|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-416 |
3.25e-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: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 101 LRSKISELTTEVNKLQKEIEMYNQENSVYLS-YEKRAETLAVEIKEFQGQLADYNMLVDKLNTNTEMEEVMNDYNMLKAQ 179
Cdd:TIGR02168 198 LERQLKSLERQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 180 NDRETqsmdviFTERQAKEKQMRSVEEEIEQEKQAADDIIKNmsLENQVKYLEmkATNEKLLQELDTLQQQLDSQNMKKE 259
Cdd:TIGR02168 278 ELEEE------IEELQKELYALANEISRLEQQKQILRERLAN--LERQLEELE--AQLEELESKLDELAEELAELEEKLE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 260 SMEAEIAHSQVKQEAvlLHEKLYELESHRDqmiAEDKSIGSPMEEREKLLKQVKDDNQEIASMERQLTDIKEKINQFNEE 339
Cdd:TIGR02168 348 ELKEELESLEAELEE--LEAELEELESRLE---ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622872397 340 IRQLDMDLEEHQ-GEMNQKYKELKKREENMDTFIETFEETKNQELERKAQIEANIVSLLEHCSRNINRMKQISSITNQ 416
Cdd:TIGR02168 423 IEELLKKLEEAElKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-409 |
3.96e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 101 LRSKISELTTEVNKLQKEIEMYNQENSvylSYEKRAETLAVEIKEFQGQLADYNMLVDKLNTNTEMEEVMNdynmlkAQN 180
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELE---ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI------AQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 181 DRETQSMDVIFTERQAKEKQMRSVEEEIEQEKQAADDIIKNMSLENQVKYLEMKATNEkllqELDTLQQQLDSQNMKKES 260
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA----ELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 261 MEAEIAhsQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEE----REKLLKQVKDDNQEIASMERQLTDIKEKINQF 336
Cdd:TIGR02168 829 LERRIA--ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEleseLEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622872397 337 NEEIRQLDMDLEEHQGEMNQKYKELKKREENMDTFIETFEETKNQELERKAQIEANIVSLLEHCSRNINRMKQ 409
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-343 |
1.35e-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: 58.14 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 101 LRSKISELTTEVNKLQKEIEMYNQE----NSVYLSYEKRAETLAVEIKEFQGQLAdyNMLVDKLNTNTEMEEVMNDYNML 176
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYALANEisrlEQQKQILRERLANLERQLEELEAQLE--ELESKLDELAEELAELEEKLEEL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 177 KAQNDRETQSMDVIFTERQAKEKQMRSVEEEIEQEKQAADDIIKNM-SLENQVKYLEmkATNEKLLQELDTLQQQLDSQN 255
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIaSLNNEIERLE--ARLERLEDRRERLQQEIEELL 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 256 MKKESMEAEIAHSQVKQEAVLLHEKLYELESHRDQMIAEDKSIgspmEEREKLLKQVKDDNQEIASMERQLTDIKEKINQ 335
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL----EEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
....*...
gi 1622872397 336 FNEEIRQL 343
Cdd:TIGR02168 504 FSEGVKAL 511
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
133-398 |
1.51e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 133 EKRAETLAVEIKEFQGQLADYNMLVDKLNTntEMEEVMNDYNMLKAQNDRETQSMDVIFTERQAKEKQMRSVEEEIEQEk 212
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEA--ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 213 QAADDIIKNMSLENQVKYLEMKATNEKLLQELDTLQQQLDSQNMKKESMEAEIAHSQVKQEAVLlhEKLYELESHRDQMI 292
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE--EALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 293 AEDKSIgspMEEREKLLKQVKDDNQEIASMERQLTDIKEKINQFNEEIRQLDMDLEEHQGEM---NQKYKELKKREENMD 369
Cdd:COG1196 379 EELEEL---AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEeeeEEALEEAAEEEAELE 455
|
250 260
....*....|....*....|....*....
gi 1622872397 370 TFIETFEETKNQELERKAQIEANIVSLLE 398
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLE 484
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
194-545 |
1.61e-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: 57.76 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 194 RQAKEKQMRSVEEEIEQEKQAADDIIKNM-SLENQV----KYLEMKATNEKL-----LQELDTLQQQLDSQNMKKESMEa 263
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLkSLERQAekaeRYKELKAELRELelallVLRLEELREELEELQEELKEAE- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 264 eiahSQVKQEAVLLHEKLYELESHRDQMIAEDKSIgspmEEREKLLKQVkddNQEIASMERQLTDIKEKINQFNEEIRQL 343
Cdd:TIGR02168 253 ----EELEELTAELQELEEKLEELRLEVSELEEEI----EELQKELYAL---ANEISRLEQQKQILRERLANLERQLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 344 DMDLEEHQGEMNQKYKELKKREENMDTFIETFEETKNqELERKAQIEANIVSLLEHCSRNINRMKQISSITNQELKMMQD 423
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEA-ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 424 DLNFKSTEVQKSQSTARNLTSD--SQRLQLDLQKMELLESKMTEEQHSLKSKIKQMTTDLETYNDLPALKSSGEEKKKKL 501
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEieELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1622872397 502 HQERMILSTRRNAFKKIMEKLNIEHEALKTQLQENETHSQLTNL 545
Cdd:TIGR02168 481 ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV 524
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
194-458 |
3.15e-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: 56.99 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 194 RQAKEKQMRSVEEEIEQEKQAADDIIKNMSlENQVKYLEMKATNEKLLQELDTLQQQLDSQNMKKESMEAEI--AHSQVK 271
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALA-ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVeqLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 272 QEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQVKDDNQEIASMERQLTDIKEKINQFNEEIRQLDMDLEEHQ 351
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 352 GEMNQKYKELKKREENMDTFIETFEETkNQELERKAQIEANIVSLLEHCSRNINRMKQISSITNQELKMMQDDLNFKSTE 431
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESL-AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
250 260
....*....|....*....|....*..
gi 1622872397 432 VQKSQSTARNLTSDSQRLQLDLQKMEL 458
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEV 936
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
198-537 |
8.76e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 198 EKQMRSVEEEIEQekqaADDII----KNM-SLENQV----KYLEMKAT-----NEKLLQELDTLQQQLDSQNMKKESMEA 263
Cdd:COG1196 178 ERKLEATEENLER----LEDILgeleRQLePLERQAekaeRYRELKEElkeleAELLLLKLRELEAELEELEAELEELEA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 264 EIAHSQVKQEAVllhEKlyELESHRDQMIAEDksigspmEEREKLLKQVKDDNQEIASMERQLTDIKEKINQFNEEIRQL 343
Cdd:COG1196 254 ELEELEAELAEL---EA--ELEELRLELEELE-------LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 344 DMDLEEHQgemnqkyKELKKREENMDTFIETFEETKNQELERKAQIEANIVSLLEHCSRNINRMKQISSITNQELKMMQD 423
Cdd:COG1196 322 EEELAELE-------EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 424 DLNFKSTEVQKSQSTARNLTSDSQRLQLDLQKMELLESKMTEEQHSLKSKIKQMTTDLETYNDLPALKSSGEEKKKKLHQ 503
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
330 340 350
....*....|....*....|....*....|....
gi 1622872397 504 ERMILSTRRNAFKKIMEKLNIEHEALKTQLQENE 537
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
165-391 |
9.99e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 9.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 165 EMEEVMNDYNMLKAQNDRETQSMDVIFTERQAKEKQMRSVE---EEIEQEKQAADDIIKNmsLENQVKYLEMKATNEK-- 239
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEkeiEQLEQEEEKLKERLEE--LEEDLSSLEQEIENVKse 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 240 ---LLQELDTLQQQLDSQNMKKESMEAEIAHSQVKQ---------------EAVLLHEKLYELESHRDQMIAEDKsIGSP 301
Cdd:TIGR02169 760 lkeLEARIEELEEDLHKLEEALNDLEARLSHSRIPEiqaelskleeevsriEARLREIEQKLNRLTLEKEYLEKE-IQEL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 302 MEEREKLLKQVKDDNQEIASMERQLTDIKEKINQFNEEIRQLDMDLEEHQGEMNQKYKELKKREENMDTFIETFEETKNQ 381
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
250
....*....|
gi 1622872397 382 ELERKAQIEA 391
Cdd:TIGR02169 919 LSELKAKLEA 928
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
88-381 |
1.34e-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: 54.68 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 88 QRQILDKSYYLGLLRSKISELTTEVNKLQKEIEMYNQENSVYLSYEKRAETLAVEIKEFQGQL-ADYNMLVDKLNTNTEM 166
Cdd:TIGR02168 725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeAQIEQLKEELKALREA 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 167 -EEVMNDYNMLKAQNDRETQSMDVIFTERQAKEKQMRSVEEEIEQEKQAADDIIKNMSlENQVKYLEMKATNEKLLQELD 245
Cdd:TIGR02168 805 lDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE-ELEELIEELESELEALLNERA 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 246 TLQQQLDSQNMKKESMEAEI------------AHSQVKQEAVLLHEKLYELESHRDQ---MIAEDKSIgsPMEEREKLLK 310
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELreleskrselrrELEELREKLAQLELRLEGLEVRIDNlqeRLSEEYSL--TLEEAEALEN 961
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622872397 311 QVKDDNQEIasmERQLTDIKEKINQFneeirqldmdleehqGEMN----QKYKELKKREENMDTFIETFEETKNQ 381
Cdd:TIGR02168 962 KIEDDEEEA---RRRLKRLENKIKEL---------------GPVNlaaiEEYEELKERYDFLTAQKEDLTEAKET 1018
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
100-483 |
1.93e-07 |
|
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: 54.26 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 100 LLRSKISELTTEVNKLQKEIEMYNQE----NSVYLSYEKRAETLAVEIKEFQGQLADYNMLVDklNTNTEMEEVMNDYNM 175
Cdd:TIGR04523 215 SLESQISELKKQNNQLKDNIEKKQQEinekTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELE--QNNKKIKELEKQLNQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 176 LKAQ-----NDRETQSMDVIFTERQAKEKQMRSVEEEIEQEKQAADDI----------IKNMSLENQVKYLEMKATNEKL 240
Cdd:TIGR04523 293 LKSEisdlnNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLneqisqlkkeLTNSESENSEKQRELEEKQNEI 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 241 LQELDTLQQQLDS-QNMKKESMEAEIAHSQVKQEAVLLHEKLYELESHRDQMiaeDKSIGSPMEEREKLLKQVKDDNQEI 319
Cdd:TIGR04523 373 EKLKKENQSYKQEiKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL---EKEIERLKETIIKNNSEIKDLTNQD 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 320 ASMERQLTDIKEKINQFNEEIRQLDMDLEEHQGEMNQKYKELKKREENMDTFIETFEETKNQELERKAQIEANIVSLLEH 399
Cdd:TIGR04523 450 SVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 400 CSRNINRMKQISSItNQELKMMQDDLNF---------KSTEVQKSQSTARNLTSDSQRLQLDLQKMELLESKMTEEQHSL 470
Cdd:TIGR04523 530 ESEKKEKESKISDL-EDELNKDDFELKKenlekeideKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEK 608
|
410
....*....|...
