|
Name |
Accession |
Description |
Interval |
E-value |
| Rabaptin |
pfam03528 |
Rabaptin; |
9-498 |
0e+00 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 765.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 9 QPDVSLQQRVAELEKINAEFLRAQQQLEQEFNQKRAKFKELYLAKEEDLKRQNAVLQAAQDDLGHLRTQLWEAQAEMENI 88
Cdd:pfam03528 1 QPDEDLQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEEDLKRQNAVLQEAQVELDALQNQLALARAEMENI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 89 KAIATVSENTKQEAIDEVKRQWREEVASLQAVMKETVRDYEHQFHLRLEQERAQWAQYRESADREIADLRRRLSEGQEEE 168
Cdd:pfam03528 81 KAVATVSENTKQEAIDEVKSQWQEEVASLQAIMKETVREYEVQFHRRLEQERAQWNQYRESAEREIADLRRRLSEGQEEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 169 NLENEMKKAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELEASKVKELNHYLEAEKSCRTDLEMYVAVLNTQKSVL 248
Cdd:pfam03528 161 NLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMKELNHYLEAEKSCRTDLEMYVAVLNTQKSVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 249 QEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQRMEIVLTSEQLRQVEELKKKDQEDDEQQR 328
Cdd:pfam03528 241 QEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQRMESVLTSEQLRQVEEIKKKDQEEHKRAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 329 LnNKRKDHKKTDAEEEAKIPVVCALTQEESSAQLSNEEfqEHLDSTHGSVHSLDADLLLPSGDPFSKSDnDMFKDGLRRA 408
Cdd:pfam03528 321 T-HKEKETLKSDREHTVSIHAVFSPAGVETSAPLSNVE--EQINSAHGSVHSLDTDVVLGAGDSFNKQE-DPFKEGLRRA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 409 QSTDSLGTSGSLQSKALGYNYKAKSAGNLDESDFGPLVGADSVSENFDTASLGSLQMPSGFMLTKDQERAIKAMTPEQEE 488
Cdd:pfam03528 397 QSTDSLGSSSSLQHKFLGHNQKAKSAGNLDESDFGPLVGADSVSENFDTSSLGSLKMPSGFMLTKDQEKAIKAMTPEQEE 476
|
490
....*....|
gi 2072346481 489 TASLLSSVTQ 498
Cdd:pfam03528 477 TASLLSSVTQ 486
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
33-345 |
3.68e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 33 QQLEQEFNQKRAkfkELYLAKEEDLKRQnavLQAAQDDLGHLRTQLWEAQAEMENIKAIATVSENTKQEAIDEVKRQWRE 112
Cdd:COG1196 216 RELKEELKELEA---ELLLLKLRELEAE---LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 113 EVASLQAVMKETvrdyEHQFHLRLEQERAQwaQYRESADREIADLRRRLSE-GQEEENLENEMKKAQEDAEKLrsvvmpm 191
Cdd:COG1196 290 EYELLAELARLE----QDIARLEERRRELE--ERLEELEEELAELEEELEElEEELEELEEELEEAEEELEEA------- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 192 EKEIAALKDKLTEAEDKIKELEASKVKELNHYLEAEKScRTDLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQ 271
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA-AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2072346481 272 QHNQLKHTWQKANDQFLESQRLLMRDMQRMEIVLTSEQLRQVEELKKKDQEDDEQQRLNNKRKDHKKTDAEEEA 345
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
14-318 |
6.25e-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: 62.38 E-value: 6.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 14 LQQRVAELEKINAEFLRAQQQLEQEFNQKRAKFKELYL---AKEEDLKRQNAVLQAAQDDLGHLRTQLWEAQAEMENIKA 90
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 91 IATVSENTKQEAIDEVKRQwREEVASLQAVMKETVRDYE--HQFHLRLEQERAQWAQYRESADREIADLRRRLsegqeeE 168
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEEL-EAQIEQLKEELKALREALDelRAELTLLNEEAANLRERLESLERRIAATERRL------E 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 169 NLENEMKKAQEDAEKLrsvvmpmEKEIAALKDKLTEAEDKIKELEASKvKELNHYLEAEKSCRTDLEMYVAVLNTQKSVL 248
Cdd:TIGR02168 842 DLEEQIEELSEDIESL-------AAEIEELEELIEELESELEALLNER-ASLEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 249 QEDAEKLRKELHEVCHLLEQERQQHNQLKhtwqkanDQFLESQRLLMRDMQRMEIVLTSEQLRQVEELKK 318
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLQ-------ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
13-283 |
8.70e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 8.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 13 SLQQRVAELEKINAEFLRAQQQLEQEFNQKRAKFKELylakEEDLKRQNAVLQAAQDDLGHLRTQLWEAQAEMENIKAia 92
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYEL----LAELARLEQDIARLEERRRELEERLEELEEELAELEE-- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 93 tvsentKQEAIDEVKRQWREEVASLQAVMKETVRDYEHQFHLRLEQERAQwAQYRESADREIADLRRRLSEGQEEENLEN 172
Cdd:COG1196 331 ------ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL-AEAEEELEELAEELLEALRAAAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 173 EMKKAQEDAEKLRSVvmpMEKEIAALKDKLTEAEDKIKELEASKVKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDA 252
Cdd:COG1196 404 ELEEAEEALLERLER---LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
250 260 270
....*....|....*....|....*....|...
gi 2072346481 253 EKLRKELHEVC--HLLEQERQQHNQLKHTWQKA 283
Cdd:COG1196 481 ELLEELAEAAArlLLLLEAEADYEGFLEGVKAA 513
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
135-392 |
3.03e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 135 RLEQERAQWAQYRESADREIADLRRRLSEGQEE-ENLENEMKKAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELE 213
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLElEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 214 ---ASKVKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAEKLR---KELHEVCHLLEQERQQHNQLKHTWQKANDQF 287
Cdd:COG1196 323 eelAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLeaeAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 288 LESQRLLMRDMQRMEIVLTSEQLRQVEELKKKDQEDDEQQRLNNKRKDHKKTDAEEEAKIPVVCALTQEESSAQLSNEEF 367
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
250 260
....*....|....*....|....*
gi 2072346481 368 QEHLDSTHGSVHSLDADLLLPSGDP 392
Cdd:COG1196 483 LEELAEAAARLLLLLEAEADYEGFL 507
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
99-373 |
6.51e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 6.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 99 KQEAIDEVKRQwREEVASLQAVMKETVRDYEHQFhLRLEQERAQWAQYRESADREIADLRRRLS-EGQEEENLENEMKKA 177
Cdd:TIGR02168 675 RRREIEELEEK-IEELEEKIAELEKALAELRKEL-EELEEELEQLRKELEELSRQISALRKDLArLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 178 QEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELEAsKVKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAEKLRK 257
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA-QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 258 ELHEVCHLLEQERQQHNQLKHTWQKANDQfLESQRLLMRDMQRmEIVLTSEQLRQVEELKKKDQEDDEQQRLNNKRKDHK 337
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAE-IEELEELIEELES-ELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
250 260 270
....*....|....*....|....*....|....*.
