|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-351 |
4.77e-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: 61.23 E-value: 4.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 101 LRSKISELTTEVNKLQKGIEMYNQENSVYLS-YEKRAETLAVEIKELQGQLADYNMLVDKLNTNTEMEEVMNDYNMLKAQ 179
Cdd:TIGR02168 198 LERQLKSLERQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 180 NDRETqsldviFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMsfENQVKYLEmkTTNEKLLQELDTLQQQLDSQNMKKE 259
Cdd:TIGR02168 278 ELEEE------IEELQKELYALANEISRLEQQKQILRERLANL--ERQLEELE--AQLEELESKLDELAEELAELEEKLE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 260 SLEAEIAHSQVKQEAvlLHEKLYELESHRDqmiAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEE 339
Cdd:TIGR02168 348 ELKEELESLEAELEE--LEAELEELESRLE---ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422
|
250
....*....|..
gi 151101151 340 IRQLDMDLEEHQ 351
Cdd:TIGR02168 423 IEELLKKLEEAE 434
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
133-349 |
4.68e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 133 EKRAETLAVEIKELQGQLADYNMLVDKLNTntEMEEVMNDYNMLKAQNDRETQSLDVI---FTERQAKEKQIRSVEEEIE 209
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEA--ELEELEAELAELEAELEELRLELEELeleLEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 210 QEKQATDDIIKnmsfENQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQEAVLlhEKLYELESHRD 289
Cdd:COG1196 302 QDIARLEERRR----ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE--EALLEAEAELA 375
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 290 QMIAEDKSIgspMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEE 349
Cdd:COG1196 376 EAEEELEEL---AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
104-285 |
7.77e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 7.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 104 KISELTTEVNKLQKGIEMYNQENSVYLSYEKRAETLAVEIKELQGQLADYNMLVDKLNTNTEMEEVmndyNMLKAQNDRE 183
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL----EAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 184 TQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFENQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKESLEA 263
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180
....*....|....*....|..
gi 151101151 264 EIAHSQVKQEAVLLHEKLYELE 285
Cdd:COG4717 228 ELEQLENELEAAALEERLKEAR 249
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-326 |
7.97e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 7.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 101 LRSKISELTTEVNKLQKGIEMYNQE----NSVYLSYEKRAETLAVEIKELQGQLAdyNMLVDKLNTNTEMEEVMNDYNML 176
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYALANEisrlEQQKQILRERLANLERQLEELEAQLE--ELESKLDELAEELAELEEKLEEL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 177 KAQNDRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNM-SFENQVKYLEmkTTNEKLLQELDTLQQQLDSQN 255
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIaSLNNEIERLE--ARLERLEDRRERLQQEIEELL 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 151101151 256 MKKESLEAEIAHSQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQL 326
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
101-353 |
5.71e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 5.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 101 LRSKISELTTEVNKLQKGIEMYNQENSvylSYEKRAETLAVEIKELQGQLADYNMLVDKLNTN-TEMEEVMNDYNmlKAQ 179
Cdd:TIGR02169 707 LSQELSDASRKIGEIEKEIEQLEQEEE---KLKERLEELEEDLSSLEQEIENVKSELKELEARiEELEEDLHKLE--EAL 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 180 NDRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFENQvkYLEmkttnekllQELDTLQQQLDSQNMKKE 259
Cdd:TIGR02169 782 NDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YLE---------KEIQELQEQRIDLKEQIK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 260 SLEAEIAHSQVKQEavllhEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEE 339
Cdd:TIGR02169 851 SIEKEIENLNGKKE-----ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
250
....*....|....
gi 151101151 340 IRQLDMDLEEHQDP 353
Cdd:TIGR02169 926 LEALEEELSEIEDP 939
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-344 |
6.41e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 6.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 101 LRSKISELTTEVNKLQKGIEMYNQENSvylSYEKRAETLAVEIKELQGQLADYNMLVDKLNTNTEMEEVMNdynmlkAQN 180
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELE---ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI------AQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 181 DRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFENQvkylEMKTTNEKLLQELDTLQQQLDSQNMKKES 260
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK----ALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 261 LEAEIAhsQVKQEAVLLHEklyELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEI 340
Cdd:TIGR02168 829 LERRIA--ATERRLEDLEE---QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
....