gi 1622872397 471 KSKIKQMTTDLET 483
Cdd:TIGR04523 609 EKKISSLEKELEK 621
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
102-482 |
7.37e-07 |
|
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: 52.33 E-value: 7.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 102 RSKISELTTEVNKLQKEIEmynqensvylSYEKRAETLAVEIKEFQGQLADYNmlVDKLNTNTEMEEVMNDYNMLKAQND 181
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKK----------ENKKNIDKFLTEIKKKEKELEKLN--NKYNDLKKQKEELENELNLLEKEKL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 182 RETQSMDVIFTERQAKEKQMRSVEEEIEqekqaaddiiKNMSLENQVkyLEMKATNEKLLQELDTLQQQLDSQNMKKESM 261
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELLLSNLKKKIQ----------KNKSLESQI--SELKKQNNQLKDNIEKKQQEINEKTTEISNT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 262 EAEIAHSQVKQEAVL--LHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQ-----VKDDNQEIASMERQLTDIK---- 330
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKkqLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIQnqis 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 331 ---EKINQFNEEIRQLDMDLEEHQGEMNQKYKELKKREENmdtfIETFEETKNQELERKAQIEANIVSLlehcSRNINRM 407
Cdd:TIGR04523 332 qnnKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE----IEKLKKENQSYKQEIKNLESQINDL----ESKIQNQ 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 408 KQISSITNQELKMMQDDLNFKSTEVQ-------KSQSTARNLTSDSQRLQLDLQKMELLESKMTEEQHSLKSKIKQMTTD 480
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIErlketiiKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483
|
..
gi 1622872397 481 LE 482
Cdd:TIGR04523 484 LE 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
303-563 |
8.52e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 8.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 303 EEREKLLKQVKDDNQEIASMERQLTDIKEKINQFNEEIRQLDMDLEEHQGEMNQKYKELKKREENMDTFIETFEETKNQE 382
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 383 LERKAQIEANiVSLLEHCSRNINRMKQISSITNQELKMMQDDLNFKSTEVQKSQSTARNLTSDSQRLQLDLQKMELLESK 462
Cdd:TIGR02168 319 EELEAQLEEL-ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 463 MTEEQHSLKSKIKQMTTDLE-------------TYNDLPALKSSGEEKKKKLHQERMILSTRRNAFKKIMEKLN-IEHEA 528
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRErlqqeieellkklEEAELKELQAELEELEEELEELQEELERLEEALEELREELEeAEQAL 477
|
250 260 270
....*....|....*....|....*....|....*
gi 1622872397 529 LKTQLQENETHSQLTNLERKWQHHEQNNFVMKELL 563
Cdd:TIGR02168 478 DAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
239-393 |
1.58e-06 |
|
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: 49.54 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 239 KLLQELDTLQQQLDSQNMKKESMEAEIAhsQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQVKDD--- 315
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELA--ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkey 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 316 ---NQEIASMERQLTDIKEKINQFNEEIRQLDMDLEEHQGEMNQKYKELKKREENMDTFIETFEETKNQELERKAQIEAN 392
Cdd:COG1579 92 ealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
.
gi 1622872397 393 I 393
Cdd:COG1579 172 I 172
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
104-285 |
2.15e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 104 KISELTTEVNKLQKEIEMYNQENSVYLSYEKRAETLAVEIKEFQGQLADYNMLVDKLNTNTEMEEVMNDYNMLKAQNDRE 183
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 184 TQSMDviftERQAKEKQMRSVEEEIEQEKQAADDIIKNMSLENQVKYLEMKATNEKLLQELDTLQQQLDSQNMKKESMEA 263
Cdd:COG4717 152 EERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180
....*....|....*....|..
gi 1622872397 264 EIAHSQVKQEAVLLHEKLYELE 285
Cdd:COG4717 228 ELEQLENELEAAALEERLKEAR 249
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
98-437 |
2.94e-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: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 98 LGLLRSKISELTTEVNKLQKEIEmynqensvylsYEKRAETLAVEIKEFQGqladYNMLVDKLNTNTEMEEVmndynmlK 177
Cdd:TIGR02169 186 IERLDLIIDEKRQQLERLRRERE-----------KAERYQALLKEKREYEG----YELLKEKEALERQKEAI-------E 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 178 AQNDRETQSMDVIFTERQAKEKQMRSVEEEIEQEKQAADDIIKNMSLENQVKYLEMKATNEKLLQELDTLQQQLdsQNMK 257
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKEREL--EDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 258 KESMEAEIAHSQVKQEAVLLHEKLYELESHRDQMIAEdksIGSPMEEREKLLKQVKDDNQEIASMERQLTDIKEKINQFN 337
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE---YAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 338 EEIrqldmdlEEHQGEMNQKYKELKKREE---NMDTFIETFEETKNQELERKAQIEANIvsllEHCSRNINRMKQISSIT 414
Cdd:TIGR02169 399 REI-------NELKRELDRLQEELQRLSEelaDLNAAIAGIEAKINELEEEKEDKALEI----KKQEWKLEQLAADLSKY 467
|
330 340
....*....|....*....|...
gi 1622872397 415 NQELKMMQDDLNFKSTEVQKSQS 437
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQR 490
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
296-490 |
4.24e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 296 KSIGSPMEEREKLLKQVKDDNQEIASMERQLTDIKEKINQFNEEIRQLD----------MDLEEHQGEMNQKYKELKKRE 365
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELReeleklekevKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 366 ENMDTFIETFEETKNQELERKAQIEAnivslLEHCSRNINRMKQiSSITNQELKMMQDDLNFKSTEVQKSQSTARNLTSD 445
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEE-----LEEKVKELKELKE-KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING 325
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622872397 446 SQRLQLDLQKMELLESKMTEEQHSLKSKIKQMTTDLETYNDLPAL 490
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAK 370
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
114-485 |
4.89e-06 |
|
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: 50.05 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 114 KLQKEIEMYNQENSVYLSYEKRAE-TLAVEIKEFQGQLADYNmLVDKLNTNTEMEEVMNDY---------NMLKAQNDRE 183
Cdd:TIGR01612 946 ILNKNIDTIKESNLIEKSYKDKFDnTLIDKINELDKAFKDAS-LNDYEAKNNELIKYFNDLkanlgknkeNMLYHQFDEK 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 184 TQSMDVIFTERQAKEKQMRSVE-----------EEIEQE-------------KQAADDI---------IKNMSLENQVKY 230
Cdd:TIGR01612 1025 EKATNDIEQKIEDANKNIPNIEiaihtsiyniiDEIEKEigkniellnkeilEEAEINItnfneikekLKHYNFDDFGKE 1104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 231 LEMKATNE--KLLQELDTLQQQLDS-----QNMKKES------MEAEIAHSQVKQEAVLLHEKLYELESHRDQMIAEDKS 297
Cdd:TIGR01612 1105 ENIKYADEinKIKDDIKNLDQKIDHhikalEEIKKKSenyideIKAQINDLEDVADKAISNDDPEEIEKKIENIVTKIDK 1184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 298 IGSPMEEREKLLkqvkddnQEIASMERQLTDIkekinqfnEEIRQLDMDLEEHQGEMN-QKYKELKKREEN----MDTFI 372
Cdd:TIGR01612 1185 KKNIYDEIKKLL-------NEIAEIEKDKTSL--------EEVKGINLSYGKNLGKLFlEKIDEEKKKSEHmikaMEAYI 1249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 373 ETFEETK--NQELERKAQIEANIVSLLE-----------HCSRNINRMKQISSITNQELKMMQDdlNFKSTEVQKSQSTA 439
Cdd:TIGR01612 1250 EDLDEIKekSPEIENEMGIEMDIKAEMEtfnishdddkdHHIISKKHDENISDIREKSLKIIED--FSEESDINDIKKEL 1327
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1622872397 440 RNLTSDSQRLQLDLQkmeLLESKMTEEQHSLK--------SKIKQMTTDLETYN 485
Cdd:TIGR01612 1328 QKNLLDAQKHNSDIN---LYLNEIANIYNILKlnkikkiiDEVKEYTKEIEENN 1378
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
262-391 |
5.78e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.01 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 262 EAEIAHSQVKQEAvllhEKlyELESHRDQMIAEDKsigspmEE----REKLLKQVKDDNQEIASMERQLTDIKEKINQFN 337
Cdd:PRK12704 35 EAEEEAKRILEEA----KK--EAEAIKKEALLEAK------EEihklRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622872397 338 EEIRQLDMDLEEHQGEMNQKYKELKKREENMDTFIE------------TFEETKNQ---ELERKAQIEA 391
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEeqlqelerisglTAEEAKEIlleKVEEEARHEA 171
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
98-353 |
6.77e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 98 LGLLRSKISELTTEVNKLQKEIEMYNQEnsvYLSYEKRAETLAVEIKEFQGQLADYnmLVDKLNTNTEMEEVMNDYNMLK 177
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAE---EYELLAELARLEQDIARLEERRREL--EERLEELEEELAELEEELEELE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 178 AQNDRETQSMDVIFTERQAKEKQMRSVEEEIEQEKQAADDIIKNMSLENQVKYLEMKATNEKLLQELDTLQQQLDSQNMK 257
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 258 KESMEAEIAHSQVKQEAVLLHEKLYELESHRDQMIAEDKsigspmEEREKLLKQVKDDNQEIASMERQLTDIKEKINQFN 337
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE------EEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
250
....*....|....*.