gi 2072346481 338 KTDAEEEAKipvvcALTQEESSAQLSNEEFQEHLDS 373
Cdd:TIGR02168 910 RSELRRELE-----ELREKLAQLELRLEGLEVRIDN 940
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
134-385 |
1.01e-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: 58.53 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 134 LRLEQERAQWAQYRESADREIadlrrrlsegQEEENLENEMKKAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELE 213
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAE----------EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 214 ASKV-------------KELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTW 280
Cdd:TIGR02168 302 QQKQilrerlanlerqlEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 281 QKAND---QFLESQRLLMRDMQRMEIVLTSEQLRQveELKKKDQEDDEQQRLNNKRKDHK----KTDAEEEAKIPVVCAL 353
Cdd:TIGR02168 382 ETLRSkvaQLELQIASLNNEIERLEARLERLEDRR--ERLQQEIEELLKKLEEAELKELQaeleELEEELEELQEELERL 459
|
250 260 270
....*....|....*....|....*....|..
gi 2072346481 354 TQEESSAQLSNEEFQEHLDSTHGSVHSLDADL 385
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARL 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
13-322 |
2.92e-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: 57.00 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 13 SLQQRVAELEKINAEFLRAQQQLEQEFNQKRAKFKELYLAKEEDLKRQNAVLQ---AAQDDLGHLRTQLWEAQAEMENIK 89
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQeeeKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 90 AiatvsentKQEAIDEVKRQWREEVASLQAVMKETVRDYEHQFHLRLEQERAQWAQYRESADREIADLRRRL-SEGQEEE 168
Cdd:TIGR02169 758 S--------ELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLnRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 169 NLENEMKKAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELEAsKVKELNHYLEAEKSCRTDLEmyvavlnTQKSVL 248
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA-ALRDLESRLGDLKKERDELE-------AQLREL 901
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2072346481 249 QEDAEKLRKElhevchlLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQRMEIVLTSEQLrqVEELKKKDQE 322
Cdd:TIGR02169 902 ERKIEELEAQ-------IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDV--QAELQRVEEE 966
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
13-300 |
3.84e-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: 56.60 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 13 SLQQRVAELEKINAEFLRAQQQLEQEFNQKRAKFKELylakeEDLKRQNAVLQAAQDdlghlrtqlwEAQAEMENIKAia 92
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKL-----EELRLEVSELEEEIE----------ELQKELYALAN-- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 93 tvsentKQEAIDEVKRQWREEVASLQAVMKETVRDYEHQFH--LRLEQERAQWAQYRESADREIADLRRRLSEGQEE-EN 169
Cdd:TIGR02168 296 ------EISRLEQQKQILRERLANLERQLEELEAQLEELESklDELAEELAELEEKLEELKEELESLEAELEELEAElEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 170 LENEMKKAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELEASKVKELNHYLEAEKSCrtdLEMYVAVLNTQKSVLQ 249
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL---EEAELKELQAELEELE 446
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2072346481 250 EDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLL--MRDMQR 300
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdsLERLQE 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
77-347 |
2.78e-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: 53.52 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 77 QLWEAQAEMENIKAIATVSEN---TKQEAIDEVKRQWREEVASLQAVMKETVRDYEhqfhlRLEQERAQWAQYRESADRE 153
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAelrKELEELEEELEQLRKELEELSRQISALRKDLA-----RLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 154 IADLRRRLSEGQEEENLENEMKKAQED-AEKLrsvvmpmEKEIAALKDKLTEAEDKIKELEAsKVKELNHYLEAEKSCRT 232
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAeIEEL-------EAQIEQLKEELKALREALDELRA-ELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 233 DLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQRMEIVltSEQLRQ 312
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL--SEELRE 905
|
250 260 270
....*....|....*....|....*....|....*
gi 2072346481 313 VEelKKKDQEDDEQQRLNNKRKDHKKTDAEEEAKI 347
Cdd:TIGR02168 906 LE--SKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
14-266 |
4.34e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 14 LQQRVAELEKInaefLRAQQQLEQEFNQKRAKFKELYLAKEEDLKRQNAVLQAAQDDLGHLRTQLWEAQAEMENIKAIAT 93
Cdd:COG1196 293 LLAELARLEQD----IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 94 VSENTKQEAIDEVKRQWREEVASLQAvmketvrdyEHQFHLRLEQERAQWAQYRESADREIADLRRRLSEGQEEENLENE 173
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRA---------AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 174 MKKAQEDAEKLRSVVmpmEKEIAALKDKLTEAEDKIKELEASKVKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAE 253
Cdd:COG1196 440 EEEALEEAAEEEAEL---EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
250
....*....|...
gi 2072346481 254 KLRKELHEVCHLL 266
Cdd:COG1196 517 AGLRGLAGAVAVL 529
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
19-266 |
1.70e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 19 AELEKINAEFLRAQQQLEQEFNQKRAKFKELylakeEDLKRQNAVLQAAQDDLGHLRTQLWEAQAEMENIKAIATVSENT 98
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRL-----EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 99 KQEAIDEVKRQWREEVASLQAVmkETVRDYEHQFHLRLEQERAQWAQYRESADREIADLRRRLSEGQ--EEENLENEMKK 176
Cdd:TIGR02168 885 LEEALALLRSELEELSEELREL--ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYslTLEEAEALENK 962
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 177 AQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELEASKvKELNHYLEAEKSCRTDLEMYVAVLNTQ-KSVLQEDAEKL 255
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERY-DFLTAQKEDLTEAKETLEEAIEEIDREaRERFKDTFDQV 1041
|
250
....*....|.