gi 151101151 341 RQLD 344
Cdd:TIGR02168 904 RELE 907
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
143-345 |
2.18e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.63 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 143 IKELQGQLADYNMLVDKLNTNTEMEEvmNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEEIEQE--------KQA 214
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHIQQQIKTYN--KNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDEllnlvmdiEDP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 215 TDDIIK--------NMSFENQVKYLEMKTTN-----------------EKLLQELDTLQQQLDSQNMKKESLEaEIAHsQ 269
Cdd:PHA02562 254 SAALNKlntaaakiKSKIEQFQKVIKMYEKGgvcptctqqisegpdriTKIKDKLKELQHSLEKLDTAIDELE-EIMD-E 331
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 151101151 270 VKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDM 345
Cdd:PHA02562 332 FNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGI 407
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
100-341 |
4.77e-06 |
|
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: 48.48 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 100 LLRSKISELTTEVNKLQKGIEMYNQENSVylsyekraetLAVEIKELQGQLADYNMLVDKLNTNTEMEEvmNDYNMLKAQ 179
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEIERLKETIIK----------NNSEIKDLTNQDSVKELIIKNLDNTRESLE--TQLKVLSRS 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 180 NDRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMS-FENQVKYL--EMKTTNEKLLQ---ELDTLQQQLDS 253
Cdd:TIGR04523 477 INKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISsLKEKIEKLesEKKEKESKISDledELNKDDFELKK 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 254 QNMKKESLEAEIAHSQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKL-------LKQIKDDNQEIASMERQL 326
Cdd:TIGR04523 557 ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKisslekeLEKAKKENEKLSSIIKNI 636
|
250
....*....|....*
gi 151101151 327 TDTKEKINQFIEEIR 341
Cdd:TIGR04523 637 KSKKNKLKQEVKQIK 651
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
127-349 |
5.43e-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: 48.53 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 127 SVYLSYEKRAETLAVEIKELQGQLADynmLVDKLNtntemeEVMNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEE 206
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSS---LQSELR------RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 207 EIEQEKQATDDIiknmsfenQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQ-------------- 272
Cdd:TIGR02169 738 RLEELEEDLSSL--------EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEiqaelskleeevsr 809
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 151101151 273 -EAVLLHEKLYELESHRDQMIAEDKsIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEE 349
Cdd:TIGR02169 810 iEARLREIEQKLNRLTLEKEYLEKE-IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
134-342 |
2.43e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 134 KRAETLAVEIKELQGQLADYNMLVDKlnTNTEMEEVMNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEEI----- 208
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA--LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIaelra 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 209 --EQEKQATDDIIKNMSFENQVKYLEMKTTNEKLLQ---ELDTLQQQLDSQNMKKESLEAEIAhsQVKQEAVLLHEKLYE 283
Cdd:COG4942 98 elEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDavrRLQYLKYLAPARREQAEELRADLA--ELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 151101151 284 LESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQ 342
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
155-352 |
3.25e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 155 MLVDKLNTntEMEEVMNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMS-FENQVKYLEM 233
Cdd:COG4717 46 MLLERLEK--EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEeLREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 234 KTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQEAVLLHEKlyELESHRDQMIAEDKSIGSPMEER-EKLLKQI 312
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA--ELAELQEELEELLEQLSLATEEElQDLAEEL 201
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 151101151 313 KDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQD 352
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
195-342 |
5.95e-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: 43.76 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 195 QAKEKQIRSVEEEIEQEKQATDDIiknmsfENQVKYLEmkTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQEA 274
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAEL------EDELAALE--ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 151101151 275 V--------LLHEklyeLESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQ 342
Cdd:COG1579 85 VrnnkeyeaLQKE----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
171-349 |