gi 1622872397 338 EEIRQLDMDLEEHQGE 353
Cdd:COG1196 491 ARLLLLLEAEADYEGF 506
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
283-482 |
1.00e-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: 47.84 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 283 ELESHRDQMIAEDKSIGSPMEEREKLLKQVKDDNQEIASMERQLTDIKEKINQFNEEIRQLDMDLEEHQGEMNQKYKELK 362
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 363 K------REENMDTFIETFEETKNQELERKAQIEANIVSLLEHCSRNINRMKQISSITNQELKMMQDDLNFKSTEVQKSQ 436
Cdd:COG4942 108 EllralyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEER 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622872397 437 STARNLTSDSQRLQLDLQKMELLESK----MTEEQHSLKSKIKQMTTDLE 482
Cdd:COG4942 188 AALEALKAERQKLLARLEKELAELAAelaeLQQEAEELEALIARLEAEAA 237
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
198-427 |
1.03e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 198 EKQMRSVEEEIE---QEKQAADDIIKNMSLENQVKYLEMKATNEKLLQELDTLQQQLDSQNMKKESMEAEIAhsQVKQEA 274
Cdd:COG4913 241 HEALEDAREQIEllePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELE--RLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 275 VLLHEKLYELESHRDQmiaedksIGSpmeEREKLLKQvkddnqEIASMERQLTDIKEKINQFNEEIRQLDMDLEEHQGEM 354
Cdd:COG4913 319 DALREELDELEAQIRG-------NGG---DRLEQLER------EIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 355 NQKYKELKKREENMDTFIETFEETKNQELERKAQIEANIVSLlehcSRNINRMKQ-ISSIT----------NQELKMMQD 423
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL----EAEIASLERrKSNIParllalrdalAEALGLDEA 458
|
....
gi 1622872397 424 DLNF 427
Cdd:COG4913 459 ELPF 462
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
77-482 |
3.33e-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: 47.04 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 77 LTGMKTGMKGPQRQILDKSYYLGLLRSKISELTTEVNKLQKEIEMYNQENSVYLSYEKRAETLAVEIKEFQGQLADYNML 156
Cdd:pfam15921 484 LTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKV 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 157 VDKLNTNTEmeevmnDYNMLKAQNDRETQSMDVifterqakekqmrsveEEIEQEKQAADdiiknmslenqvKYLEmkat 236
Cdd:pfam15921 564 IEILRQQIE------NMTQLVGQHGRTAGAMQV----------------EKAQLEKEIND------------RRLE---- 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 237 neklLQELDTLQqqlDSQNMKKESMEAEIahSQVKQEAVllheKLYELESHRDQMIAEDKsigspmEEREKLLKQVKDDN 316
Cdd:pfam15921 606 ----LQEFKILK---DKKDAKIRELEARV--SDLELEKV----KLVNAGSERLRAVKDIK------QERDQLLNEVKTSR 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 317 QEIASMERQLTDIKEKINQFNEEIR----QLDMDLEEHQGEMNQKYKELKKREENMDTFIETFEETKNQELERKAQIEA- 391
Cdd:pfam15921 667 NELNSLSEDYEVLKRNFRNKSEEMEtttnKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDAl 746
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 392 -NIVSLLEHCSRNINR----MKQISSITNQELKMMQDDLNFKSTEVQKSQSTARNLTSDSQRLQLDLQKMELLESK---- 462
Cdd:pfam15921 747 qSKIQFLEEAMTNANKekhfLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAEcqdi 826
|
410 420
....*....|....*....|.
gi 1622872397 463 -MTEEQHSLKSKIkQMTTDLE 482
Cdd:pfam15921 827 iQRQEQESVRLKL-QHTLDVK 846
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
89-465 |
4.78e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 89 RQILDKSYYLGLLRSKISELTTEVNKLQKEIEMYNQENSVYLSYEKRAETLAVEIKEFQGQLADYNMLVDKLNTNTEM-- 166
Cdd:PRK01156 204 KQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERhm 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 167 ----------EEVMNDYNMLKAQNDRETQSMDVIFTERQAKEKQMRSVEE------EIEQEKQAADDIIKNMSlenQVKY 230
Cdd:PRK01156 284 kiindpvyknRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVlqkdynDYIKKKSRYDDLNNQIL---ELEG 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 231 LEMKATNekLLQELDTLQQQLDSQNMKKESMEAEIAHSQVKQEAVLLHEKLYELESHRDQMIAEDKSigSPMEEREKLLK 310
Cdd:PRK01156 361 YEMDYNS--YLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKV--SSLNQRIRALR 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 311 QVKDDNQEIASM-------------------ERQLTDIKEKINQFNEEIRQLDMDLEehqgEMNQKYKELKKREENMDTF 371
Cdd:PRK01156 437 ENLDELSRNMEMlngqsvcpvcgttlgeeksNHIINHYNEKKSRLEEKIREIEIEVK----DIDEKIVDLKKRKEYLESE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 372 -IETFEETKNQELERKAQIEANIVSLlehcSRNINRMKQISSITNQELKMMQDDLNFKSTEVQKSQSTARNLTSDSQRLQ 450
Cdd:PRK01156 513 eINKSINEYNKIESARADLEDIKIKI----NELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIETNRSR 588
|
410
....*....|....*..
gi 1622872397 451 LDLQKMEL--LESKMTE 465
Cdd:PRK01156 589 SNEIKKQLndLESRLQE 605
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
190-525 |
6.59e-05 |
|
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: 46.12 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 190 IFTERQAKEKQMRSVEEEIEQEKQAADDIIKNMSLENQVKYLEMKATNEKLLQELDTLQQQLDSQNMKKESMEAEIAHSQ 269
Cdd:pfam02463 178 LIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 270 VKQEAVLlheklyELESHRDQMIAEDKSIGSPMEEREKLL-KQVKDDNQEIASMERQLTDIKEKINQFNEEIRQLDMDLE 348
Cdd:pfam02463 258 QEIEKEE------EKLAQVLKENKEEEKEKKLQEEELKLLaKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 349 EHQGEMNQKYKELKKREENMDTFIETFEETKNQELERKAQIEANIVSLLEHCSRNINRMKQISSITNQELKMMQDDLNFK 428
Cdd:pfam02463 332 KEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 429 STEVQKSQSTARNLTSDSQRLQLDLQKMELLESKMTEEQHSLKS----KIKQMTTDLETYNDLPALKSSGEEKKKKLHQE 504
Cdd:pfam02463 412 ELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKqelkLLKDELELKKSEDLLKETQLVKLQEQLELLLS 491
|
330 340
....*....|....*....|.