gi 2072346481 256 RKELHEVCHLL 266
Cdd:TIGR02168 1042 NENFQRVFPKL 1052
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
22-370 |
8.40e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 22 EKINAEFLRAQQQLEQEFNQKRAKfkelYLAKEEDLKRQNAVLQAAQDDLGHLRTQLWEAQAEMENIKAIATVSENTKQE 101
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKAE----ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 102 AIDEVKRQWREEVASLQAVMKETVRDYEHQFHLRLEQERAQWAQYRESADREIADLRRRLSEGQEEENLENEMKKAQEDA 181
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 182 EKLRSVVMPMEKEIAALKDKLTEAEDKIKELEASKVKELNHYLEAEKSCRTDLEMyvavlntqksvlQEDAEKLRKElhe 261
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED------------KKKAEEAKKD--- 1752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 262 vchllEQERQQHNQLKHTWQKANDQFLESQRLLMRDmqrmEIVLTSEQLRQVEELKKKDQEDDEQQRLNNKRKDHKKTDA 341
Cdd:PTZ00121 1753 -----EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE----ELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVIND 1823
|
330 340
....*....|....*....|....*....
gi 2072346481 342 EEEAKIPVVCALTQEESSAQLSNEEFQEH 370
Cdd:PTZ00121 1824 SKEMEDSAIKEVADSKNMQLEEADAFEKH 1852
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
13-214 |
1.01e-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: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 13 SLQQRVAELEKINAEFLRAQQQLE---------QEFNQKRAKFKEL-YLAKEEDLKRQNAVLQAAQDDLGHLRTQLWEAQ 82
Cdd:COG4913 229 ALVEHFDDLERAHEALEDAREQIEllepirelaERYAAARERLAELeYLRAALRLWFAQRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 83 AEMENIKAiatvSENTKQEAIDEVKRQWRE----EVASLQAVMKetvrdyehqfhlRLEQERAQWAQYRESADREIADLr 158
Cdd:COG4913 309 AELERLEA----RLDALREELDELEAQIRGnggdRLEQLEREIE------------RLERELEERERRRARLEALLAAL- 371
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2072346481 159 rRLSEGQEEENLENEMKKAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELEA 214
Cdd:COG4913 372 -GLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
15-361 |
1.61e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 15 QQRVAELEKINAEFLRAQQQLEQEFNQKRAKFKELYLAKEEDLKRQNAVLQAAQDDLGHLRTQLWEAQAEMENIKAIATV 94
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEA 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 95 ---SENTKQEAiDEVKRQWREEVASLQAVMKETVRDYEHqfhLRLEQERAQWAQYRESADREIADLRRRLSEgqEEENLE 171
Cdd:PTZ00121 1321 kkkAEEAKKKA-DAAKKKAEEAKKAAEAAKAEAEAAADE---AEAAEEKAEAAEKKKEEAKKKADAAKKKAE--EKKKAD 1394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 172 NEMKKAQEDAEKLRSVvmpmeKEIAALKDKLTEAEDKIKEL-----------EASKVKELNHYLE----AEKSCRTDLEM 236
Cdd:PTZ00121 1395 EAKKKAEEDKKKADEL-----KKAAAAKKKADEAKKKAEEKkkadeakkkaeEAKKADEAKKKAEeakkAEEAKKKAEEA 1469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 237 YVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHT--------------WQKANDQFLESQRLLMRDMQRME 302
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAdeakkaeeakkadeAKKAEEAKKADEAKKAEEKKKAD 1549
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2072346481 303 IVLTSEQLRQVEELKKKDQEDDEQQRLNNKRKDHKKTDAEEEAKIPVVCALTQEESSAQ 361
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
138-348 |
2.99e-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: 46.68 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 138 QERAQWAQYRESADREIADLRRRLSEGQ-EEENLENEMKKAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELEASK 216
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKkEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 217 VKELNHYLE----AEKSCR-------------TDLEMYVAVLNTQKSVLQEDAEKLRKELHEvchlLEQERQQHNQLKHT 279
Cdd:COG4942 100 EAQKEELAEllraLYRLGRqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAE----LAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2072346481 280 WQKANDQFLESQRLLMRDMQRMEIVLTSEQLRQVEELKKKDQEDDEQQRLNNKRKDHKKTDAEEEAKIP 348
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
536-562 |
3.15e-05 |
|
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow for binding to the GTPase Rab5. This interaction is necessary and sufficient for Rab5-dependent recruitment of Rabaptin5 to early endosomal membranes.
Pssm-ID: 462752 [Multi-domain] Cd Length: 307 Bit Score: 46.11 E-value: 3.15e-05
10 20
....*....|....*....|....*..
gi 2072346481 536 CDMCSNYEKQLQGIQIQEAETRDQVKK 562
Cdd:pfam09311 1 CDMCSNYEKQLQAIQEQEAETRDQVKK 27
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
158-346 |
3.50e-05 |
|
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: 46.66 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 158 RRRLSEGQEEENLENEMKKAQEDAEKLRSVVMPMEKEIAALKDKLteAEDKIKELEASKVKELNHYLEAEKSCRTDLEM- 236
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERM--AMERERELERIRQEERKRELERIRQEEIAMEIs 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 237 YVAVLNTQKSVLQEDAEKLRKELHEV--CHLLEQERQQHNQLKHTW------QKANDQFLESQRLLMRDMQRMEIVLTSE 308
Cdd:pfam17380 376 RMRELERLQMERQQKNERVRQELEAArkVKILEEERQRKIQQQKVEmeqiraEQEEARQREVRRLEEERAREMERVRLEE 455
|
170 180 190
....*....|....*....|....*....|....*....