6.85e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.89 E-value: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 171 NDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVE-EEIEQEKQATDdiiKNMSFENQVKYLEMKTTnEKLLQELDTLQQ 249
Cdd:PLN02939 95 DDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQlEDLVGMIQNAE---KNILLLNQARLQALEDL-EKILTEKEALQG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 250 QLDSQNMKKESLEAEIA-HSQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQ----IKDDNQEIASMER 324
Cdd:PLN02939 171 KINILEMRLSETDARIKlAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEenmlLKDDIQFLKAELI 250
|
170 180
....*....|....*....|....*
gi 151101151 325 QLTDTKEKINQFIEEIRQLDMDLEE 349
Cdd:PLN02939 251 EVAETEERVFKLEKERSLLDASLRE 275
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
104-349 |
7.36e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 104 KISELTTEVNKLQKGIEMYNQE--NSVYLSYEKRAETLAVEIKELQGQLADYNMLVDKLNTNTE---------------- 165
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEklEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEelkkakgkcpvcgrel 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 166 ----MEEVMNDYNmlkaqndRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFENQVKYLEMKTTN---- 237
Cdd:PRK03918 446 teehRKELLEEYT-------AELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKynle 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 238 --EKLLQELDTLQQQLDSQNMKKESLEAEIAHSQ-VKQEAVLLHEKLYELESHRDQMIAEDKSIG-SPMEEREKLLKQI- 312
Cdd:PRK03918 519 elEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEeLKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELe 598
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 151101151 313 ---------KDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEE 349
Cdd:PRK03918 599 pfyneylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEE 644
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
70-339 |
8.61e-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: 44.72 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 70 RPVTQQgLTGMKTGTKGPQRQILDKSYYLGLLRSKISELTTEVNKLQKGIEMYNQENSVYLSYEKRAETLAVEIKELQGQ 149
Cdd:pfam15921 478 RKVVEE-LTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 150 LADYNMLVDKLNTNTE-MEEVMNDYN-------MLKAQ-----NDR--ETQSLDVIFTERQAKEKQIRSVEEEIEQEKQA 214
Cdd:pfam15921 557 MAEKDKVIEILRQQIEnMTQLVGQHGrtagamqVEKAQlekeiNDRrlELQEFKILKDKKDAKIRELEARVSDLELEKVK 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 215 tddiIKNMSFENQVKYLEMKTTNEKLLQELDTLQQQLDS---------QNMKKESLEAEIAHSQVKQEavlLHEKLYELE 285
Cdd:pfam15921 637 ----LVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSlsedyevlkRNFRNKSEEMETTTNKLKMQ---LKSAQSELE 709
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 151101151 286 SHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLtdtkekinQFIEE 339
Cdd:pfam15921 710 QTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKI--------QFLEE 755
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
101-351 |
9.15e-05 |
|
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: 44.63 E-value: 9.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 101 LRSKISELTTEVNKLQKGIEMYNQENsvyLSYEKRAETLAVEIKELQGQLADYNMLVDKLNT-NTEMEEVMNDYNMLKAQ 179
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELENEL---NLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKkIQKNKSLESQISELKKQ 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 180 NDRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMS---------------FENQVKYLEMKTT---NEKLL 241
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSekqkeleqnnkkikeLEKQLNQLKSEISdlnNQKEQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 242 QELDTLQQQLDSQNMKKESLEAEIahSQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQ---- 317
Cdd:TIGR04523 307 DWNKELKSELKNQEKKLEEIQNQI--SQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQsykq 384
|
250 260 270
....*....|....*....|....*....|....
gi 151101151 318 EIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQ 351
Cdd:TIGR04523 385 EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ 418
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
101-349 |
9.99e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 101 LRSKISELTTEVNKLQKGIEMYNQENSVYLSYEKRAETLAVEIKELQGQLADYNMLVDKLNTN----TEMEEVMNDYNML 176
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelKELKEKAEEYIKL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 177 KAQNDRETQSLDVIFTERQAKEKQIRSVEEEIEQ--EKQATDDIIKNMSFENQVKYLEMKtTNEKLLQELDTLQQQLDSQ 254
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKEleEKEERLEELKKKLKELEKRLEELE-ERHELYEEAKAKKEELERL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 255 NMKKESLEAEiahsQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEK-- 332
Cdd:PRK03918 378 KKRLTGLTPE----KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKel 453
|
250
....*....|....*..