gi 1622872397 505 RMILSTRRNAFKKIMEKLNIE 525
Cdd:pfam02463 492 RQKLEERSQKESKARSGLKVL 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
238-384 |
7.02e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 7.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 238 EKLLQELDTLQQQLDSQNMKKESMEAEIAHSQVKQEAvllHEKLYELESHRDQMIAEDKSIgspmEEREKLLKQVKDDNQ 317
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREA---LQRLAEYSWDEIDVASAEREI----AELEAELERLDASSD 685
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622872397 318 EIASMERQLTDIKEKINQFNEEIRQLDMDLEEHQGEMNQKYKELKKREENMDTFIETFEETKNQELE 384
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
69-385 |
9.64e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 69 DRPVTQQGLTGMKTGM--KGPQRQIlDKSYYLG--------LLRSKISELTTEVNKLQKEIEMYNQEnsvYLSYEKRAET 138
Cdd:COG4913 574 PRAITRAGQVKGNGTRheKDDRRRI-RSRYVLGfdnraklaALEAELAELEEELAEAEERLEALEAE---LDALQERREA 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 139 LAvEIKEFQGQLADYNMLVDKL-NTNTEMEEVMNDYNMLKAQNDRE----------TQSMDVIFTERQAKEKQMRSVEEE 207
Cdd:COG4913 650 LQ-RLAEYSWDEIDVASAEREIaELEAELERLDASSDDLAALEEQLeeleaeleelEEELDELKGEIGRLEKELEQAEEE 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 208 IEQEKQAADDIIKNMS------LENQVKYLEMKATNEKLLQELDTLQQQLDSQNMKKESmEAEIAHSQVKQEAVLLH--- 278
Cdd:COG4913 729 LDELQDRLEAAEDLARlelralLEERFAAALGDAVERELRENLEERIDALRARLNRAEE-ELERAMRAFNREWPAETadl 807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 279 ----EKLYELESHRDQMIAEDksigspMEEREKLLKQVKDDNQE------IASMERQLTDIKEKINQFNEEIRQLD---- 344
Cdd:COG4913 808 dadlESLPEYLALLDRLEEDG------LPEYEERFKELLNENSIefvadlLSKLRRAIREIKERIDPLNDSLKRIPfgpg 881
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1622872397 345 ----MDLEEHQG-EMNQKYKELKKREENMDTFIETFEETKNQELER 385
Cdd:COG4913 882 rylrLEARPRPDpEVREFRQELRAVTSGASLFDEELSEARFAALKR 927
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
318-472 |
1.01e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 318 EIASMERQLTDIKEKINQFNEEIRQLDMDLEEHQGEMNQKYKELKKREENMDTFIETFEETKNQELERKAQIEANIVSLL 397
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 398 EHCSRN---------------INRMKQISSITNQELKMMqDDLNFKSTEVQKSQSTARNLTSDSQRLQLDLQKM-ELLES 461
Cdd:COG3883 97 RSGGSVsyldvllgsesfsdfLDRLSALSKIADADADLL-EELKADKAELEAKKAELEAKLAELEALKAELEAAkAELEA 175
|
170
....*....|.
gi 1622872397 462 KMTEEQHSLKS 472
Cdd:COG3883 176 QQAEQEALLAQ 186
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
171-486 |
1.23e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.28 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 171 NDYNMLKAQNDRETQSMDVIFTERQAKEKQMRSVE-EEIEQEKQAADdiiKNMSLENQVKYLEMKATnEKLLQELDTLQQ 249
Cdd:PLN02939 95 DDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQlEDLVGMIQNAE---KNILLLNQARLQALEDL-EKILTEKEALQG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 250 QLDSQNMKKESMEAEIA-HSQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQvkddnqEIASMERQLTD 328
Cdd:PLN02939 171 KINILEMRLSETDARIKlAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKE------ENMLLKDDIQF 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 329 IKEKINQFNEEIRQLDMdLEEHQGEMNQKYKELKKREENMDTFIETFEETKNQELERKAQieaNIVSLLEhcsRNINRMK 408
Cdd:PLN02939 245 LKAELIEVAETEERVFK-LEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVE---NLQDLLD---RATNQVE 317
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622872397 409 QISSITNQelkmmQDDLNFKSTEVQKSQSTARNLTSDSQRLQLDLQKMELLESKMTEEQHSLKSKIKQMTTDLETYND 486
Cdd:PLN02939 318 KAALVLDQ-----NQDLRDKVDKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQD 390
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
142-335 |
1.45e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 142 EIKEFQGQLADYNMLVDKLNTntEMEEVMNDYNMLKAQNDRETQSMDvifterqAKEKQMRSVEEEIEQEKQAADDIIKN 221
Cdd:COG3883 24 ELSELQAELEAAQAELDALQA--ELEELNEEYNELQAELEALQAEID-------KLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 222 MSLE-NQVKYLEM--KATN-EKLLQELDTLQQQLDSQNMKKESMEAEIAhsQVKQEAVLLHEKLYELESHRDQMIAEDKS 297
Cdd:COG3883 95 LYRSgGSVSYLDVllGSESfSDFLDRLSALSKIADADADLLEELKADKA--ELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622872397 298 IGSPMEEREKLLKQVKDD----NQEIASMERQLTDIKEKINQ 335
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEeaaaEAQLAELEAELAAAEAAAAA 214
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
253-389 |
1.75e-04 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 44.47 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 253 SQNMKKESMEAEIAHSQVKQEAV------------LLHEKLYELESHRDQMIAEDKSigSPMEEREKLLKQVKDDNQEIA 320
Cdd:PRK00106 23 SIKMKSAKEAAELTLLNAEQEAVnlrgkaerdaehIKKTAKRESKALKKELLLEAKE--EARKYREEIEQEFKSERQELK 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622872397 321 SMERQLTDIKEKINQFNEEIRQLDMDLEEHQGEMNQKYKELKKREENmdtfIETFEETKNQELERKAQI 389
Cdd:PRK00106 101 QIESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHIDEREEQ----VEKLEEQKKAELERVAAL 165
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
289-364 |
1.78e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 1.78e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622872397 289 DQMIAEDKSIGSPMEEREKLLKQVKDDNQEIASMERQLTDIKEKINQFNEEIRQLDMDLEEHQGEMNQKYKELKKR 364
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
176-548 |
2.97e-04 |
|
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: 44.01 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 176 LKAQNDRETQSMDVIFTE-RQAKEKQMRSVEEEIEQE-KQAADDIiknmslenqvkylemkATNEKLLQELDTLQQQLDS 253
Cdd:pfam01576 725 LKAQFERDLQARDEQGEEkRRQLVKQVRELEAELEDErKQRAQAV----------------AAKKKLELDLKELEAQIDA 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 254 QNMKKESmeaeiAHSQVKQEAVLLHEKLYELESHRdqmiaedksigspmEEREKLLKQVKDDNQEIASMERQLTDIKEKI 333
Cdd:pfam01576 789 ANKGREE-----AVKQLKKLQAQMKDLQRELEEAR--------------ASRDEILAQSKESEKKLKNLEAELLQLQEDL 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 334 NQFNEEIRQLDMDLEEHQGEMNQKYKElkkreenmdtfietfeetKNQELERKAQIEANIVSL---LEHCSRNINRMKQI 410
Cdd:pfam01576 850 AASERARRQAQQERDELADEIASGASG------------------KSALQDEKRRLEARIAQLeeeLEEEQSNTELLNDR 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 411 SSITNQELKMMQDDLNFKSTEVQKSQSTARNLTSDSQRLQLDLQKME-LLESKMTEEQHSLKSKIKQMTTDLETYNDLPA 489
Cdd:pfam01576 912 LRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEgTVKSKFKSSIAALEAKIAQLEEQLEQESRERQ 991
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622872397 490 LKSSGEEKKKKLHQERMIL--STRRNA--FKKIMEKLNIEHEALKTQLQENETHSQLTNLERK 548
Cdd:pfam01576 992 AANKLVRRTEKKLKEVLLQveDERRHAdqYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARR 1054
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
103-562 |
3.07e-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: 43.86 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 103 SKISELTTEVNKLQKEIEMYNQE----NSVYLSYEKRAETLAVEIKEFQGQLADYNmlvDKLNTNTEM-EEVMNDYNMLK 177
Cdd:TIGR04523 33 TEEKQLEKKLKTIKNELKNKEKElknlDKNLNKDEEKINNSNNKIKILEQQIKDLN---DKLKKNKDKiNKLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 178 AQNDRETQSMDvifterqAKEKQMRSVEEEIEQ-EKQAADDIIKNMSLENQVKYLEMKatNEKLLQELDTLQQQLDSQNM 256
Cdd:TIGR04523 110 SEIKNDKEQKN-------KLEVELNKLEKQKKEnKKNIDKFLTEIKKKEKELEKLNNK--YNDLKKQKEELENELNLLEK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 257 KKESMEAEIahSQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQVKDDNQEIASMERQLTDIKEKINQF 336
Cdd:TIGR04523 181 EKLNIQKNI--DKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 337 NEEIRQLDMDLEEHQGEM---NQKYKELKKREENMDTFIETFEETKNQEL--ERKAQIEA------NIVSLLEHCSRNIN 405
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELeqnNKKIKELEKQLNQLKSEISDLNNQKEQDWnkELKSELKNqekkleEIQNQISQNNKIIS 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 406 RMKQISSITNQELKMMQDDLNFKSTEVQKSQSTARNLTSDSQRLQLDLQKMEL----LESKMTEEQHSLKSKIKQMTTDL 481
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESqindLESKIQNQEKLNQQKDEQIKKLQ 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 482 ETYNDLPALKSSGEEKKKKLHQERMILSTRRNAFKKIMEKLNIEHEALKTQLQ--ENETHSQLTNLERKWQHHEQNNFVM 559
Cdd:TIGR04523 419 QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlSRSINKIKQNLEQKQKELKSKEKEL 498
|
...