gi 2072346481 309 QLRQVE-ELKKKDQEDDEQQRLNNKRKDHKKTDAEEEAK 346
Cdd:pfam17380 456 QERQQQvERLRQQEEERKRKKLELEKEKRDRKRAEEQRR 494
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
26-219 |
4.86e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 26 AEFLRA--QQQLEQEFNQ---KRAKFKELYLAKEEDLKRQNAVLQAAQDDLGHLRTQLWEAQAEMENIKAIATVSENtKQ 100
Cdd:COG4717 40 LAFIRAmlLERLEKEADElfkPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE-EL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 101 EAIDEVKRQWR--EEVASLQAVMKETVRDYEHqfHLRLEQERAQWAQYRESADREIADLRRRLSEGQEEENL--ENEMKK 176
Cdd:COG4717 119 EKLEKLLQLLPlyQELEALEAELAELPERLEE--LEERLEELRELEEELEELEAELAELQEELEELLEQLSLatEEELQD 196
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2072346481 177 AQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELEASKVKE 219
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
13-317 |
7.55e-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: 45.88 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 13 SLQQRVAELEKINAEFLRAQQQLEQEFNQKRAKFKELYLAKEE-DLKRQNavLQAAQDDLghlrtqlweaqaEMENIKAI 91
Cdd:pfam15921 573 NMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKkDAKIRE--LEARVSDL------------ELEKVKLV 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 92 ATVSENTKQ-EAIDEVKRQWREEVASLQAVMKETVRDYEhqfhlrleQERAQWAQYRESADREIADLRRRLSEGQEE-EN 169
Cdd:pfam15921 639 NAGSERLRAvKDIKQERDQLLNEVKTSRNELNSLSEDYE--------VLKRNFRNKSEEMETTTNKLKMQLKSAQSElEQ 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 170 LENEMKKAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELEA--SKVKELNHYLEAEKScrtDLEMYVAVLNTQKSV 247
Cdd:pfam15921 711 TRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEamTNANKEKHFLKEEKN---KLSQELSTVATEKNK 787
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 248 LQEDAEKLRKELHEVchlleqeRQQHNQLKHTWQKANDQFLESQRLLMRDMQRmEIVLTSEQLRQVEELK 317
Cdd:pfam15921 788 MAGELEVLRSQERRL-------KEKVANMEVALDKASLQFAECQDIIQRQEQE-SVRLKLQHTLDVKELQ 849
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
75-223 |
1.06e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 75 RTQLWEAQAEMENIKAIATVS-ENTKQEAIDEVKRQWreevaslqavmketvrdyehqFHLRLEQERaqwaQYREsADRE 153
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEaEAIKKEALLEAKEEI---------------------HKLRNEFEK----ELRE-RRNE 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 154 IADLRRRLSegQEEENLENEMkkaqEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELEASKVKELNHY 223
Cdd:PRK12704 84 LQKLEKRLL--QKEENLDRKL----ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
13-225 |
1.40e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 13 SLQQRVAELEKINAEFLRAQQQLEqefnQKRAKFKELYLAKEEdLKRQNAVLQAAQDDLGHLRTQLWEAQAEMENIKAIA 92
Cdd:COG4913 672 ELEAELERLDASSDDLAALEEQLE----ELEAELEELEEELDE-LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 93 TVSENTK---QEAIDEVKRQWREEVASLQAVMKETVRDYEHQFHLRLEQERAQWAQYRESADREIADLR--RRLSEGQEE 167
Cdd:COG4913 747 LRALLEErfaAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPeyLALLDRLEE 826
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2072346481 168 ENL---ENEMKKAQEDAeklrsvvmpMEKEIAALKDKLTEAEDKIKEleasKVKELNHYLE 225
Cdd:COG4913 827 DGLpeyEERFKELLNEN---------SIEFVADLLSKLRRAIREIKE----RIDPLNDSLK 874
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
151-272 |
1.46e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 151 DREIADLRRRLSEGQEE-ENLENEMKKAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELE-----ASKVKE---LN 221
Cdd:COG1579 16 DSELDRLEHRLKELPAElAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnVRNNKEyeaLQ 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2072346481 222 HYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQ 272
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
19-117 |
1.60e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 19 AELEkINAEFLRAQQQLEQEFNQKRAKF---------KELYLAKE-EDLKRQNAVLQAAQDDLGHLRTQLWEAQAEMENI 88
Cdd:PRK12704 58 ALLE-AKEEIHKLRNEFEKELRERRNELqklekrllqKEENLDRKlELLEKREEELEKKEKELEQKQQELEKKEEELEEL 136
|
90 100 110
....*....|....*....|....*....|....*...
gi 2072346481 89 KA--------IATVS-ENTKQEAIDEVKRQWREEVASL 117
Cdd:PRK12704 137 IEeqlqelerISGLTaEEAKEILLEKVEEEARHEAAVL 174
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
4-214 |
2.01e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 4 PGPASQPDVSLQQRVAELEKINAEFLRAQQQLEQEFNQKRAKFKELYLAkEEDLKRQNAVLQAAQDDLGHLRTQLWEAQA 83
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-ERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 84 EmenIKAIATVSENTKQEAIDEVKRQWR----------------EEVASLQAVMKETVRDYEHQFHlRLEQERAQWAQYR 147
Cdd:COG4942 91 E---IAELRAELEAQKEELAELLRALYRlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAE-ELRADLAELAALR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2072346481 148 ESADREIADLRRRLSEGQEE-ENLENEMKKAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELEA 214
Cdd:COG4942 167 AELEAERAELEALLAELEEErAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
151-280 |
2.12e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 151 DREIADLRRRLSEGQEEENLENEMKKAQEDAE--KLRSVVMPMEKEIAALKDKLTEAEDKIKELEAsKVKELNhyLEAEK 228
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEirRLEEQVERLEAEVEELEAELEEKDERIERLER-ELSEAR--SEERR 459
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2072346481 229 SCRTDLEMyvavlntqkSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTW 280
Cdd:COG2433 460 EIRKDREI---------SRLDREIERLERELEEERERIEELKRKLERLKELW 502
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
86-227 |
2.17e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 86 ENIKAIATVSENTKQEAIDEVKRQWREEVASLQAVMKETVRDYEHQFHlRLEQERAQWAQYRESADREIADLRRRLSEGQ 165
Cdd:COG2433 376 LSIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVE-RLEAEVEELEAELEEKDERIERLERELSEAR 454
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2072346481 166 EEENLEnemkkAQEDAEklrsvVMPMEKEIAALKDKLTEAEDKIKELEaSKVKELNHYLEAE 227
Cdd:COG2433 455 SEERRE-----IRKDRE-----ISRLDREIERLERELEEERERIEELK-RKLERLKELWKLE 505
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
14-347 |
3.33e-04 |
|
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: 43.81 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 14 LQQRVAELEKINAEFLRAQQQLEQEFNQKRAKFKELYLAKEE-DLKRQNAVLQAAQDDLGHLRTQLWEAQAEMENIKAIA 92
Cdd:pfam02463 680 ELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEElLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKK 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 93 TVSENTKQEAIDEVKRQWREEVASLQAVMKETVRDYEhQFHLRLEQERAQWAQYRESADREIADLRRRLSEGQEEENLEN 172