gi 151101151 333 INQFIEEIRQLDMDLEE 349
Cdd:PRK03918 454 LEEYTAELKRIEKELKE 470
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
192-352 |
2.10e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 192 TERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFENQV--------------KYLEMKTTNEKLLQELDTLQQQLDSQNMK 257
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLleelnkkikdlgeeEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 258 KESLEAEIAHSQVKQEAVL-----LHEKLYELESHRDQMIAEdksIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEK 332
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLaeieeLEREIEEERKRRDKLTEE---YAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
170 180
....*....|....*....|
gi 151101151 333 INQFIEEIRQLDMDLEEHQD 352
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQE 413
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
128-345 |
3.09e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 128 VYLSYEKRAETLAVEIKELQGQLADYNMLvdklnTNTEMEEVMNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEE 207
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEEL-----EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 208 I-----EQEKQATDDIIKNMSFENQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQEAVLLHEKLY 282
Cdd:COG4717 363 LqleelEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELE 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 151101151 283 ELESHRDQMIAEdksigspMEEREKLLKQIKDDNqEIASMERQLTDTKEKINQFIEEIRQLDM 345
Cdd:COG4717 443 ELEEELEELREE-------LAELEAELEQLEEDG-ELAELLQELEELKAELRELAEEWAALKL 497
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
194-352 |
3.19e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 194 RQAKEKQIRSVEEEIEQEKQATddiiknmsfenqvkylemkttnEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQvkqe 273
Cdd:COG4913 612 LAALEAELAELEEELAEAEERL----------------------EALEAELDALQERREALQRLAEYSWDEIDVAS---- 665
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 151101151 274 avlLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQD 352
Cdd:COG4913 666 ---AEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
194-352 |
3.63e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 194 RQAKEKQIRSVEEEIEQEKQATDDIIKNMSfENQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAhsQVKQE 273
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALA-ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE--QLEER 748
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 151101151 274 AVLLHEKLYELEshrdqmiaedksigspmEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQD 352
Cdd:TIGR02168 749 IAQLSKELTELE-----------------AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
193-352 |
4.63e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 193 ERQAKEKQIRSVEEEIEQEKQATDDIIKNM-SFENQVKYLEMKTtnEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVK 271
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEkALLKQLAALERRI--AALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 272 QEAV--LLHEKLYELESHR--------------DQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQ 335
Cdd:COG4942 99 LEAQkeELAELLRALYRLGrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170
....*....|....*..
gi 151101151 336 FIEEIRQLDMDLEEHQD 352
Cdd:COG4942 179 LLAELEEERAALEALKA 195
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
101-343 |
5.41e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 101 LRSKISELTTEVNKLQKGIEMYNQENSVY-LSYEKRAETLAVEIKELQGQLADYNMLVDKlntNTEMEEVMNDynmLKAQ 179
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESLETQLKVLsRSINKIKQNLEQKQKELKSKEKELKKLNEE---KKELEEKVKD---LTKK 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 180 NDRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQA-TDDIIKNMSFENQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKK 258
Cdd:TIGR04523 519 ISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEK 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 259 ESLEAEIAHSQVKQEAvlLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDdnqeiasmerQLTDTKEKINQFIE 338
Cdd:TIGR04523 599 KDLIKEIEEKEKKISS--LEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE----------TIKEIRNKWPEIIK 666
|
....*
gi 151101151 339 EIRQL 343
Cdd:TIGR04523 667 KIKES 671
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
73-343 |
6.39e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 73 TQQGLTGMKTGTKGPQRQILDKSYYLGLLRSKISELTTEVNKLQKGIEMYNQENSVYLSYEKRAETLAVE--IKELQGQL 150
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEkkLEEIQNQI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 151 ADYNMLVDKLNTN-----TEMEEVMNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIK-NMSF 224
Cdd:TIGR04523 331 SQNNKIISQLNEQisqlkKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKlNQQK 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 225 ENQVKYLEmkTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAhsqvkqEAVLLHEKLYELESHRDQMIAE-DKSIGSPME 303
Cdd:TIGR04523 411 DEQIKKLQ--QEKELLEKEIERLKETIIKNNSEIKDLTNQDS------VKELIIKNLDNTRESLETQLKVlSRSINKIKQ 482
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 151101151 304 EREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQL 343
Cdd:TIGR04523 483 NLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSL 522
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
101-343 |
6.67e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 101 LRSKISELTTEVNKLQKGIEMYNQENSvylSYEKRAETLAVEIKELQGQLADYNMLVDKLNTN-----TEMEEVMNDYNM 175
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLKKENQ---SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQikklqQEKELLEKEIER 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 176 LKAQNDRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKnmsfenqvKYLEMKTTNEKLLQELDTLQQQLDSQN 255
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR--------SINKIKQNLEQKQKELKSKEKELKKLN 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 256 MKKESLEAEIahSQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEE------REKLLKQIKDDNQEIASMERQLTDT 329
Cdd:TIGR04523 503 EEKKELEEKV--KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKddfelkKENLEKEIDEKNKEIEELKQTQKSL 580
|
250
....*....|....