gi 1622872397 560 KEL 562
Cdd:TIGR04523 499 KKL 501
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
238-396 |
4.53e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 238 EKLLQELDTLQQQLDSQNMKKESMEAEIAHSQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQVKDDNQ 317
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEE 163
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622872397 318 EIASMERQLTDIKEKINqfnEEIRQLDMDLEEHQGEMNQKYKELKKREENMDTFIETFEETKNQELERKAQIEANIVSL 396
Cdd:COG4717 164 ELEELEAELAELQEELE---ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
290-470 |
4.87e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.76 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 290 QMIAE-DKSIGSPMEEREKLLKQVKDDNQEIASMERQLTDIKEKINQFNEEIRQLDMDLEEHQGEMNQKYKELKKReenM 368
Cdd:PRK11637 54 QDIAAkEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAQ---L 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 369 DTFIETFEET------KNQELERKAQIEANIVSLlehcsrNINRMKQISsitnqELKMMQDDLNFKSTEVQKSQSTARNL 442
Cdd:PRK11637 131 DAAFRQGEHTglqlilSGEESQRGERILAYFGYL------NQARQETIA-----ELKQTREELAAQKAELEEKQSQQKTL 199
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622872397 443 TSDSQRLQldlQKMEL-----------LESKMTEEQHSL 470
Cdd:PRK11637 200 LYEQQAQQ---QKLEQarnerkktltgLESSLQKDQQQL 235
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
105-550 |
6.98e-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: 42.80 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 105 ISELTTEVNKL-QKEIEMYNQENSVYLSYEKRAETLAVEIKEFQGQLADYNMLVDKLNTntEMEEVMNDYnmlkaqnDRE 183
Cdd:pfam15921 273 ISEHEVEITGLtEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRS--ELREAKRMY-------EDK 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 184 TQSMDVIFTERQAKEKQMRSVEEEIEQEKQAADDIIKNM--SLENQVKYLEMKATNEKLLQELDT--------LQQQLDS 253
Cdd:pfam15921 344 IEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLlaDLHKREKELSLEKEQNKRLWDRDTgnsitidhLRRELDD 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 254 QNMKKESMEAeiahsqvkqeavLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQVKDDNQEIASMERQLTDIKEKI 333
Cdd:pfam15921 424 RNMEVQRLEA------------LLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTL 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 334 NQFNEEIRQLDMDLEEHQGEMNQKYKELKKREENMDTFIETFEETKNQELE-RKAQIEANIVSL-LEHCSRNINRMKQis 411
Cdd:pfam15921 492 ESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHlRNVQTECEALKLqMAEKDKVIEILRQ-- 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 412 SITNQELKMMQDDLNFKSTEVQKSQstarnLTSDSQRLQLDLQKMELLESKMTEEQHSLKSKIKQMttDLETYNDLPAlK 491
Cdd:pfam15921 570 QIENMTQLVGQHGRTAGAMQVEKAQ-----LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL--ELEKVKLVNA-G 641
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622872397 492 SSGEEKKKKLHQERMILSTRRNAFKKIMEKLNIEHEALKTQLQENETHSQLTNLERKWQ 550
Cdd:pfam15921 642 SERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ 700
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
193-398 |
7.26e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 193 ERQAKEKQMRSVEEEIEQEKQAADDIIKNMSlENQVKYLEMKATNEKLLQELDTLQQQLDSQNMKKESMEA---EIAHSQ 269
Cdd:COG1340 44 KRDELNAQVKELREEAQELREKRDELNEKVK-ELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKlrkEIERLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 270 VKQE-AVLLHEKlyeleshRDQMIAEDKSIGSPMEEREKLLKQvkddNQEIASMERQLTDIKEKINQFNEEIRQLDMDLE 348
Cdd:COG1340 123 WRQQtEVLSPEE-------EKELVEKIKELEKELEKAKKALEK----NEKLKELRAELKELRKEAEEIHKKIKELAEEAQ 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622872397 349 EHQGEMNQKYKELKKREENMDTFIETFEETKNQELERKAQIEANIVSLLE 398
Cdd:COG1340 192 ELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE 241
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
143-345 |
9.47e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 143 IKEFQGQLADYNMLVDKLNTNTEMEEvmNDYNMLKAQNDRETQSMDVIFTERQAKEKQMRSVEEE---------IEQEKQ 213
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHIQQQIKTYN--KNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEEltdellnlvMDIEDP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 214 AAD-------DIIKNMSLENQVKYLEMKATN-----------------EKLLQELDTLQQQLDsQNMKKESMEAEIAHsQ 269
Cdd:PHA02562 254 SAAlnklntaAAKIKSKIEQFQKVIKMYEKGgvcptctqqisegpdriTKIKDKLKELQHSLE-KLDTAIDELEEIMD-E 331
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622872397 270 VKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQVKDDNQEIASMERQLTDIKEKINQFNEEIRQLDM 345
Cdd:PHA02562 332 FNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGI 407
|
|
| TTC8_N |
cd21341 |
N-terminal domain of tetratricopeptide repeat domain 8; Tetratricopeptide repeat domain 8 ... |
7-63 |
9.53e-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: 39.59 E-value: 9.53e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622872397 7 SSAARPVSRggvglTGRPPSGI--------RPLSGNIRVATAMPPGTARPGS----RGGPIGTGGVLSS 63
Cdd:cd21341 66 SQAMRPTTS-----SGRPITGFvrpgtqsgRPGTSRQALRTPRRAGTARPVTsasgRFVRLGTASMLSG 129
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
304-486 |
1.13e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 304 EREKLLK-QVKDDNQEIASMERQLTDIKEKINQFNEEIRQLDMDLEEHQGEMNQKYKELKKREENMdtfietfeetKNQE 382
Cdd:PHA02562 167 EMDKLNKdKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTI----------KAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 383 LERKAQIeANIVSLLEHCSRNINRMKQISSITNQELKMMQDDLNFK-------------STEVQKSQSTARNLTSDSQRL 449
Cdd:PHA02562 237 EELTDEL-LNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYekggvcptctqqiSEGPDRITKIKDKLKELQHSL 315
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622872397 450 QLDLQKMELLESKMTE------EQHSLKSKIKQMTTDLETYND 486
Cdd:PHA02562 316 EKLDTAIDELEEIMDEfneqskKLLELKNKISTNKQSLITLVD 358
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
192-541 |
1.25e-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: 41.65 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 192 TERQAKEKQMRSVEEEIEQEKqaaddiiknmslENQVKYLEMKatnEKLLQELDTLQQQLDSQNMKKESMEAEIAHSQVK 271
Cdd:pfam17380 285 SERQQQEKFEKMEQERLRQEK------------EEKAREVERR---RKLEEAEKARQAEMDRQAAIYAEQERMAMERERE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 272 QEAVLLHEKLYELESHRDQMIAEDKsigSPMEEREKLlkqvkddnqeiaSMERQLTDikEKINQFNEEIRQLDMDLEEHQ 351
Cdd:pfam17380 350 LERIRQEERKRELERIRQEEIAMEI---SRMRELERL------------QMERQQKN--ERVRQELEAARKVKILEEERQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 352 GEMNQKYKEL----KKREENMDTFIETFEETKNQELERKAQIEanivsllehcsrnINRMKQISSITNQE-------LKM 420
Cdd:pfam17380 413 RKIQQQKVEMeqirAEQEEARQREVRRLEEERAREMERVRLEE-------------QERQQQVERLRQQEeerkrkkLEL 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 421 MQDDLNFKSTEVQKSQSTARNLTSDSQRLQLDLQKMELLESKMTEEQHSLKSKIKQMTTDLETyndlpalKSSGEEKKKK 500
Cdd:pfam17380 480 EKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEER-------RKQQEMEERR 552
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1622872397 501 LHQERMILSTRRNAFKKIMEKlniEHEALKtQLQENETHSQ 541
Cdd:pfam17380 553 RIQEQMRKATEERSRLEAMER---EREMMR-QIVESEKARA 589
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
99-537 |
1.52e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 99 GLLRSKISELTTEVNKLQKEIEMYNQENSvylSYEKRAETLAVEIKEFQGQLADYNMLVDKLNT-----NTEMEEVMnDY 173
Cdd:pfam15921 373 GNLDDQLQKLLADLHKREKELSLEKEQNK---RLWDRDTGNSITIDHLRRELDDRNMEVQRLEAllkamKSECQGQM-ER 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 174 NMLKAQNDRET-QSMDVIFTERQAKEKQMRSVEEEIEQEK---QAADDIIKNMSLENQVKYLEMKATNekllQELDTLQQ 249
Cdd:pfam15921 449 QMAAIQGKNESlEKVSSLTAQLESTKEMLRKVVEELTAKKmtlESSERTVSDLTASLQEKERAIEATN----AEITKLRS 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 250 QLDSQNMKKESMEAEIAHSQVKQEavllheklyELESHRDQMIAEDKSIgspmeerEKLLKQVKDDNQEIASMERQLTDI 329
Cdd:pfam15921 525 RVDLKLQELQHLKNEGDHLRNVQT---------ECEALKLQMAEKDKVI-------EILRQQIENMTQLVGQHGRTAGAM 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 330 KEKINQFNEEIRQLDMDLEEhqgemnqkYKELKKREEnmdtfietfeeTKNQELE-RKAQIEANIVSLLEHCSRNINRMK 408
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQE--------FKILKDKKD-----------AKIRELEaRVSDLELEKVKLVNAGSERLRAVK 649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 409 QISSITNQ---ELKMMQDDLNFKSTEVQKSQSTARN------LTSDSQRLQLDLQKMELLESKMT------EEQHSLKSK 473
Cdd:pfam15921 650 DIKQERDQllnEVKTSRNELNSLSEDYEVLKRNFRNkseemeTTTNKLKMQLKSAQSELEQTRNTlksmegSDGHAMKVA 729
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 474 I---KQMTTDL--------------ETYNDLPALKSSGEEKKKKLHQERMILSTRRNAFKKIMEKLNIEHEALKTQLQEN 536
Cdd:pfam15921 730 MgmqKQITAKRgqidalqskiqfleEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANM 809
|
.
