|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
42-324 |
3.26e-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: 63.15 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 42 KETKDKLKET-----TTKLTQAKEEAEQIRQNCQDMIKTYQESEEiKSNELDAK---LRVTKGELEKQMQEKSDQLEMHH 113
Cdd:TIGR02168 216 KELKAELRELelallVLRLEELREELEELQEELKEAEEELEELTA-ELQELEEKleeLRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 114 AKIKELEDLKRTFKEgmdELRTLRTKAKCLEDERLRTEDELSKYREIINRQKSEIQnlldkvkitdQLHEQLQSGKQEIE 193
Cdd:TIGR02168 295 NEISRLEQQKQILRE---RLANLERQLEELEAQLEELESKLDELAEELAELEEKLE----------ELKEELESLEAELE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 194 HLKEEMESLNSLINDLQKDIEGSRKRESELLlftEKLTSKNAQLQSESSALQSQVDNLSCTESQLQSQCQQMGQANRNLE 273
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLETLRSKVAQLE---LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL 438
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 569006759 274 SKLLKEEELRKEevqTLQAELSAAQTEVKALSTQVEELKDELVTQRRKHAS 324
Cdd:TIGR02168 439 QAELEELEEELE---ELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
74-374 |
2.32e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 74 KTYQESEEIKSNEL----DAKLRVTKGELEKQMQEKSDQLEMHHAKIKELEDLKRTFKEGMDELRTLRTKAKcleDERLR 149
Cdd:COG1196 216 RELKEELKELEAELlllkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ---AEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 150 TEDELSKYREIINRQKSEIQNLLDKVkitDQLHEQLQSGKQEIEHLKEEMESLNSLINDLQKDIEGSRKRESELLLFTEK 229
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERL---EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 230 LTSKNAQLQSESSALQSQVDNLSCTESQLQSQCQQMGQANRNLESKLlkeeelrkeevQTLQAELSAAQTEVKALSTQVE 309
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL-----------ERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569006759 310 ELKDELVTQRRKHAsNVKDLSKQLQQARRKLEQTENGNHDKDISSMGSRSSSSGSLNARISAEDR 374
Cdd:COG1196 439 EEEEALEEAAEEEA-ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
14-314 |
2.52e-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: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 14 EKLKE-EMNSQVIKVKWAQNKLKAEMDSHKETKDKLKETTTKLTQAKEEAEQIRQNcqdmiktyQESEEIKSNELDAKLR 92
Cdd:COG1196 220 EELKElEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE--------LEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 93 VTKGELEKQMQEKSDQLEMHHAKIKELEDLKRtfkegmdELRTLRTKAKCLEDERLRTEDELskyREIINRQKSEIQNLL 172
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEE-------ELAELEEELEELEEELEELEEEL---EEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 173 DKVKITDQLHEQLQSGKQEIEHLKEEMESLNSLINDLQKDIEGSRKRESELLLFTEKLTSKNAQLQSESSALQSQVDNLS 252
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006759 253 CTESQLQSQCQQMGQANRNLESKLLKEEELRKEEVQTLQAELSAAQTEVKALSTQVEELKDE 314
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5-343 |
4.25e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 5 ETTRLIREIEKLKEEMNSQVIKVKWAQNKLKAEMDSHKETKDKLK----ETTTKLTQAKEEAEQIRQNCQDMIKTYQeSE 80
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRkeleELSRQISALRKDLARLEAEVEQLEERIA-QL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 81 EIKSNELDAKLRVTKGELEKQMQEKsdqlemhHAKIKELEDLKRTFKEGMDELRTLRTKAKCLEDERLRTEDEL----SK 156
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEEL-------AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlrER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 157 YREIINRQKSEIQNLLDKVKITDQLHEQLQSGKQEIEHLKEEMESLNSLINDLQKDIEGSRKRESELLLFTEKLTSKNAQ 236
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 237 LQSESSALQSQVDNLSCTESQLQSQCQQMGQANRNLESKLLKEEELRKEEVQTLQ----AELSAAQTEVKALSTQVEELK 312
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEnkieDDEEEARRRLKRLENKIKELG 985