gi 151101151 330 KEKINQFIEEIRQL 343
Cdd:TIGR04523 581 KKKQEEKQELIDQK 594
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
195-338 |
6.82e-04 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 40.68 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 195 QAKEKQIRSVEEEIEQEKQATDDIIKNMSFEnqvkYLEMKTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAH-SQVKQE 273
Cdd:pfam11932 19 LDLAEKAVAAAAQSQKKIDKWDDEKQELLAE----YRALKAELESLEVYNRQLERLVASQEQEIASLERQIEEiERTERE 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 151101151 274 AVLLhekLYELESHRDQMIAEDKsigsP--MEEREKLLKQIKDdnqeiaSMERQLTDTKEKINQFIE 338
Cdd:pfam11932 95 LVPL---MLKMLDRLEQFVALDL----PflLEERQARLARLRE------LMDDADVSLAEKYRRILE 148
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
107-350 |
7.51e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 107 ELTTEVNKLQKGIEMYNQENSVYLSYEKRAETLAVEIKELQGQLADYNMLVDKLNTNTEmEEVmndynmlkaqnDRETQS 186
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESV-EEL-----------EERLKE 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 187 LDVI---FTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFENqvKYLEMKttnEKLLQELDTLQQQLDSQNMKKESLEA 263
Cdd:PRK03918 597 LEPFyneYLELKDAEKELEREEKELKKLEEELDKAFEELAETE--KRLEEL---RKELEELEKKYSEEEYEELREEYLEL 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 264 EIAHSQVKqeavllhEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERqltdtkekinqFIEEIRQL 343
Cdd:PRK03918 672 SRELAGLR-------AELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE-----------LREKVKKY 733
|
....*..
gi 151101151 344 DMDLEEH 350
Cdd:PRK03918 734 KALLKER 740
|
|
| TTC8_N |
cd21341 |
N-terminal domain of tetratricopeptide repeat domain 8; Tetratricopeptide repeat domain 8 ... |
7-50 |
8.52e-04 |
|
N-terminal domain of tetratricopeptide repeat domain 8; Tetratricopeptide repeat domain 8 (TTC80), also known a BBS8, has been directly linked to Bardet-Biedl syndrome, an autosomal recessive ciliopathy characterized by retinal degeneration, renal failure, obesity, diabetes, male infertility, polydactyly and cognitive impairment. Mutations in BBS8 cause early vision loss. In addition to C-terminal tetratricopeptide repeats, TTC8 also contains an N-terminal domain of unknown function.