Cdd:pfam02463 760 EEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKL-KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEEL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 173 E-MKKAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELEASKVKELNHYLEAEKSC-RTDLEMYVAVLNTQKSVLQE 250
Cdd:pfam02463 839 AlELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEeKKELEEESQKLNLLEEKENE 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 251 DAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQR---MEIVLTSEQLRQVEELKKKDQEDDEQQ 327
Cdd:pfam02463 919 IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAkeeLGKVNLMAIEEFEEKEERYNKDELEKE 998
|
330 340
....*....|....*....|
gi 2072346481 328 RLNNKRKDHKKTDAEEEAKI 347
Cdd:pfam02463 999 RLEEEKKKLIRAIIEETCQR 1018
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
12-330 |
4.01e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 12 VSLQQRVAELEKINAEFLRAQQQLEQEFN----------------QKRAKFKELYLAKEEDLKRQNAVLQAAQDDLGHLR 75
Cdd:COG3096 302 AEEQYRLVEMARELEELSARESDLEQDYQaasdhlnlvqtalrqqEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 76 TQLWEAQAEMENIKA-IATVsentkQEAIDEVKR---QWREEVASLQAVMKETVRD--YEHQFHLRLEQERAQwaqyRES 149
Cdd:COG3096 382 ARLEAAEEEVDSLKSqLADY-----QQALDVQQTraiQYQQAVQALEKARALCGLPdlTPENAEDYLAAFRAK----EQQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 150 ADREIADLRRRLS-----EGQEEENLE------------NEMKKAQEDAEKLRSVVMPMEKEiAALKDKLTEAEDKIKEL 212
Cdd:COG3096 453 ATEEVLELEQKLSvadaaRRQFEKAYElvckiageversQAWQTARELLRRYRSQQALAQRL-QQLRAQLAELEQRLRQQ 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 213 EASK--VKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHT---WQKAND-- 285
Cdd:COG3096 532 QNAErlLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapaWLAAQDal 611
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2072346481 286 --------QFLESQRLLMRDMQRmeivlTSEQLRQVEELK-----KKDQEDDEQQRLN 330
Cdd:COG3096 612 erlreqsgEALADSQEVTAAMQQ-----LLEREREATVERdelaaRKQALESQIERLS 664
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
87-275 |
4.08e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 87 NIKAIATVSEntKQEAIDEVKRQWREEVASLQAVMKETVRdyehQFHLRLEQERAQWAQYR-ESADREIADL---RRRLS 162
Cdd:COG4913 608 NRAKLAALEA--ELAELEEELAEAEERLEALEAELDALQE----RREALQRLAEYSWDEIDvASAEREIAELeaeLERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 163 EGQEE-ENLENEMKKAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELE-----ASKVKELNHYLEAEKSCRTDLEM 236
Cdd:COG4913 682 ASSDDlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQdrleaAEDLARLELRALLEERFAAALGD 761
|
170 180 190
....*....|....*....|....*....|....*....
gi 2072346481 237 yvAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQ 275
Cdd:COG4913 762 --AVERELRENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
14-322 |
4.76e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 14 LQQRVAELEKINAEFLRAQQQLEQEFNQKR-----------AKFKELYLAKEEdLKRQNAVLQAAQDDLGHLRTQLWEAQ 82
Cdd:PRK03918 350 LEKRLEELEERHELYEEAKAKKEELERLKKrltgltpekleKELEELEKAKEE-IEEEISKITARIGELKKEIKELKKAI 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 83 AEMENIKAIATV-SENTKQEAIDEVKRQWREEVASLQAVMKETVRDYEHQFHLRLEQERAQWAQYRESADREIADLRRRL 161
Cdd:PRK03918 429 EELKKAKGKCPVcGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKEL 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 162 SEGQEEENLEnEMKKAQEDAEKLRSVVMPMEKEI----------AALKDKLTEAEDKIKELEaSKVKELNHYLEAEK-SC 230
Cdd:PRK03918 509 EEKLKKYNLE-ELEKKAEEYEKLKEKLIKLKGEIkslkkeleklEELKKKLAELEKKLDELE-EELAELLKELEELGfES 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 231 RTDLEM-----------YVAVLNTQKSV---------LQEDAEKLRKELHEVCHLLEQERQQHNQLK-----HTWQKAND 285
Cdd:PRK03918 587 VEELEErlkelepfyneYLELKDAEKELereekelkkLEEELDKAFEELAETEKRLEELRKELEELEkkyseEEYEELRE 666
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2072346481 286 QFLESQRLLMR--------DMQRMEIVLTSEQL-RQVEELKKKDQE 322
Cdd:PRK03918 667 EYLELSRELAGlraeleelEKRREEIKKTLEKLkEELEEREKAKKE 712
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
15-160 |
4.92e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 15 QQRVAELEKINAEFLRAQQQLEQEFNQKRAKFKELyLAKEEDLKRQnaVLQAAQDDLGHLRTQLWEAQAEMENIKAIAT- 93
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDAL-REELDELEAQ--IRGNGGDRLEQLEREIERLERELEERERRRAr 363
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2072346481 94 ---------VSENTKQEAIDEVKRQWREEVASLQAvMKETVRDYEHQFHLRLEQERAQwaqyRESADREIADLRRR 160
Cdd:COG4913 364 leallaalgLPLPASAEEFAALRAEAAALLEALEE-ELEALEEALAEAEAALRDLRRE----LRELEAEIASLERR 434
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
14-185 |
5.18e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 14 LQQRVAELEKINAEFLRAQ---QQLEQEFNQKRAKFKELY-----LAKEEDLKRQNAVLQAAQDDLGHLRTQLWEAQAEM 85
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQeelEELEEELEELEAELEELReelekLEKLLQLLPLYQELEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 86 ENIKaiatvsenTKQEAIDEVKRQWREEVASLQAVMKETVRDYEHQFHlRLEQERAQWAQYRESADREIADLRRRLSEGQ 165
Cdd:COG4717 156 EELR--------ELEEELEELEAELAELQEELEELLEQLSLATEEELQ-DLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180
....*....|....*....|
gi 2072346481 166 EEENLENEMKKAQEDAEKLR 185
Cdd:COG4717 227 EELEQLENELEAAALEERLK 246
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
192-386 |
6.31e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 192 EKEIAALKDKLTEAEDKIKELE------------ASKVKELNHYLEAEKSC-----RTDLEMYVAVLNTQKSVLQEDAEK 254
Cdd:COG1196 178 ERKLEATEENLERLEDILGELErqleplerqaekAERYRELKEELKELEAEllllkLRELEAELEELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 255 LRKELHEVCHLLEQERQQHNQLkhtwQKANDQFLESQRLLMRDMQRMEIVLTSEQLRQVEELKKKDQEDDEQQRLNNKRK 334
Cdd:COG1196 258 LEAELAELEAELEELRLELEEL----ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2072346481 335 DHKKTDAEEEAKIPvvcALTQEESSAQLSNEEFQEHLDSTHGSVHSLDADLL 386
Cdd:COG1196 334 ELEEELEELEEELE---EAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
152-344 |
7.12e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 152 REIADLRRRLSEGQEE-ENLENEMKKAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELEaSKVKELNHYLEAEKSC 230
Cdd:PRK03918 210 NEISSELPELREELEKlEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK-KEIEELEEKVKELKEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 231 RTDLEMYVAvlntqksvLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLMRDmqrmeivltSEQL 310
Cdd:PRK03918 289 KEKAEEYIK--------LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL---------KELE 351
|
170 180 190
....*....|....*....|....*....|....