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 569006759 313 D---------ELVTQRRKHASNVKDlskQLQQARRKLEQT 343
Cdd:TIGR02168 986 PvnlaaieeyEELKERYDFLTAQKE---DLTEAKETLEEA 1022
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
8-251 |
4.03e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 8 RLIREIEKLKEEMNSQVIKVKWAQNKLKAEMDSHKETKDKLKETTTKLTQAKEEAEQIRQNCQDMIKTYQESEEIKsnEL 87
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELE--KE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 88 DAKLRVTKGELEKQMQEKSDQLEMHHAKIKELEDLKRTFKE---GMDELRTLRTKAKCLEDERLRTEDELSKYREIINRQ 164
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkeKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 165 KSEIQNLLDKVKITDQLHEQLQSGKQEIEHLKEEMESLNSL------------------INDLQKDIEGSRKRESELLLF 226
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAkakkeelerlkkrltgltPEKLEKELEELEKAKEEIEEE 406
|
250 260
....*....|....*....|....*
gi 569006759 227 TEKLTSKNAQLQSESSALQSQVDNL 251
Cdd:PRK03918 407 ISKITARIGELKKEIKELKKAIEEL 431
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
78-341 |
7.04e-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: 52.38 E-value: 7.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 78 ESEEIKSNELDAKLRVTKGELEKQMQEKSDQLEMHHAKIKELEDLKRTFKEGMDELRTLRTKAKCLEDERLRTEDELSKY 157
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 158 REIINRQKSEIQNLLDKV-KITDQL-HEQLQSGKQEIEHLKEEMESLNSLINDLQKDIEGSRKRESELLLFTEKLTSKNA 235
Cdd:TIGR02169 764 EARIEELEEDLHKLEEALnDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 236 QLQSESSALQSQVDNLSCTESQLQSQCQQMGQANRNLESkllkEEELRKEEVQTLQAELSAAQTEVKALSTQVEELKDEL 315
Cdd:TIGR02169 844 DLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES----RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL 919
|
250 260
....*....|....*....|....*.
gi 569006759 316 VTQRRKhASNVKDLSKQLQQARRKLE 341
Cdd:TIGR02169 920 SELKAK-LEALEEELSEIEDPKGEDE 944
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
5-321 |
8.21e-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: 51.99 E-value: 8.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 5 ETTRLIREIEKLKEEMNSQvikvkwaQNKLKAEMdshKETKDKLKETTTKLTQAKEEAEQIRQNCQDM---IKTYQES-E 80
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQE-------EEKLKERL---EELEEDLSSLEQEIENVKSELKELEARIEELeedLHKLEEAlN 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 81 EIKSNELDAKLRVTKGELEKQMQEKSD---QLEMHHAKIKELEDLKRTFKEGMDELRTLRTKAKCLEDERLRTEDELSKY 157
Cdd:TIGR02169 783 DLEARLSHSRIPEIQAELSKLEEEVSRieaRLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 158 REIINRQKSEIQNLLdkvkitDQLHEQLQSGKQEIEHLKEEMESLNSLINDLQKDIEGSRKRESELLLFTEKLTSKNAQL 237
Cdd:TIGR02169 863 KEELEEELEELEAAL------RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 238 QSESSALQSQVDNLSCTEsQLQSQCQQMGQANRNLESKLLKEEELRKEEVQTLQaELSAAQTEVKALSTQVEELKDELVT 317
Cdd:TIGR02169 937 EDPKGEDEEIPEEELSLE-DVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLD-ELKEKRAKLEEERKAILERIEEYEK 1014
|
....
gi 569006759 318 QRRK 321
Cdd:TIGR02169 1015 KKRE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-349 |
1.08e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 101 QMQEKSDQLEMHHAKIKELE----DLKRTFKEGMDELRTLRTKAKCLEDERLRTEDELSKYREIINRQKSEIQNLLDKVK 176
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEekiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 177 ITD----QLHEQLQSGKQEIEHLKEEMESLNSLINDLQKDIEgsrKRESELLLFTEKLTSKNAQLQSESSALQSQVDNLS 252
Cdd:TIGR02168 751 QLSkeltELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE---QLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 253 CTESQLQSQCQQMGQANRNLE--SKLLKEEELRKEEVQTLQAELSAAQTEVKALSTQVEELKDELVTQRRKHASNVKDLS 330
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEelSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
250
....*....|....*....