Pssm-ID: 411061 [Multi-domain] Cd Length: 139 Bit Score: 39.21 E-value: 8.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 151101151 7 SSAARPVSRggvglTGRPPSGI--------RPLSGNIRVATAMPPGTARPGS 50
Cdd:cd21341 66 SQAMRPTTS-----SGRPITGFvrpgtqsgRPGTSRQALRTPRRAGTARPVT 112
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
204-352 |
8.98e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 8.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 204 VEEEIEQ-----EKQAtddiiknmsfENQVKYLEMKTT-----NEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQE 273
Cdd:COG1196 194 ILGELERqleplERQA----------EKAERYRELKEElkeleAELLLLKLRELEAELEELEAELEELEAELEELEAELA 263
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 151101151 274 AVllhEKlyELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQD 352
Cdd:COG1196 264 EL---EA--ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
101-274 |
9.05e-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: 40.90 E-value: 9.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 101 LRSKISELTTEVNKLQKGIEMYNQENSvylSYEKRAETLAVEIKELQGQLADYNMLVDKLNTNTEMEEVMNDYNMLKAQN 180
Cdd:COG4942 60 LERRIAALARRIRALEQELAALEAELA---ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 181 DRE-----TQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSfENQVKYLEMKTTNEKLLQELDT----LQQQL 251
Cdd:COG4942 137 RLQylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELE-EERAALEALKAERQKLLARLEKelaeLAAEL 215
|
170 180
....*....|....*....|...
gi 151101151 252 DSQNMKKESLEAEIAHSQVKQEA 274
Cdd:COG4942 216 AELQQEAEELEALIARLEAEAAA 238
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
135-323 |
1.20e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.88 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 135 RAETLAVEIKELQgQLADYNMLVDKLNTNTEME-EVMNDYNMLKAQNDRETQSLDVIFT-----ERQAKEKQIRSVEEEI 208
Cdd:pfam17380 366 RQEEIAMEISRMR-ELERLQMERQQKNERVRQElEAARKVKILEEERQRKIQQQKVEMEqiraeQEEARQREVRRLEEER 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 209 ----------EQEKQATDDIIKNMSFENQVKYLEMKTTNEK-----------LLQELDTLQQQLDSQNMKKESLEAE--- 264
Cdd:pfam17380 445 aremervrleEQERQQQVERLRQQEEERKRKKLELEKEKRDrkraeeqrrkiLEKELEERKQAMIEEERKRKLLEKEmee 524
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 151101151 265 ----IAHSQVKQEAVLLHEKLYELESHR---DQM--IAEDKSIGSPMEEREKLLKQIKDDNQEIASME 323
Cdd:pfam17380 525 rqkaIYEEERRREAEEERRKQQEMEERRriqEQMrkATEERSRLEAMEREREMMRQIVESEKARAEYE 592
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
93-264 |
1.33e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 93 DKSYYLGLLRSKISELTTEVNKLQKGIEMYNQENSvylSYEKRAETLAVEIKELQGQLADY-----NMLVDKLNTNTEME 167
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE---NLNGKKEELEEELEELEAALRDLesrlgDLKKERDELEAQLR 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 168 EVMNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFENQVKYLE-----MKTTNEKLLQ 242
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEeeiraLEPVNMLAIQ 979
|
170 180
....*....|....*....|..
gi 151101151 243 ELDTLQQQLDSQNMKKESLEAE 264
Cdd:TIGR02169 980 EYEEVLKRLDELKEKRAKLEEE 1001
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
114-356 |
1.35e-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: 40.81 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 114 KLQKGIEMYNQENSVYLSYEKRAE-TLAVEIKELQGQLADYNMLVDKLNTNtemeEVMNDYNMLKAqnDRETQSLDVIFT 192
Cdd:TIGR01612 946 ILNKNIDTIKESNLIEKSYKDKFDnTLIDKINELDKAFKDASLNDYEAKNN----ELIKYFNDLKA--NLGKNKENMLYH 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 193 ERQAKEKQIRSVEEEIEqekqatdDIIKNMSFENQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKesLEAEIAHSQVKQ 272
Cdd:TIGR01612 1020 QFDEKEKATNDIEQKIE-------DANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLNKEILEE--AEINITNFNEIK 1090
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 273 EAVllheKLYELEShrdqmIAEDKSIgSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQD 352
Cdd:TIGR01612 1091 EKL----KHYNFDD-----FGKEENI-KYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVAD 1160
|
....