gi 2072346481 311 RQVEELKKKDQEDDEQQRLNNKRKDHKKTDAEEE 344
Cdd:PRK03918 352 KRLEELEERHELYEEAKAKKEELERLKKRLTGLT 385
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
15-215 |
9.01e-04 |
|
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: 42.03 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 15 QQRVAELEKINAEFLRAQQQLEQEFNQkrakfkelylakEEDLKRQNAVLQAAQDDlghlrtqlwEAQAEMENIKAIATV 94
Cdd:pfam17380 442 EERAREMERVRLEEQERQQQVERLRQQ------------EEERKRKKLELEKEKRD---------RKRAEEQRRKILEKE 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 95 SENTKQEAIDEV-KRQWREEvaslqavmketvrdyehqfhlrlEQERAQWAQYRESADREIADLRRRLSEGQEEENLENE 173
Cdd:pfam17380 501 LEERKQAMIEEErKRKLLEK-----------------------EMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQ 557
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2072346481 174 MKKAQEDaeklRSVVMPMEKEIAALKdKLTEAEDKIKELEAS 215
Cdd:pfam17380 558 MRKATEE----RSRLEAMEREREMMR-QIVESEKARAEYEAT 594
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
15-369 |
1.09e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 15 QQRVAELEKINAEFLRAQQQLEQEFNQKRAKFKELYLAKEEDlKRQNAVLQAAQDDLGHLRTQLWEAQAEMENIKAIATV 94
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED-KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 95 SENTKQEAiDEVKRQWREEVASLQAVMKETVRDYEHQFHLRLEQERAQWAQYRESADREIADLRRRLSEGQEEENLENEM 174
Cdd:PTZ00121 1711 EAEEKKKA-EELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 175 KKAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELEASKVKElnhyleaekscrtdlemyvaVLNTQKSVLQEDAEK 254
Cdd:PTZ00121 1790 EKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKE--------------------VADSKNMQLEEADAF 1849
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 255 LRKELHEVCHLLEQERQQHNQLKHTWQKAND--QFLESQRLLMRDMQRMEIVLTSEQLR-----------QVEELKKKDQ 321
Cdd:PTZ00121 1850 EKHKFNKNNENGEDGNKEADFNKEKDLKEDDeeEIEEADEIEKIDKDDIEREIPNNNMAgknndiiddklDKDEYIKRDA 1929
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2072346481 322 EDDEQQRLNNKRKDHKKTDAEEEakipvVCALTQEE-SSAQLSNEEFQE 369
Cdd:PTZ00121 1930 EETREEIIKISKKDMCINDFSSK-----FCDYMKDNiSSGNCSDEERKE 1973
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
13-223 |
1.35e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 13 SLQQRVAELEKiNAEFLRAQQqlEQEFNQKRAKFKELyLAKEEDLKRQNAVLQAA-----------QDDLGHLRTQLWEA 81
Cdd:PHA02562 192 HIQQQIKTYNK-NIEEQRKKN--GENIARKQNKYDEL-VEEAKTIKAEIEELTDEllnlvmdiedpSAALNKLNTAAAKI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 82 QAEMENIKAIA------TVSENTKQEAIDEVKRqwreeVASLQAVMKETVRDYEhQFHLRLEQERAQWAQYREsADREIA 155
Cdd:PHA02562 268 KSKIEQFQKVIkmyekgGVCPTCTQQISEGPDR-----ITKIKDKLKELQHSLE-KLDTAIDELEEIMDEFNE-QSKKLL 340
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2072346481 156 DLRRRLS-EGQEEENLENEMKKAQEDAEKLRSVVMPMEKEIAALKDKLteaeDKIKELEASKVKELNHY 223
Cdd:PHA02562 341 ELKNKIStNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDEL----DKIVKTKSELVKEKYHR 405
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
144-347 |
1.48e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 144 AQYRESADREIADLRRRLSEGQEE-ENLENEMKKAQEDAEKLRSVVMP--MEKEIAALKDKLTEAEDKIKELEASkvkel 220
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERlEALEAELDALQERREALQRLAEYswDEIDVASAEREIAELEAELERLDAS----- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 221 NHYLEAekscrtdlemyvavlntqksvLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQR 300
Cdd:COG4913 684 SDDLAA---------------------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2072346481 301 MEIVLTSEQLRQVEELKKKDQEDDEQQRLNNKRKDHKKTDAEEEAKI 347
Cdd:COG4913 743 ARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
168-456 |
2.42e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 40.80 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 168 ENLENEMKKAQEDAEKLRSvvmpmeKEIAAL-KDKLTEAEDKIKELEASKVKELNHYLEAEKSCRTDlemyvaVLNTQKS 246
Cdd:PTZ00108 1105 EKLNAELEKKEKELEKLKN------TTPKDMwLEDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGK------ASKLRKP 1172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 247 VLQEDAEKLR-KELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQRMEIVLTSEQLRQVEELKKKDQEDDE 325
Cdd:PTZ00108 1173 KLKKKEKKKKkSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSK 1252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 326 QQRLNNK-RKDHKKTDAEEEAKIPVVCALTQEESSAQLSNEEFQEHLDSTHGSVHSLDADLLLPSGDPFSKSdNDMFKDG 404