gi 569006759 331 KQLQQARRKLEQTENGNHD 349
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQ 926
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
143-342 |
1.19e-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: 50.92 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 143 LEDERLRTEDELSKYREIINRQKSEIQNLLDKVKITDQ----LHEQLQSGKQEIEHLKEEMESLNSLINDLQKDIEGSRK 218
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERriaaLARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 219 RESELL--LFTEKLTSKNAQLQSESSALQSqVDNLSCTESQLQSQCQQMGQANRNLEskllkeeelrkeEVQTLQAELSA 296
Cdd:COG4942 105 ELAELLraLYRLGRQPPLALLLSPEDFLDA-VRRLQYLKYLAPARREQAEELRADLA------------ELAALRAELEA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 569006759 297 AQTEVKALSTQVEELKDELVTQRRKHASNVKDLSKQLQQARRKLEQ 342
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-313 |
2.28e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 2 QEGETTRLIREIEKLKEEMNsqvikvkwaqnKLKAEMDSHKETKDKLKETTTKLTQAKEEAEQIRQNCQDMIKTYQESEE 81
Cdd:TIGR02169 221 REYEGYELLKEKEALERQKE-----------AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 82 IKSNELDAKLRVTKGELEKQMQEKSDQLEMHHAKIKELEDLKRTFKEGMDELRT-LRTKAKcledERLRTEDELSKYREI 160
Cdd:TIGR02169 290 LRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEReIEEERK----RRDKLTEEYAELKEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 161 INRQKSEIQNLLDKVKITDQLHEQLQsgkQEIEHLKEEMESLNSLINDLQkdiEGSRKRESELLLFTEKLTSKNAQLQSE 240
Cdd:TIGR02169 366 LEDLRAELEEVDKEFAETRDELKDYR---EKLEKLKREINELKRELDRLQ---EELQRLSEELADLNAAIAGIEAKINEL 439
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006759 241 SSALQSQVDNLSCTESQLQSQCQQMGQANRNLESKLLKEEELRKEEVQtLQAELSAAQTEVKALSTQVEELKD 313
Cdd:TIGR02169 440 EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK-LQRELAEAEAQARASEERVRGGRA 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
101-342 |
5.90e-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: 5.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 101 QMQEKSDQLEMHHAKIKELEDLKRTFkegmDELRTLRTKAKCLEdeRLRTEDElsKYREIInRQKSEIQNLLDKVKItDQ 180
Cdd:COG4913 216 YMLEEPDTFEAADALVEHFDDLERAH----EALEDAREQIELLE--PIRELAE--RYAAAR-ERLAELEYLRAALRL-WF 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 181 LHEQLQSGKQEIEHLKEEMESLNSLINDLQKDIEGSRKRESELLLftEKLTSKN---AQLQSESSALQSQVDNLSCTESQ 257
Cdd:COG4913 286 AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEA--QIRGNGGdrlEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 258 LQSQCQQMGQANRNLESKLLKEEELRKEEVQTLQAELSAAQTEVKALSTQVEELKDELVTQRRKHAS---NVKDLSKQLQ 334
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASlerRKSNIPARLL 443
|
....*...
gi 569006759 335 QARRKLEQ 342
Cdd:COG4913 444 ALRDALAE 451
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
144-384 |
9.54e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 9.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 144 EDERLRTEDELSKYREIINRQKSEIQNLLDKVkitDQLHEQLQSGKQEIEHLKEEMESLNSLINDLQKDIEGSRKRESEL 223
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAEL---EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 224 LLFTEK----LTSKNAQLQSES-SALQSQVDNLSctesqlqsqcqQMGQANRNLesklLKEEELRKEEVQTLQAELSAAQ 298
Cdd:COG3883 92 ARALYRsggsVSYLDVLLGSESfSDFLDRLSALS-----------KIADADADL----LEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 299 TEVKALSTQVEELKDELVTQRRKHASNVKDLSKQLQQARRKLEQTENGNHDKDISSMGSRSSSSGSLNARISAEDRSPEN 378
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
....*.