gi 151101151 353 PTNY 356
Cdd:TIGR01612 1161 KAIS 1164
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
90-349 |
1.43e-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: 40.77 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 90 QILDKSYYLGLLRSKISELTTEVNKLQKGIEMYNQENSVYLSYEKRAETLAVEIKELQGQLADYNMLVdkLNTNTEMEEV 169
Cdd:TIGR04523 181 EKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEI--SNTQTQLNQL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 170 MNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEEIEQ-EKQATDDIIKNM-----SFENQVKYLEMKTTNEKllQE 243
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDlNNQKEQDWNKELkselkNQEKKLEEIQNQISQNN--KI 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 244 LDTLQQQLdsQNMKKESLEAEIAHSQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASME 323
Cdd:TIGR04523 337 ISQLNEQI--SQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
250 260
....*....|....*....|....*.
gi 151101151 324 RQLTDTKEKINQFIEEIRQLDMDLEE 349
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNS 440
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
106-349 |
1.66e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 106 SELTTEVNKLQKGIEmynQENSVYLSYEKRAETLAVEIKELQGQLADYNMLVD-----KLNTNTEMEEVMNDYNMLKAQN 180
Cdd:pfam01576 429 AELAEKLSKLQSELE---SVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQeetrqKLNLSTRLRQLEDERNSLQEQL 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 181 DRETQSldvifteRQAKEKQIRSVEEEIEQEKQATDDIIKNMS------------FENQVKYLEMKT--------TNEKL 240
Cdd:pfam01576 506 EEEEEA-------KRNVERQLSTLQAQLSDMKKKLEEDAGTLEaleegkkrlqreLEALTQQLEEKAaaydklekTKNRL 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 241 LQELDTLQQQLDSQNMKKESLEAeiahsqvKQEAVllheklyeleshrDQMIAEDKSIGSPM-EEREKLLKQIKDDNQEI 319
Cdd:pfam01576 579 QQELDDLLVDLDHQRQLVSNLEK-------KQKKF-------------DQMLAEEKAISARYaEERDRAEAEAREKETRA 638
|
250 260 270
....*....|....*....|....*....|
gi 151101151 320 ASMERQLTDTKEKINQFIEEIRQLDMDLEE 349
Cdd:pfam01576 639 LSLARALEEALEAKEELERTNKQLRAEMED 668
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
197-340 |
1.79e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 197 KEKQIRSVEEEIEQEKQATDDIIKNMsfENQVKYLEmkttnEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQEAvl 276
Cdd:PRK12704 55 KKEALLEAKEEIHKLRNEFEKELRER--RNELQKLE-----KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQE-- 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 151101151 277 LHEKLYELESHRDQMIAEDKSIG--SPMEEREKLLKQIKDD-NQEIASMERQL-TDTKEKINQFIEEI 340
Cdd:PRK12704 126 LEKKEEELEELIEEQLQELERISglTAEEAKEILLEKVEEEaRHEAAVLIKEIeEEAKEEADKKAKEI 193
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
72-348 |
1.98e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 72 VTQQGLTGMKTGTKGPQRQILDKSYYLGLLRSKISELTTEVNKLQKGIEMYNQENSVYLSYEKRAETLAVEIKELQGQLA 151
Cdd:PRK01156 135 VGQGEMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 152 DynMLVDKLNTNTEMEEVMNDYNMLKAQNDRETQSLDVI------FTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFE 225
Cdd:PRK01156 215 I--TLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKnryeseIKTAESDLSMELEKNNYYKELEERHMKIINDPVYK 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 226 NQ---VKYLEMKTTNEKLLQELDTLQQQLDS--QNMKK-ESLEAEIAHSQVKQ-EAVLLHEKLYELESHRDQMIAEDKSI 298
Cdd:PRK01156 293 NRnyiNDYFKYKNDIENKKQILSNIDAEINKyhAIIKKlSVLQKDYNDYIKKKsRYDDLNNQILELEGYEMDYNSYLKSI 372
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 151101151 299 GSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLE 348
Cdd:PRK01156 373 ESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDIS 422
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
101-274 |
2.18e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 101 LRSKISELTTEVNKLQKGIEMYNQE----NSVYLSYEKRAETLAVEIKELQGQLADYNMLVDKLNTntEMEEVMNDYnml 176
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAEleelNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE--ELGERARAL--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 177 kAQNDRETQSLDVIF------------------TERQAKE-KQIRSVEEEIEQEKQATDDIIKnmsfenqvkylEMKTTN 237