gi 1622872397 537 E 537
Cdd:pfam15921 810 E 810
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
101-307 |
1.65e-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: 40.90 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 101 LRSKISELTTEVNKLQKEIEMYNQENSvylSYEKRAETLAVEIKEFQGQLADYNMLVDKLNTNTEMEEVMNDYNMLKAQn 180
Cdd:COG4942 60 LERRIAALARRIRALEQELAALEAELA---ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAV- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 181 dRETQSMDVIFTERQAKEKQMRSVEEEIEQEKQAADdiiknmslenqvkylEMKATNEKLLQELDTLQQQLDSQNMKKES 260
Cdd:COG4942 136 -RRLQYLKYLAPARREQAEELRADLAELAALRAELE---------------AERAELEALLAELEEERAALEALKAERQK 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622872397 261 MEAEIAHSQVKQEAvllheKLYELESHRDQMIAEDKSIGSPMEEREK 307
Cdd:COG4942 200 LLARLEKELAELAA-----ELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
101-274 |
1.83e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 101 LRSKISELTTEVNKLQKEIEMYNQENSvylSYEKRAETLAVEIKEFQGQLADY----------NMLVDKLNTNTEMEEVM 170
Cdd:COG3883 42 LQAELEELNEEYNELQAELEALQAEID---KLQAEIAEAEAEIEERREELGERaralyrsggsVSYLDVLLGSESFSDFL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 171 NDYNMLKAQNDRETQSMDVIFTERQAKEKQMRSVEEEIEQEKQAADDIIKNMS-LENQVKylEMKATNEKLLQELDTLQQ 249
Cdd:COG3883 119 DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAeLEAQQA--EQEALLAQLSAEEAAAEA 196
|
170 180
....*....|....*....|....*
gi 1622872397 250 QLDSQNMKKESMEAEIAHSQVKQEA 274
Cdd:COG3883 197 QLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
109-482 |
1.83e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.58 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 109 TTEVNKLQKEIEMYNQENSVYLS----YEKRAETLAVEIKefqGQLADYNMLVDKLNTNTEMEEVMNDYNMLKAQNDRET 184
Cdd:TIGR01612 1110 ADEINKIKDDIKNLDQKIDHHIKaleeIKKKSENYIDEIK---AQINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKK 1186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 185 ---QSMDVIFTERQAKEKQMRSVE------------------EEIEQEKQAADDIIKNMslenqvkylemkatnEKLLQE 243
Cdd:TIGR01612 1187 niyDEIKKLLNEIAEIEKDKTSLEevkginlsygknlgklflEKIDEEKKKSEHMIKAM---------------EAYIED 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 244 LDTLQQQ--------LDSQNMKKESMEAEIAHSQVKQEAVLLHEKLYELESHRDQMI------AEDKSIGSPMEEREKLL 309
Cdd:TIGR01612 1252 LDEIKEKspeienemGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSLkiiedfSEESDINDIKKELQKNL 1331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 310 KQVKDDNQEIASMERQLTDIKE--KINQfneeIRQLDMDLEEHQGEMNQKYKELKKREENMDTFIETFEETKNQElERKA 387
Cdd:TIGR01612 1332 LDAQKHNSDINLYLNEIANIYNilKLNK----IKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLE-ECKS 1406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 388 QIEANIVSL-LEHCSRNINRMKqissitnqelkmmqddlNFKSTEVQKSQSTARNLTSDSQRLQLDLQKMELLESKmteE 466
Cdd:TIGR01612 1407 KIESTLDDKdIDECIKKIKELK-----------------NHILSEESNIDTYFKNADENNENVLLLFKNIEMADNK---S 1466
|
410
....*....|....*.
gi 1622872397 467 QHSLKSKIKQMTTDLE 482
Cdd:TIGR01612 1467 QHILKIKKDNATNDHD 1482
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
107-342 |
1.89e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 107 ELTTEVNKLQKEIEMYNQENSVYLSYEKRAETLAVEIKEFQGQLADYNMLVDKLNTNT---------EMEEVMNDYNMLK 177
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESveeleerlkELEPFYNEYLELK 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 178 AQndretqsmdvifterqakEKQMRSVEEEIEQEKQAADDIIKNMSLENqvKYLEMKatnEKLLQELDTLQQQLDSQNMK 257
Cdd:PRK03918 609 DA------------------EKELEREEKELKKLEEELDKAFEELAETE--KRLEEL---RKELEELEKKYSEEEYEELR 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 258 KESMEAEIAHSQVKqeavllhEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQVKDDNQEIASMERqltdIKEKINQFN 337
Cdd:PRK03918 666 EEYLELSRELAGLR-------AELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE----LREKVKKYK 734
|
....*
gi 1622872397 338 EEIRQ 342
Cdd:PRK03918 735 ALLKE 739
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
103-349 |
1.99e-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: 40.90 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 103 SKISELTTEVNKLQKEIEmynQENSVYLSYEKRAETLAVEIKEFQGQLADYNMLVDKLNTNtemeevmndynmLKAQNDR 182
Cdd:COG4942 20 DAAAEAEAELEQLQQEIA---ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE------------LAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 183 ETQsmdvifterqaKEKQMRSVEEEIEQEKQAADDIIKNMSLENQVKYLEMKATNEKLLQ---ELDTLQQQLDSQNMKKE 259
Cdd:COG4942 85 LAE-----------LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDavrRLQYLKYLAPARREQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 260 SMEAEIAhsQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQVkddNQEIASMERQLTDIKEKINQFNEE 339
Cdd:COG4942 154 ELRADLA--ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL---EKELAELAAELAELQQEAEELEAL 228
|
250
....*....|
gi 1622872397 340 IRQLDMDLEE 349
Cdd:COG4942 229 IARLEAEAAA 238
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
161-483 |
2.03e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 161 NTNTEMEEVMNDYNMLKAQNDRETQSMDVIFTERQAKEKQMrsveEEIEQEKQAADDIIKNMSLENQVKYLEMKATNEKL 240
Cdd:TIGR00618 546 DVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDI----PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKL 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 241 LQELDTLQQQLDSQNMKKESMEAEIAHSQvkqeavLLHEKLYELESHRDQMIAEDKsigspmeerEKLLKQVKDDNQEIA 320
Cdd:TIGR00618 622 QPEQDLQDVRLHLQQCSQELALKLTALHA------LQLTLTQERVREHALSIRVLP---------KELLASRQLALQKMQ 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 321 SMERQLTDIKEKINQFNEEIRQldmdLEEHQGEMNQKYKELKKREENMDTFIETFEETKNQELERKAQIEANIVSLLEHC 400
Cdd:TIGR00618 687 SEKEQLTYWKEMLAQCQTLLRE----LETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEA 762
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 401 SRNINRMKQISSITNQELKMMQDDLNFKSTEVQKS-QSTARNLTSDSQRLQLDLQKMELLESKMTEEQHSLKSKIKQMTT 479
Cdd:TIGR00618 763 HFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDtHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSA 842
|
....
gi 1622872397 480 DLET 483
Cdd:TIGR00618 843 TLGE 846
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
101-563 |
2.23e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 101 LRSKISELTTEVNKLQKEIEMYNQENSVY---LSYEKRAETLAVEIKEFQGQLADYNMLVDKLNTNTEMEEVMNDYNMLK 177
Cdd:TIGR00618 224 LEKELKHLREALQQTQQSHAYLTQKREAQeeqLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVT 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 178 AQNdretQSMDVIFTERQAkekQMRSVEEEIEQEKQAADDiikNMSLENQVKYLEmkatneKLLQELDTLQQQLDSQNMK 257
Cdd:TIGR00618 304 QIE----QQAQRIHTELQS---KMRSRAKLLMKRAAHVKQ---QSSIEEQRRLLQ------TLHSQEIHIRDAHEVATSI 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 258 KESMEAEIAHSQ----VKQEAVLLHEKLYELESHRDQMIAEDKSIgSPMEEREKLLKQVKDDNQEIASMERQLTDIKEki 333
Cdd:TIGR00618 368 REISCQQHTLTQhihtLQQQKTTLTQKLQSLCKELDILQREQATI-DTRTSAFRDLQGQLAHAKKQQELQQRYAELCA-- 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 334 nQFNEEIRQLDMDLEEHQGEMNQKYKELKKREENMDTFIETFEETKNQELERKAQIEANIVSLLEHCS------------ 401
Cdd:TIGR00618 445 -AAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIhpnparqdidnp 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 402 --------RNINRMK-----------QISSITNQ------ELKMMQDDLNFKSTEVQKSQSTARNLTSDSQRLQLDLQKM 456
Cdd:TIGR00618 524 gpltrrmqRGEQTYAqletseedvyhQLTSERKQraslkeQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 457 ELLESKMTEEQHSLKSKIKQMTTDLETYNDLPALKSSGEEKKKKLHQERMILSTRRnafkkimeklnIEHEALKTQLQEN 536
Cdd:TIGR00618 604 SEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQER-----------VREHALSIRVLPK 672
|
490 500
....*....|....*....|....*..