gi 569006759 379 TSSSVA 384
Cdd:COG3883 237 AAAAAA 242
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
13-338 |
1.65e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.81 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 13 IEKLKEEMNSQVikvKWAQNKLKAEMDSHKETKDKLKETTTKLTQAKEEAEQIRQNCQDMIKTYQESEEiksnELDAKLR 92
Cdd:pfam15921 76 IERVLEEYSHQV---KDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQE----DLRNQLQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 93 VTKGELEKQMQEKSDQLEMHHAKIKELEDLKRTFKEGMDELRTLRTKAKCLEDERLRTEDELSKY---------REIINR 163
Cdd:pfam15921 149 NTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMhfrslgsaiSKILRE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 164 QKSEIQNLLDKV-KITDQLHEQLQSGKQEIE-HLKEEMESLNSLINDLQKDIEGsrkreselllFTEKLTSKNAQ---LQ 238
Cdd:pfam15921 229 LDTEISYLKGRIfPVEDQLEALKSESQNKIElLLQQHQDRIEQLISEHEVEITG----------LTEKASSARSQansIQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 239 SESSALQSQVDNLS----CTESQLQSQCQQMGQANRNLESKLLKEEELRKEEVQTLQAELSAAQTEVKALSTQVEELKDE 314
Cdd:pfam15921 299 SQLEIIQEQARNQNsmymRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQ 378
|
330 340
....*....|....*....|....
gi 569006759 315 LVTQRRKHASNVKDLSKQLQQARR 338
Cdd:pfam15921 379 LQKLLADLHKREKELSLEKEQNKR 402
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
10-344 |
2.29e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 10 IREIEKLKEEMNSQVIKVKWAQNKLKAEMDSHKETK---DKLKETTTKLTQAKEEAEQIRQNCQDMIKTyqeseeiksne 86
Cdd:PRK02224 215 LAELDEEIERYEEQREQARETRDEADEVLEEHEERReelETLEAEIEDLRETIAETEREREELAEEVRD----------- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 87 ldakLRVTKGELEKQMQEKSDQLEMHHAKIKELEDLKRTfkegmdelrtlrtkakcLEDERLRTEDELSKYREIINRQKS 166
Cdd:PRK02224 284 ----LRERLEELEEERDDLLAEAGLDDADAEAVEARREE-----------------LEDRDEELRDRLEECRVAAQAHNE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 167 EIQNLLDKVKI----TDQLHEQLQSGKQEIEHLKEEMESLNSLINDLQKDIEGSRKRESELLLFTEKLTSKNAQLQSESS 242
Cdd:PRK02224 343 EAESLREDADDleerAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 243 ALQSQVDNLSCTESQLQS------------QCQQMGQANRnlESKLLKEEELRKEEVQTLQAELSAAQTEVKALSTQVEE 310
Cdd:PRK02224 423 ELREREAELEATLRTARErveeaealleagKCPECGQPVE--GSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER 500
|
330 340 350
....*....|....*....|....*....|....*.
gi 569006759 311 LKD--ELVTQRRKHASNVKDLSKQLQQARRKLEQTE 344
Cdd:PRK02224 501 AEDlvEAEDRIERLEERREDLEELIAERRETIEEKR 536
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
86-431 |
9.99e-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: 45.44 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 86 ELDAKLRVTKGELEkQMQEKSDQLEmhhAKIKELedlkrtfKEGMDELRTLRTKAKCLEDERLRTED----ELSKYREII 161
Cdd:TIGR02169 167 EFDRKKEKALEELE-EVEENIERLD---LIIDEK-------RQQLERLRREREKAERYQALLKEKREyegyELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 162 NRQKSEIQNLLDkvkitdQLHEQLQSGKQEIEHLKEEMESLNSLINDLQKDIEgsRKRESELLLFTEKL---TSKNAQLQ 238
Cdd:TIGR02169 236 ERQKEAIERQLA------SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK--DLGEEEQLRVKEKIgelEAEIASLE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 239 SESSALQSQVDNLSCTESQLQSQCQQMGQANRNLESKLLKEEELR---KEEVQTLQAELSAAQTEVKALSTQVEELKDEL 315
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRdklTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 316 vtqrrkhasnvKDLSKQLQQARRKLEQTeNGNHDKDISSMGSRSSSSGSLNARI-SAEDRSPEntSSSVAVDNFPEVDKA 394
Cdd:TIGR02169 388 -----------KDYREKLEKLKREINEL-KRELDRLQEELQRLSEELADLNAAIaGIEAKINE--LEEEKEDKALEIKKQ 453
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 569006759 395 -----MLIERIVRLQKAHARKNEKIEFMEDHIKQLVEEIRKK 431
Cdd:TIGR02169 454 ewkleQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA 495
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
11-431 |
1.03e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 11 REIEKLKEEMNSQVIKVKWAQNKLKAEMDSHKETKDKLKETTTKLTQAKEEAEQIRQNCQDMIKtyqeSEEIKSNELDAK 90
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK----ADEAKKKAEEDK 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 91 LRVTKGELEKQMQEKSDQLEMHHAKIKELEDLKRTFKEG--MDELRTLRTKAKCLEDERLRTEDElskyreiinRQKSEI 168
Cdd:PTZ00121 1405 KKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAkkADEAKKKAEEAKKAEEAKKKAEEA---------KKADEA 1475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 169 QNLLDKVKITDQLHEQLQSGKQEIEHLKEEMESLNSLinDLQKDIEGSRKREsELLLFTEKLTSKNAQLQSESSALQS-- 246
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA--DEAKKAEEAKKAD-EAKKAEEAKKADEAKKAEEKKKADElk 1552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 247 QVDNLSCTESQLQSQCQQMGQANRNLESKLLKEEELRKEEVQTLQAELSAAQTEVKALSTQVEE---LKDELVTQRRKHA 323
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEeakIKAEELKKAEEEK 1632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 324 SNVKDLSKQLQQARRKLEQTENGNHDKDISSMGSRSSSSGslNARISAEDRSPENTSSSVAVDNFPEVDKAMLIERIVRL 403
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE--DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
410 420
....*....|....*....|....*...