Cdd:COG3883 96 -YRSGGSVSYLDVLLgsesfsdfldrlsalskiADADADLlEELKADKAELEAKKAELEAKLA-----------ELEALK 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 151101151 238 EKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQEA 274
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAE 200
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
69-342 |
2.43e-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: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 69 HRPVTQQGLTGMK--TGTKGPQRQIlDKSYYLG--------LLRSKISELTTEVNKLQKGIEMYNQEnsvYLSYEKRAET 138
Cdd:COG4913 574 PRAITRAGQVKGNgtRHEKDDRRRI-RSRYVLGfdnraklaALEAELAELEEELAEAEERLEALEAE---LDALQERREA 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 139 LA---------VEIKELQGQLADYNMLVDKL-NTNTEMEEVMNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEEI 208
Cdd:COG4913 650 LQrlaeyswdeIDVASAEREIAELEAELERLdASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 209 EQEKQATDDIIKNMSFEnqvkylemkttnekLLQELDTLQQQLDSQNmkKESLEAEIAHSQVKQEAVLLHEKLYELESHR 288
Cdd:COG4913 730 DELQDRLEAAEDLARLE--------------LRALLEERFAAALGDA--VERELRENLEERIDALRARLNRAEEELERAM 793
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 151101151 289 DQMIAEDKSIGSPM-------EEREKLLKQIKDDN-----QEIA-----SMERQLTDTKEKINQFIEEIRQ 342
Cdd:COG4913 794 RAFNREWPAETADLdadleslPEYLALLDRLEEDGlpeyeERFKellneNSIEFVADLLSKLRRAIREIKE 864
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
239-352 |
4.11e-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: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 239 KLLQELDTLQQQLDSQNMKKESLEAEIAhsQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDD--- 315
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELA--ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkey 91
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 151101151 316 ---NQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQD 352
Cdd:COG1579 92 ealQKEIESLKRRISDLEDEILELMERIEELEEELAELEA 131
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
242-335 |
5.09e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 38.91 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 242 QELDTLQQQLDSQNMKKESLEAEiAHSQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIAS 321
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKE-QDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPE 489
|
90
....*....|....
gi 151101151 322 MERQLTDTKEKINQ 335
Cdd:COG0542 490 LEKELAELEEELAE 503
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
101-300 |
5.35e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 38.84 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 101 LRSKISELTTEVNKLQKGIEMYNQENSVyLSYEKRAETLAVEIKELQGQLAD-----------YNMLVDKLNTN-TEMEE 168
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGL-VDLSEEAKLLLQQLSELESQLAEaraelaeaearLAALRAQLGSGpDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 169 VMND--YNMLKAQ-NDRETQ--SLDVIFTERQAkekQIRSVEEEIEQEKQATDDIIKNMSFENQVKYLEMKTTNEKLLQE 243
Cdd:COG3206 259 LLQSpvIQQLRAQlAELEAElaELSARYTPNHP---DVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQ 335
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 151101151 244 LDTLQQQLDSQNmkkeslEAEIAHSQVKQEAVLLhEKLYE--LESHRDQMIAEDKSIGS 300
Cdd:COG3206 336 LAQLEARLAELP------ELEAELRRLEREVEVA-RELYEslLQRLEEARLAEALTVGN 387
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
164-351 |
5.46e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 38.80 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 164 TEMEEVMNDYNMLKaqndRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFENQVKYLEMKTTNEKLLQE 243
Cdd:pfam02463 156 LEIEEEAAGSRLKR----KKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151101151 244 LDTLQQQLDSQNMKKESLEAEIAHSQVKQEAVLlheklyELESHRDQMIAEDKSIGSPMEEREKLL-KQIKDDNQEIASM 322
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEE------EKLAQVLKENKEEEKEKKLQEEELKLLaKEEEELKSELLKL 305
|
170 180
....*....|....*....|....*....
gi 151101151 323 ERQLTDTKEKINQFIEEIRQLDMDLEEHQ 351
Cdd:pfam02463 306 ERRKVDDEEKLKESEKEKKKAEKELKKEK 334
|
|
|