Cdd:PTZ00108 1253 SSEDNDEfSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKK-KKSEKKT 1331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2072346481 405 LRRAQSTDSLGTSGSLQSKALGYNYKAKSAGNLDESDFGPLVGADSVSENFD 456
Cdd:PTZ00108 1332 ARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSEDDDDSEVDDSEDEDDED 1383
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
59-439 |
2.67e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 59 RQNAVLQAAQDDLGHLRTQLWEAQAEMENIKAIATVSENTKQEAIDEVKRQWREEVASLQAVMK--ETVRDYEhqfhlrl 136
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKkaEDARKAE------- 1131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 137 EQERAQWAQYRESAdREIADLRRRLSEGQEEENLENEMKKAQEDAEKLRSVVMPMEKEIAalkDKLTEAEDKIKELEASK 216
Cdd:PTZ00121 1132 EARKAEDARKAEEA-RKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKA---EELRKAEDARKAEAARK 1207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 217 VKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLMR 296
Cdd:PTZ00121 1208 AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE 1287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 297 DMQRMEIVLTSEQLRQVEELKKKDQEDDEQQRLNNKRKDHKK------TDAEEEAKIPVVCALTQEESSAQLSNEEFQEH 370
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKkadaakKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2072346481 371 LDSTHGSVHSLDADLLLPSGDPFSKSDnDMFKDGLRRAQSTDSLGTSGSLQSKALGYNYKAKSAGNLDE 439
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKAD-EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADE 1435
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
35-271 |
2.87e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 35 LEQEFNQKRAKFKELylakEEDLKRQNAVLQAAQDDLG---HLRTQLWEAQAEMENIKAIATVSENTKQEAIDEVKRQwR 111
Cdd:PRK02224 211 LESELAELDEEIERY----EEQREQARETRDEADEVLEeheERREELETLEAEIEDLRETIAETEREREELAEEVRDL-R 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 112 EEVASLQAVMKETVRDYEHQfhlRLEQERAqwAQYRESADREIADLRRRLSE--------GQEEENLENEMKKAQEDAEK 183
Cdd:PRK02224 286 ERLEELEEERDDLLAEAGLD---DADAEAV--EARREELEDRDEELRDRLEEcrvaaqahNEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 184 LRSVVMPMEKEIAALKDKLTEAEDKIKELEaSKVKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAEKLRKELHEVC 263
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEIEELE-EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR 439
|
....*...
gi 2072346481 264 HLLEQERQ 271
Cdd:PRK02224 440 ERVEEAEA 447
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
13-277 |
3.05e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 13 SLQQRVAELEKinaEFLRAQQQLEQEFNQKRAKFKELYLAKEEDLKRQNAVLQAAQDDLGHLRTQLWEAQAEMENIKAIA 92
Cdd:COG4717 203 ELQQRLAELEE---ELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 93 TV---------SENTKQEAIDEVKRQWREEVASLQAVMKETVRDYEHQFHLRLEQERAQWAQYRES------ADREIADL 157
Cdd:COG4717 280 FLvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRieelqeLLREAEEL 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 158 RRRLSEGQEEENLENEMKKAQ-EDAEKLRSVVMpMEKEIAALKDKLTEAEDKIKELEASKVKELNHYLEAE-KSCRTDLE 235
Cdd:COG4717 360 EEELQLEELEQEIAALLAEAGvEDEEELRAALE-QAEEYQELKEELEELEEQLEELLGELEELLEALDEEElEEELEELE 438
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2072346481 236 MYVAVLNTQKSVLQEDAEKLRKELHEVC--HLLEQERQQHNQLK 277
Cdd:COG4717 439 EELEELEEELEELREELAELEAELEQLEedGELAELLQELEELK 482
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
93-346 |
3.53e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.11 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 93 TVSENTKQEAIDEVK----RQWREEVA-------SLQAVMKETVRDYEHQFHLRLEQERAQWAQYREsADREIADLRRRL 161
Cdd:pfam17380 283 AVSERQQQEKFEKMEqerlRQEKEEKAreverrrKLEEAEKARQAEMDRQAAIYAEQERMAMERERE-LERIRQEERKRE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 162 SEGQEEENLENEMKKAQEdaekLRSVVMPMEKEIAALKDKLtEAEDKIKELEASKVKELNHYLEAEKSCRTDLEmyvAVL 241
Cdd:pfam17380 362 LERIRQEEIAMEISRMRE----LERLQMERQQKNERVRQEL-EAARKVKILEEERQRKIQQQKVEMEQIRAEQE---EAR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 242 NTQKSVLQED----AEKLRKELHEVCHLLEQERQQHNQLKHtwQKANDQFLESQRLLMRDMQRMEIVLTSEQLRQV---E 314
Cdd:pfam17380 434 QREVRRLEEErareMERVRLEEQERQQQVERLRQQEEERKR--KKLELEKEKRDRKRAEEQRRKILEKELEERKQAmieE 511
|
250 260 270
....*....|....*....|....*....|..