gi 569006759 404 QKAHARKNEKIEFMEDHIKQLVEEIRKK 431
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEENKIKAEEAKKE 1738
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
5-144 |
5.89e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 5 ETTRLIREIEKLKEEMNSQVIKVKWAQNKLKAEMdsHKETKDKLKEtttkltqAKEEAEQIRQNCQDMIKtyQESEEIKS 84
Cdd:PRK00409 538 EAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA--EKEAQQAIKE-------AKKEADEIIKELRQLQK--GGYASVKA 606
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006759 85 NELDAKLRvtkgELEKQMQEKSdqlemhhAKIKELEDLKRTFKEGMD-ELRTLRTKAKCLE 144
Cdd:PRK00409 607 HELIEARK----RLNKANEKKE-------KKKKKQKEKQEELKVGDEvKYLSLGQKGEVLS 656
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
83-324 |
7.77e-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: 42.06 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 83 KSNELDAKLRVTKGELEKQMQEKSDQLEMHHAKIKELEDLKRTFKEGMDELRTLRTKAKCLEDERLRTEDELSKYREIIN 162
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 163 RQKSEIQNLLDKV-KITDQLHEQLQSGKQEIEHLKEEMESLNSLINDLQKDIEGSRKReselllfTEKLTSKNAQLQSES 241
Cdd:COG4942 101 AQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD-------LAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 242 SALQSQVDNLSCTESQLQSQCQQMGQANRNLESKLlkeeelrkeevQTLQAELSAAQTEVKALSTQVEELKDELVTQRRK 321
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKEL-----------AELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
...
gi 569006759 322 HAS 324
Cdd:COG4942 243 TPA 245
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
71-345 |
8.63e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 71 DMIKTYQESEEIKSNELDAKLRVTK----GELEKQM---QEKSDQLEMHHAKIKELEDLKRTFKEGMDELRTLRTKAKCL 143
Cdd:pfam15921 415 DHLRRELDDRNMEVQRLEALLKAMKsecqGQMERQMaaiQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 144 EDERLRTEDELSKYREIINRQKSEIQNLLDKVKITDQLHEQLQSGKQEIEHLKEEMESLNSLINDLQKDIEGSRKRESEL 223
Cdd:pfam15921 495 ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENM 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 224 LLFTEKLTSKNAQLQSESSALQSQVDNLSCTESQLQSQCQQMGQANRNLESKLLKEEELRKEEVQT-------------- 289
Cdd:pfam15921 575 TQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAgserlravkdikqe 654
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 569006759 290 ---LQAELSAAQTEVKALSTQVEELKDELVTQRRKHASNVKDLSKQLQQARRKLEQTEN 345
Cdd:pfam15921 655 rdqLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRN 713
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
46-221 |
9.40e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 9.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 46 DKLKETTTKLTQAKEEAEQIRQNCQDMIKTYQESEEIKSNELDAKLRVTKGELEKQMQEKSDQLEMHHAKIKELEDLKRT 125
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 126 FKEGMDELRTLRTKAKCLEDERLRTEDELSKYREIIN-RQKSEIQNLLDKVkitDQLHEQLQSGKQEIEHLKEEMESLNS 204
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEEL---EELQQRLAELEEELEEAQEELEELEE 227
|
170
....*....|....*..
