--- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 96 gESREESLIQESASKEQYYVRKVLELQ---TELKQLRNVLTNTQSE----NERLTSVAQELKEINQNVEiqrgRLRDDIK 168
Cdd:TIGR02169 391 -REKLEKLKREINELKRELDRLQEELQrlsEELADLNAAIAGIEAKinelEEEKEDKALEIKKQEWKLE----QLAADLS 465
|
170 180 190
....*....|....*....|....*....|
gi 85702355 169 EYKFREARLLQDYSELEEENISLQKQVSVL 198
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKELSKLQRELAEA 495
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
22-472 |
8.27e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.82 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 22 LRAEVKRLSHELA---ETTREKIQAAEYGLAVLEEKHQ--LKLQFEELEVDYE---AIRSEMEQLKEAFGQAHTNHKKVA 93
Cdd:pfam12128 295 LDDQWKEKRDELNgelSAADAAVAKDRSELEALEDQHGafLDADIETAAADQEqlpSWQSELENLEERLKALTGKHQDVT 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 94 ADGESREESLiqesaskeqyyvrkVLELQTELKQLRNVLTNTQSENERLTSVA-----QELKEINQNVEIQRGRLRDDIK 168
Cdd:pfam12128 375 AKYNRRRSKI--------------KEQNNRDIAGIKDKLAKIREARDRQLAVAeddlqALESELREQLEAGKLEFNEEEY 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 169 EYKFR--EARLLQDYSELEEENIsLQKQVSVLRQN--QVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEAL 244
Cdd:pfam12128 441 RLKSRlgELKLRLNQATATPELL-LQLENFDERIEraREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQ 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 245 ETLKTEREQKNNLRKELSHYMSINDSFYTSHLQVSLDGLKFSDDTVTAEPNNDAEALVNGFEHSGLVKSSLDNKTSTPRK 324
Cdd:pfam12128 520 SALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASE 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 325 DGLAPPSPSLVSDLLSELhiSEIQKLKQQLVQMEREKVGLLATLQDTQKQLEQAR---GTLSEQHEKVNRLTENLSALRR 401
Cdd:pfam12128 600 EELRERLDKAEEALQSAR--EKQAAAEEQLVQANGELEKASREETFARTALKNARldlRRLFDEKQSEKDKKNKALAERK 677
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 85702355 402 LQAGKERQtSLDNEKDRDSHEDGDYYE-VDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEE 472
Cdd:pfam12128 678 DSANERLN-SLEAQLKQLDKKHQAWLEeQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAE 748
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
116-261 |
8.40e-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: 38.75 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 116 RKVLELQTELKQLRNVLTNTQSENERLTSVAQELKEINQNVEIQRGRLRDDIKEYKFREARLlQDYSELEEENISLQKQV 195
Cdd:COG1579 7 RALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI-EEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 85702355 196 SvlrqNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNNLRKEL 261
Cdd:COG1579 86 R----NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
32-261 |
9.64e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 32 ELAETTREKIQAAEYGLAVLEEKHQlklQFEELEVDYEAIRSEMEQLKEAFGQAHtnhKKVAADGESREESLIQESASKE 111
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSLKKELE---KLEELKKKLAELEKKLDELEEELAELL---KELEELGFESVEELEERLKELE 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 112 QYYvRKVLELQTELKQLRNVLTNTQSENERLTSVAQELKEINQNVEIQRGRLRDDIKEYKFREarllqdYSELEEENISL 191
Cdd:PRK03918 599 PFY-NEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE------YEELREEYLEL 671
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 192 QKQVSVLRQnqvEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERqLEEALETLKTEREQKNNLRKEL 261
Cdd:PRK03918 672 SRELAGLRA---ELEELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALERVEELREKVKKYKALL 737
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
17-247 |
9.94e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 17 AQPEWLRAEVKRLSHELAETtREKIQAAEYGLAVLEEkhqLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHkkvaadg 96
Cdd:COG4913 654 AEYSWDEIDVASAEREIAEL-EAELERLDASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGRLEKEL------- 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85702355 97 ESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLTSVAQELKEINQNVEIQRGRLRDDIKEYKFREAR 176
Cdd:COG4913 723 EQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPA 802
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 85702355 177 LLQDYSELEEENISLQKQVSVLRQN-----QVEFEGLKHEikRLEEETEYLNSQLEDAIRlkEISER--QLEEALETL 247
Cdd:COG4913 803 ETADLDADLESLPEYLALLDRLEEDglpeyEERFKELLNE--NSIEFVADLLSKLRRAIR--EIKERidPLNDSLKRI 876
|
|
| |