gi 1622872397 537 ETHSQLTNLERKWQHHEQNNFVMKELL 563
Cdd:TIGR00618 673 ELLASRQLALQKMQSEKEQLTYWKEML 699
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
101-392 |
2.49e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 101 LRSKISELTTEVNKLQKE----IEMYNQENSVYLSYEKRAETLAV---EIKEFQGQLA----DYNMLVDKLNTNTE-MEE 168
Cdd:PRK02224 211 LESELAELDEEIERYEEQreqaRETRDEADEVLEEHEERREELETleaEIEDLRETIAeterEREELAEEVRDLRErLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 169 VMNDYNMLKAQNDRETQSMDVIFTERQAKEKQMRSVEEEIEQEKQAADDIIKNM-SLENQVKYLEMKATN-----EKLLQ 242
Cdd:PRK02224 291 LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAeSLREDADDLEERAEElreeaAELES 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 243 ELDTLQQQLDSQNMKKESMEAEI-------AHSQVKQEAV-----LLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLK 310
Cdd:PRK02224 371 ELEEAREAVEDRREEIEELEEEIeelrerfGDAPVDLGNAedfleELREERDELREREAELEATLRTARERVEEAEALLE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 311 QVK------------------DDNQEIASMERQLTDIKEKINQFNEEIRQLDmDLEEHQGEMNqkykELKKREENMDTFI 372
Cdd:PRK02224 451 AGKcpecgqpvegsphvetieEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIE----RLEERREDLEELI 525
|
330 340
....*....|....*....|
gi 1622872397 373 ETFEETKNQELERKAQIEAN 392
Cdd:PRK02224 526 AERRETIEEKRERAEELRER 545
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
135-526 |
3.35e-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: 40.34 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 135 RAETLAVEIKEFQGQLADYNMLVDKLNTNTEMEEVMNDYNMLKAQNDRETQSMDVIFTERQAKEKQmrsvEEEIEQEKQA 214
Cdd:pfam02463 654 LEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEA----EELLADRVQE 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 215 ADDIIKNMSLENQVKYLEMKATNEKLLQELDTLQQQLDSQNMKKESMEAEIAHSQVKQEAVLLHEKLYELESHRDQMIAE 294
Cdd:pfam02463 730 AQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEE 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 295 DKSIGSPMEEREKLLKQVKDDNQEIASMERQLTDIKEKINQFNEE-IRQLDMDLEEHQGEMNQKYKELKKREENMDTFIE 373
Cdd:pfam02463 810 LKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEeLERLEEEITKEELLQELLLKEEELEEQKLKDELE 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 374 TFEETKNQELERKAQIEANIVSLLEHCSRNINRMKQISSITNQELKMMQDDLNFKSTEVQKSQSTARNLTSDSQRLQLDL 453
Cdd:pfam02463 890 SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAK 969
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622872397 454 QKMELLESKMteeqhslkskIKQMTTDLETYNDLPALKSSGEEKKKKLHQERMILSTRRnaFKKIMEKLNIEH 526
Cdd:pfam02463 970 EELGKVNLMA----------IEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQR--LKEFLELFVSIN 1030
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
206-391 |
3.89e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 206 EEIEQEKQAADDIIKNmsLENQVKYLEMKATNEKLLQELDTLQQQLDSQNMKKESMEAEIAhSQVKQEAVLLHEKLYELE 285
Cdd:PRK03918 462 KRIEKELKEIEEKERK--LRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEEL-EKKAEEYEKLKEKLIKLK 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 286 SHRDQMIAEDKSIGSPMEEREKLLKQVKDDNQEIASMERQLTDIK-EKINQFNEEIRQLD------MDLEEHQGEMNQKY 358
Cdd:PRK03918 539 GEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyneyLELKDAEKELEREE 618
|
170 180 190
....*....|....*....|....*....|...
gi 1622872397 359 KELKKREENMDTFIETFEETKNQELERKAQIEA 391
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
104-517 |
3.90e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 104 KISELTTEVNKLQKEIEMYNQENSV-YLSYEKRAETLAVEIKEFQGQLADYNMLVDKLntnTEMEEVMNDYNMLKAQNDR 182
Cdd:PRK01156 274 YYKELEERHMKIINDPVYKNRNYINdYFKYKNDIENKKQILSNIDAEINKYHAIIKKL---SVLQKDYNDYIKKKSRYDD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 183 --------ETQSMDVIFTERQAKEKQMRSVEEEIEQEKQAAD------------DIIKNMSLENQVKYLEMKATNEKLLQ 242
Cdd:PRK01156 351 lnnqilelEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFiseilkiqeidpDAIKKELNEINVKLQDISSKVSSLNQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 243 ELDTLQQQLD--SQNM------------------------------KKESMEAEIAHsqVKQEAVLLHEKLYELESHRDQ 290
Cdd:PRK01156 431 RIRALRENLDelSRNMemlngqsvcpvcgttlgeeksnhiinhyneKKSRLEEKIRE--IEIEVKDIDEKIVDLKKRKEY 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 291 MIAED--KSIGS--PMEEREKLLKQVKDDNQEIASMERQLTDIKEKINQFNEEIRQL-------------DMDLEEHQGE 353
Cdd:PRK01156 509 LESEEinKSINEynKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSkrtswlnalavisLIDIETNRSR 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 354 MNQKYKELKKREENMDTFIETFEETKNQELERKAQIEANIVSLlehcsRNINRMKQISSITNQELKMMQDDLNFKSTEVQ 433
Cdd:PRK01156 589 SNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNL-----NNKYNEIQENKILIEKLRGKIDNYKKQIAEID 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 434 KSQSTARNLTSDSQRLQLDLQKMELLESKMTEEQHSLKSKIKQMTTDLETYNDLPALKSSGEEKKKKLHQERMILSTRRN 513
Cdd:PRK01156 664 SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDLKRLRE 743
|
....
gi 1622872397 514 AFKK 517
Cdd:PRK01156 744 AFDK 747
|
|
| V_ScBro1_like |
cd09237 |
Protein-interacting V-domain of Saccharomyces cerevisiae Bro1 and related domains; This family ... |
207-362 |
5.51e-03 |
|
Protein-interacting V-domain of Saccharomyces cerevisiae Bro1 and related domains; This family contains the V-shaped (V) domain of Saccharomyces cerevisiae Bro1, and related domains. It belongs to the V_Alix_like superfamily which also includes the V-domain of Saccharomyces cerevisiae Rim20 (also known as PalA), mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Bro1 interacts with the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in endosomal trafficking. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Bro1 also has an N-terminal Bro1-like domain, which binds Snf7, a component of the ESCRT-III complex, and a C-terminal proline-rich region (PRR). The C-terminal portion (V-domain and PRR) of S. cerevisiae Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes. It interacts with a YPxL motif in the Doa4s catalytic domain to stimulate its deubiquitination activity.