gi 569006759 205 LINDLQKDIEGSRKRES 221
Cdd:COG4717 228 ELEQLENELEAAALEER 244
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
164-345 |
1.07e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 164 QKSEIQNL---LDKVKITDQLHEQLQSGKQEIEHLKEEMESLNSLINDLQKDIEGSRKRESELLLFTE---KLTSKNAQL 237
Cdd:PRK11281 58 DKLVQQDLeqtLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSLRQlesRLAQTLDQL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 238 Q----------SESSALQSQVDNlscTESQLQSQCQQMGQANRNLESKLLKEEELRKEEVQTLQAELSA--AQTEVKALS 305
Cdd:PRK11281 138 QnaqndlaeynSQLVSLQTQPER---AQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALlnAQNDLQRKS 214
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 569006759 306 TQVEELKDELVTQRRKHAS-NVKDLSKQLQ--QA---RRKLEQTEN 345
Cdd:PRK11281 215 LEGNTQLQDLLQKQRDYLTaRIQRLEHQLQllQEainSKRLTLSEK 260
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
183-345 |
1.12e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 183 EQLQSGKQEIEHLKEEMESLNSLINDLQKDIEGSRKRESELLLFTEKLTS--KNAQLQSESSALQSQVDNLSCTESQLQS 260
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDeiDVASAEREIAELEAELERLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 261 QCQQMGQANRNLEsKLLKEEELRKEEVQTLQAELSAAQTEVKALSTQVEELKDELVTQRRKHASN--------------V 326
Cdd:COG4913 690 LEEQLEELEAELE-ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErfaaalgdaverelR 768
|
170
....*....|....*....
gi 569006759 327 KDLSKQLQQARRKLEQTEN 345
Cdd:COG4913 769 ENLEERIDALRARLNRAEE 787
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
14-329 |
1.26e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 14 EKLKEEMNSQVIKVKWAQNKLKAEMDSHKETKDKLKETTTKLTQAKEEAEQIRQNCQDMIKTYQESEEI-KSNELDAKLR 92
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKkKADELKKAEE 1556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 93 VTKGELEKQMQEKSDQLEMHHAKIKELEDLKRTFKEGMDELRTLRTKAKCLEDERLRTEDE-------LSKYREIINRQK 165
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeeLKKAEEEKKKVE 1636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 166 SEIQNLLDKVKITDQLHEQLQSGKQEIEHLKEEMESLNSLINDLQKDIEGSRKREsELLLFTEKLTSKNAQLQSESSALQ 245
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA-EALKKEAEEAKKAEELKKKEAEEK 1715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 246 SQVDNLSCTESQLQSQCQQmgqANRNLESKLLKEEELR-----KEEVQTLQAELSAAQTEVKALSTQV--EELKDELVTQ 318
Cdd:PTZ00121 1716 KKAEELKKAEEENKIKAEE---AKKEAEEDKKKAEEAKkdeeeKKKIAHLKKEEEKKAEEIRKEKEAVieEELDEEDEKR 1792
|
330
....*....|.
gi 569006759 319 RRKHASNVKDL 329
Cdd:PTZ00121 1793 RMEVDKKIKDI 1803
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
13-213 |
2.65e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 13 IEKLKEEMNSQVIKVKWAQNKLKAEMD----SHKETKDKLKETTTKLTQAKEEAEQIRQ---NCQDMIKTYQESEEIKSN 85
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHIQQQIKTYNKnieeQRKKNGENIARKQNKYDELVEEAKTIKAeieELTDELLNLVMDIEDPSA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 86 ELdAKLRVTKGELEKQMQEKSDQLEMHH----------------AKIKELEDLKRTFKEGMDELRTLRTKAKCLEDERLR 149
Cdd:PHA02562 256 AL-NKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctqqisegpDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNE 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006759 150 TEDELSKYREIINRQKSEIQNLLDKVKITDQLHEQLQSG----KQEIEHLKEEMESLNSLINDLQKDI 213
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEfvdnAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
151-347 |
4.17e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 151 EDELSKYREIINRQKSEIQNLLDKVKITD------QLHEQLQSGKQEIEHLKEEMESLNSLINDLQKDIEGSRKRESELL 224
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLVDlseeakLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 225 LfteklTSKNAQLQSESSALQSQVDNLSCTES----QLQSQCQQMGQANRNLESKLLKEEELRKEEVQTLQAELSAAQTE 300
Cdd:COG3206 261 Q-----SPVIQQLRAQLAELEAELAELSARYTpnhpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQ 335
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 569006759 301 VKALSTQVEELKDELVTQRR--KHASNVKDLSKQLQQARRKLEQTENGN 347
Cdd:COG3206 336 LAQLEARLAELPELEAELRRleREVEVARELYESLLQRLEEARLAEALT 384
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
145-344 |
4.25e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.04 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 145 DERLRTEDELSKYREIINrqkseiqnllDKVKITDQLHEQLQSGKQEIEHLKEEMESlnsliNDLqkdiegsrkrESELL 224
Cdd:PRK10929 58 EERKGSLERAKQYQQVID----------NFPKLSAELRQQLNNERDEPRSVPPNMST-----DAL----------EQEIL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 225 LFTEKLTSKNAQLQSESSALQSQVDNLscteSQLQsqcQQMGQANRNLESKLLKEEELRKEEVQTLQAELSAAQTEVKAL 304
Cdd:PRK10929 113 QVSSQLLEKSRQAQQEQDRAREISDSL----SQLP---QQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQAESAAL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006759 305 STQVEEL----------------KDELVTQRRKHASN-VKDLSKQL-----QQARRKLEQTE 344
Cdd:PRK10929 186 KALVDELelaqlsannrqelarlRSELAKKRSQQLDAyLQALRNQLnsqrqREAERALESTE 247
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
5-223 |
4.35e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 5 ETTRLIREIEKLKEEMNSQVIKVKWAQNKLKAEMDSHKETKDKLKETTTKLTQAKEEAEQIRQNCQDMIKTYQESEE-IK 83
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyIK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 84 SNELDAKLRVTKGELEKQMQEKSDQLEMHHAKIKELEDLKRTFKEGMDELRTLRTKAKCLEdERLRTEDELSKYREIINR 163
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE-ERHELYEEAKAKKEELER 376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 164 QKSEIQNLldkvkITDQLHEQLQSGKQEIEHLKEEMESLNSLINDLQKDIEGSRKRESEL 223
Cdd:PRK03918 377 LKKRLTGL-----TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL 431
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
192-346 |
4.63e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 192 IEHLKEEMESLNSLINDLQKDIEGSRKREselllftekltsknAQLQSESSALQsQVDNLSCTESQLQSQCQQMGQANRN 271
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAEL--------------DALQERREALQ-RLAEYSWDEIDVASAEREIAELEAE 676
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569006759 272 LESKLLKEEElrkeeVQTLQAELSAAQTEVKALstqvEELKDELVTQRRKHASNVKDLSKQLQQARRKLEQTENG 346
Cdd:COG4913 677 LERLDASSDD-----LAALEEQLEELEAELEEL----EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
54-223 |
5.59e-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: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 54 KLTQAKEEAEQIRQNCQDMIKTYQESEEIKsNELDAKLRVTKGELEKQMQEksDQLEMHHAKIKELEDLKRTFKEGMDEL 133
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAEL-DALQERREALQRLAEYSWDE--IDVASAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 134 RTLRTKAKCLEDERLRTEDELSKYREIINRQKSEIQNLLDKVKITDQLHEQLQSGKQEI------EHLKEEM--ESLNSL 205
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElralleERFAAALgdAVEREL 767
|
170
....*....|....*...