Pssm-ID: 185750 [Multi-domain] Cd Length: 356 Bit Score: 39.20 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 207 EIEQEKQAADDIIKNMSLENQVKylEMKATNEKLLQELDTLQQQLDSQNMKKESMEAEIAHSQVKQEAVLLHEKLYE-LE 285
Cdd:cd09237 54 EGENELMEIVSGLKSSSVDSQLE--LLRPQSASWVNEIDSSYNDLDEEMKEIEKMRKKILAKWTQSPSSSLTASLREdLV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 286 SHRDQMIAEDKSigspmeeREKLLKQVKDDNQEIASMERQLTDIKEKINQFNEEIRQ---LDMDLEEHQGEMNQKYKELK 362
Cdd:cd09237 132 KLKKSLVEASAS-------DEKLFSLVDPVKEDIALLLNGGSLWEELFGFSSSGSPEpslLDLDDSQNEQTVLKQIKQLE 204
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
132-399 |
5.60e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 132 YEKRAETLAVEIKEFQGQLADYNMLVDklntntemeevmndynmlkAQNDRETQSmdvifteRQAKekqmrSVEEEIEQE 211
Cdd:PRK04863 381 NEARAEAAEEEVDELKSQLADYQQALD-------------------VQQTRAIQY-------QQAV-----QALERAKQL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 212 KQAADdiiknMSLENQVKYLE-MKATNEKLLQELDTLQQQLDSQNMKKESME----------AEIAHSQVKQEAVllhEK 280
Cdd:PRK04863 430 CGLPD-----LTADNAEDWLEeFQAKEQEATEELLSLEQKLSVAQAAHSQFEqayqlvrkiaGEVSRSEAWDVAR---EL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 281 LYELESHR----------------DQMIAEDKSIGSPMEEREKLLKQVKDDNQEIASMERQLTDIKEKINQFNEEIRQLD 344
Cdd:PRK04863 502 LRRLREQRhlaeqlqqlrmrlselEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERR 581
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622872397 345 MDLEEHQGEMNQKYKELKKREE---NMDTFIETFEETKNQELERKAQIEANIVSLLEH 399
Cdd:PRK04863 582 MALRQQLEQLQARIQRLAARAPawlAAQDALARLREQSGEEFEDSQDVTEYMQQLLER 639
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
101-539 |
5.86e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 101 LRSKISELTTEVNKLQKEIEMYNQENSVYLSYEKRAETLAVEIKEFQGQLADYNMLVDKLNTN----TEMEEVMNDYNML 176
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelKELKEKAEEYIKL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 177 KAQNDRETQSMDVIFTERQAKEKQMRSVEEEIEQ--EKQAADDIIKNMSLENQVKYLEMKaTNEKLLQELDTLQQQLDSQ 254
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKEleEKEERLEELKKKLKELEKRLEELE-ERHELYEEAKAKKEELERL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 255 NMKKESMEAEiahsQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQVKDDNQEIASMERQLTdikekin 334
Cdd:PRK03918 378 KKRLTGLTPE----KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT------- 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 335 qfneeirqldmdlEEHQGEMNQKY-KELKKREENMDTFIETFEETKNQ--ELERKAQIEANIVSLLEhcsrninRMKQIS 411
Cdd:PRK03918 447 -------------EEHRKELLEEYtAELKRIEKELKEIEEKERKLRKElrELEKVLKKESELIKLKE-------LAEQLK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 412 SITNQELKMMQDDLNFKSTEVQKSQSTARNLTSDSQRLQLDLQKMELLESKMTE---EQHSLKSKIKQMTTDLET----- 483
Cdd:PRK03918 507 ELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAElekKLDELEEELAELLKELEElgfes 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 484 --------------YN----------DLPALKSSGEEKKKKLHQERMILSTRRNAFKKI--------------------- 518
Cdd:PRK03918 587 veeleerlkelepfYNeylelkdaekELEREEKELKKLEEELDKAFEELAETEKRLEELrkeleelekkyseeeyeelre 666
|
490 500
....*....|....*....|..
gi 1622872397 519 -MEKLNIEHEALKTQLQENETH 539
Cdd:PRK03918 667 eYLELSRELAGLRAELEELEKR 688
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
101-300 |
6.97e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.23 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 101 LRSKISELTTEVNKLQKEIEMYNQENSVyLSYEKRAETLAVEIKEFQGQLAD-----------YNMLVDKLNTN-TEMEE 168
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGL-VDLSEEAKLLLQQLSELESQLAEaraelaeaearLAALRAQLGSGpDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 169 VMND--YNMLKAQ-NDRETQ--SMDVIFTERQAkekQMRSVEEEIEQEKQAADDIIKNMSLENQVKYLEMKATNEKLLQE 243
Cdd:COG3206 259 LLQSpvIQQLRAQlAELEAElaELSARYTPNHP---DVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQ 335
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622872397 244 LDTLQQQLDSQNmkkesmEAEIAHSQVKQEAVLLhEKLYE--LESHRDQMIAEDKSIGS 300
Cdd:COG3206 336 LAQLEARLAELP------ELEAELRRLEREVEVA-RELYEslLQRLEEARLAEALTVGN 387
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
316-537 |
7.95e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.98 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 316 NQEIASMERQLTDIKEKINQFNEEIRQLDMDLEEHQGEM---NQKYKELKKREENMDTFIETFEETKNQELERKAQIEAN 392
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLaalERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 393 IVSLLEHCSRNINRMKQISSITNQELKMMQDDLNFKSTEVQKSQSTARNLTSDSQRLQLDLQKMELLESKMTEEQHSLKS 472
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622872397 473 KIKQMTTDLETyndLPALKSSGEEKKKKLHQERMILSTRRNAFKKIMEKLNIEHEALKTQLQENE 537
Cdd:COG4942 179 LLAELEEERAA---LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
88-381 |
8.02e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 39.05 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 88 QRQILDKSYYLGllrSKISELTTEVNKLQKEIEMYNQENSV--YLSYEKRAETLAVEIKEFQGQLADYNMLVDKLNTN-- 163
Cdd:PRK04778 153 RKSLLANRFSFG---PALDELEKQLENLEEEFSQFVELTESgdYVEAREILDQLEEELAALEQIMEEIPELLKELQTElp 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 164 TEMEEVMNDYNMLKAQN-DRETQSMDViftERQAKEKQMRSVEEEIEQ-EKQAADDIIKNmsLENQVKYL------EMKA 235
Cdd:PRK04778 230 DQLQELKAGYRELVEEGyHLDHLDIEK---EIQDLKEQIDENLALLEElDLDEAEEKNEE--IQERIDQLydilerEVKA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 236 TNEkLLQELDTLQQQLDSQNMKKESMEAEIAHsqVKQEavllheklYELeSHRDqmIAEDKSIGspmEEREKLLKQVKDD 315
Cdd:PRK04778 305 RKY-VEKNSDTLPDFLEHAKEQNKELKEEIDR--VKQS--------YTL-NESE--LESVRQLE---KQLESLEKQYDEI 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 316 NQEIAS--------------MERQLTDIKEKINQFNEEIRQL---DMDLEEHQGEMNQKYKELKKREENM------DTFI 372
Cdd:PRK04778 368 TERIAEqeiayselqeeleeILKQLEEIEKEQEKLSEMLQGLrkdELEAREKLERYRNKLHEIKRYLEKSnlpglpEDYL 447
|
....*....
gi 1622872397 373 ETFEETKNQ 381
Cdd:PRK04778 448 EMFFEVSDE 456
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
188-530 |
8.84e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 188 DVIFTERQAKEKQMRSVE--EEIEQEKQAADDIIKNmsLENQVKYLEmkatnekllqelDTLQQQLDSQNMKKEsMEAEI 265
Cdd:PRK03918 138 DAILESDESREKVVRQILglDDYENAYKNLGEVIKE--IKRRIERLE------------KFIKRTENIEELIKE-KEKEL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 266 AhsQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQVKDDNQEIASMERQLTDIKEKINQFNEEIRQLDm 345
Cdd:PRK03918 203 E--EVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 346 dleehqgemnQKYKELKKREENMDTFIEtFEETKNQELERKAQIEANIVSLLEHCSRNINRMKQISSitnqelkmmqddl 425
Cdd:PRK03918 280 ----------EKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE------------- 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 426 nfKSTEVQKSQSTARNLTSDSQRLQLDLQKMELLESKMTEEQhSLKSKIKQMTTDletynDLPALKSSGEEKKKKLHQER 505
Cdd:PRK03918 336 --KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELE-RLKKRLTGLTPE-----KLEKELEELEKAKEEIEEEI 407
|
330 340
....*....|....*....|....*
gi 1622872397 506 MILSTRRNAFKKIMEKLNIEHEALK 530
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELK 432
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
101-437 |
9.61e-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: 39.26 E-value: 9.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 101 LRSKISELTTEVNKLQKEI-EMYNQ-----ENSVYLSyekraeTLAVEIKEFQGQLADYNMLVDKLNTNTEMEEVMNDY- 173
Cdd:TIGR01612 563 IKKELEEENEDSIHLEKEIkDLFDKyleidDEIIYIN------KLKLELKEKIKNISDKNEYIKKAIDLKKIIENNNAYi 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 174 ----NMLKAQNDRETQSMDVIFTERQAKEKQMrsVEEEIEQEKQAADDIIKnmslENQVKYLEMKAtnekllqELDTLQQ 249
Cdd:TIGR01612 637 delaKISPYQVPEHLKNKDKIYSTIKSELSKI--YEDDIDALYNELSSIVK----ENAIDNTEDKA-------KLDDLKS 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 250 QLDS-----QNMKKESMEAEIAHSQVKQEAVLlhEKLYELESHRDQMIAEDksIGSPMEEREKLLKQVKDDNQEIASMER 324
Cdd:TIGR01612 704 KIDKeydkiQNMETATVELHLSNIENKKNELL--DIIVEIKKHIHGEINKD--LNKILEDFKNKEKELSNKINDYAKEKD 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872397 325 QLTDIKEKI----NQFNEEIRQLDMDLEEHQGEMNQKYKELKKREENMDTFIETFEETKNQELERKAQIEAnIVSLLEHC 400
Cdd:TIGR01612 780 ELNKYKSKIseikNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDK-FINFENNC 858
|
330 340 350
....*....|....*....|....*....|....*....
gi 1622872397 401 SRNINR-MKQISSITNQELKMMQDD-LNFKSTEVQKSQS 437
Cdd:TIGR01612 859 KEKIDSeHEQFAELTNKIKAEISDDkLNDYEKKFNDSKS 897
|
|
| |