gi 569006759 206 INDLQKDIEGSRKRESEL 223
Cdd:COG4913 768 RENLEERIDALRARLNRA 785
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
16-218 |
5.67e-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: 39.65 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 16 LKEEMNSQVIKVKWAQNKLKAEMDSHKETKDKLKETTTKLTQAKEEAEQIRQNCQDMIKTYQESEeiksneLDAKLRVTK 95
Cdd:TIGR01612 1470 LKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALA------IKNKFAKTK 1543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 96 GELEKQMQEKSD-------QLEMHHAKIKELEDLKRTFKEGMDE--------------LRTLRTKAKCLEDERLRTEDEL 154
Cdd:TIGR01612 1544 KDSEIIIKEIKDahkkfilEAEKSEQKIKEIKKEKFRIEDDAAKndksnkaaidiqlsLENFENKFLKISDIKKKINDCL 1623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006759 155 SKYREI--------INRQKSEIQNLLDKVKITDQLHEQLQSGKQEIEHLKEEMESLNSLINDLQKDIEGSRK 218
Cdd:TIGR01612 1624 KETESIekkissfsIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKK 1695
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
4-430 |
6.02e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 4 GETTRLIREIEKLKEEMNSQVIKVKwaqnKLKAEMDSHKETKDKLKETTTKLTQAKEEAEQIRQNCQDMIKTYQESEEIK 83
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELK----ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 84 S--NELDAKLRVTKGELEKqMQEKSDQLEMHHAKIKELEDLKRtfKEGMDELRTLRTKAKCLEDERLRTEDELSKYREII 161
Cdd:PRK03918 338 ErlEELKKKLKELEKRLEE-LEERHELYEEAKAKKEELERLKK--RLTGLTPEKLEKELEELEKAKEEIEEEISKITARI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 162 NRQKSEIQNLLDKVKITDQLHEQLQSGKQEI--EHLKEEMESLNSLINDLQKDIEGSRKRESELLLFTEKLTSKNAQlQS 239
Cdd:PRK03918 415 GELKKEIKELKKAIEELKKAKGKCPVCGRELteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK-ES 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 240 ESSALQSQVDNLSCTESQLQS-QCQQMGQANRNLE---------SKLLKEEELRKEEVQTLQAELSAAQTEVKALSTQVE 309
Cdd:PRK03918 494 ELIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEklkekliklKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELA 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 310 ELKDELVTQRRKHASNVKDLSKQLQQARRKLEQTENGNHDKDISSMGSRSSSSGSLNARISAEDRSPENTSSSVAVD--- 386
Cdd:PRK03918 574 ELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEele 653
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 569006759 387 -NFPEVDKAMLIERIVRLQKAHARKNEKIEFMEDHIKQLVEEIRK 430
Cdd:PRK03918 654 kKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
117-265 |
7.04e-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: 38.37 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 117 KELEDLKRTFKEGMDELRTLRTKAKCLEDERLRTEDELSKYREIINRQKSEIQNLLDKV-KITDQLHE-----QLQSGKQ 190
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIkKYEEQLGNvrnnkEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569006759 191 EIEHLKEEMESLNSLINDLQKDIEGSRKRESELllfTEKLTSKNAQLQSESSALQSQVDNLSCTESQLQSQCQQM 265
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELAEL---EAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
97-327 |
8.22e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.59 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 97 ELEKQMQEKSDQLEmhhAKIKELEDLKRTFKEGMDELRTLRTKAKCLEDERLRTEDELSKYREIINRQKSEIQnlldkvk 176
Cdd:COG4942 24 EAEAELEQLQQEIA---ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 177 itdQLHEQLQSGKQEIEHL------KEEMESLNSLINdlQKDIEGSRKRESELLLFTEKLTSKNAQLQSESSALQSQVDN 250
Cdd:COG4942 94 ---ELRAELEAQKEELAELlralyrLGRQPPLALLLS--PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006759 251 LSCTESQLQSQCQQMGQANRNLESkllkEEELRKEEVQTLQAELSAAQTEVKALSTQVEELKDELVTQRRKHASNVK 327
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEA----LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
115-341 |
8.55e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 38.76 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 115 KIKELEDLKRTFKEGMDELRTLRTKAKCLEDERLRTEDELSKyrEIINRQKSEIQNLLDKVK-ITDQLHEqLQSGKQEIE 193
Cdd:PRK05771 44 RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLE--ELIKDVEEELEKIEKEIKeLEEEISE-LENEIKELE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006759 194 HLKEEMESLNSLindlqkDIEGSRKRESELLLFTEKLTSKNAQLQSESSALQSQVDNLSCTES-------QLQSQCQQMG 266
Cdd:PRK05771 121 QEIERLEPWGNF------DLDLSLLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGyvyvvvvVLKELSDEVE 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569006759 267 QANRNLESKLLKEEELRkeevqTLQAELSAAQTEVKALSTQVEELKDELVTQRRKHASNVKDLSKQLQQARRKLE 341
Cdd:PRK05771 195 EELKKLGFERLELEEEG-----TPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAE 264
|
|
| |