gi 2072346481 315 ELKKKDQEDDEQQRLNNKRKDHKKTDAEEEAK 346
Cdd:pfam17380 512 ERKRKLLEKEMEERQKAIYEEERRREAEEERR 543
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
129-366 |
4.05e-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: 40.10 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 129 EHQFHLRLEQERAQWAQYRESADREIADLRRRLSEGQEEEN-LENEMKKAQEDAEKLRSVVM----PMEKEIAALKDKLT 203
Cdd:pfam15921 255 QNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANsIQSQLEIIQEQARNQNSMYMrqlsDLESTVSQLRSELR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 204 EA----EDKIKELEASKVKELNHYLEAekscRTDLEMYvavlNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQL--- 276
Cdd:pfam15921 335 EAkrmyEDKIEELEKQLVLANSELTEA----RTERDQF----SQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwdr 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 277 --------KHTWQKANDQFLESQRL--LMRDM----------QRMEIVLTSEQLRQVEELKKKDQEDDEQQRLNNKRKDH 336
Cdd:pfam15921 407 dtgnsitiDHLRRELDDRNMEVQRLeaLLKAMksecqgqmerQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTA 486
|
250 260 270
....*....|....*....|....*....|..
gi 2072346481 337 KKTDAE--EEAKIPVVCALTQEESSAQLSNEE 366
Cdd:pfam15921 487 KKMTLEssERTVSDLTASLQEKERAIEATNAE 518
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
20-366 |
5.22e-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: 39.95 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 20 ELEKINAEFLRAQQQLEQEFNQKRAKFKELYLAKEEDLKRQNAVLQAAQDDLGHLRTQLWEAQAEMENIKAIATVSENTK 99
Cdd:pfam02463 184 NLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 100 QEAIDEVKRQWREEvaslQAVMKETVRDYEHQFHLRLEQERAQwaqyresadreIADLRRRLSEGQEEENLENEMKKAQE 179
Cdd:pfam02463 264 EEKLAQVLKENKEE----EKEKKLQEEELKLLAKEEEELKSEL-----------LKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 180 DAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELEASKVKELNHYLEAEKSCRTDLEMyvavLNTQKSVLQEDAEKLRKEL 259
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESER----LSSAAKLKEEELELKSEEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 260 HEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLmrDMQRMEIVLTSEQLRQVEELKKKDQEDDEQQRLNNKRkdhKKT 339
Cdd:pfam02463 405 KEAQLLLELARQLEDLLKEEKKEELEILEEEEESI--ELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE---TQL 479
|
330 340
....*....|....*....|....*..
gi 2072346481 340 DAEEEAKIPVVCALTQEESSAQLSNEE 366
Cdd:pfam02463 480 VKLQEQLELLLSRQKLEERSQKESKAR 506
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
176-380 |
5.96e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 39.50 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 176 KAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIK-------------ELEASKVKELNHYLEAEKSCRTDLEMYVAVLN 242
Cdd:PLN02939 153 QALEDLEKILTEKEALQGKINILEMRLSETDARIKlaaqekihveileEQLEKLRNELLIRGATEGLCVHSLSKELDVLK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 243 TQKSVLQEDAEKLRKELHEVCH------LLEQERqqhNQLKHTWQKANDQFLESQrllmRDMQRMEIVLTSEQLRQVEEL 316
Cdd:PLN02939 233 EENMLLKDDIQFLKAELIEVAEteervfKLEKER---SLLDASLRELESKFIVAQ----EDVSKLSPLQYDCWWEKVENL 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2072346481 317 -----KKKDQEDDEQQRLNNKRKDHKKTDAEEEAkipVVCALTQEESS-----AQLSNEEFQEHLDSTHGSVHS 380
Cdd:PLN02939 306 qdlldRATNQVEKAALVLDQNQDLRDKVDKLEAS---LKEANVSKFSSykvelLQQKLKLLEERLQASDHEIHS 376
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
7-315 |
6.00e-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: 39.57 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 7 ASQPDVSLQQRVAELEKINAEFLRAQQQLEQEFNQKRAKFKelylAKEEDLKRQNAvLQAAQDDLGHLRTQ---LWEAQA 83
Cdd:TIGR00618 210 TPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE----AQEEQLKKQQL-LKQLRARIEELRAQeavLEETQE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 84 EMENIKAIATVSENtkQEAIDEVKRQWREEVASLQAVMKETVRDYEH-QFHLRLEQERAQWAQYRESADREIADLRRrls 162
Cdd:TIGR00618 285 RINRARKAAPLAAH--IKAVTQIEQQAQRIHTELQSKMRSRAKLLMKrAAHVKQQSSIEEQRRLLQTLHSQEIHIRD--- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 163 EGQEEENLENEMKKAQEDAEKLRSvvmpMEKEIAALKDKLteaedKIKELEASKVKELNHYLEAEKSCRTDLEMYVAVLN 242
Cdd:TIGR00618 360 AHEVATSIREISCQQHTLTQHIHT----LQQQKTTLTQKL-----QSLCKELDILQREQATIDTRTSAFRDLQGQLAHAK 430
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2072346481 243 TQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQRMEIVLTSEQLRQVEE 315
Cdd:TIGR00618 431 KQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEP 503
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
81-361 |
6.71e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 81 AQAEMENIKAIATVSE--NTKQEAIDEVKRQwREEVASLQAVMKETVRDYEhqfhlRLEQERAQWAQYRESADREI---- 154
Cdd:TIGR02169 152 PVERRKIIDEIAGVAEfdRKKEKALEELEEV-EENIERLDLIIDEKRQQLE-----RLRREREKAERYQALLKEKReyeg 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 155 -ADLRRRLSEGQEEENLENEMKKAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKEL---EASKVKELNHYLEAE-KS 229
Cdd:TIGR02169 226 yELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeEQLRVKEKIGELEAEiAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 230 CRT----------DLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQ-------ERQQHNQLKHTWQKANDQFLESQR 292
Cdd:TIGR02169 306 LERsiaekereleDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKlteeyaeLKEELEDLRAELEEVDKEFAETRD 385
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2072346481 293 LLMRDMQRMEIV------LTSEQLRQVEELKKKDQE-DDEQQRLNNKRKDHKKTDAEEEAKIPVVCALTQEESSAQ 361
Cdd:TIGR02169 386 ELKDYREKLEKLkreineLKRELDRLQEELQRLSEElADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
46-369 |
9.41e-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: 39.18 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 46 FKELYLAKEEDLKRQNAVLQAAQDDLGHLRTQLWEAQAEMENIKAIATVSENTKQEAIDEVKRQwREEVASLQAVMKETV 125
Cdd:pfam02463 660 EKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELL-ADRVQEAQDKINEEL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 126 RDYEHQFhLRLEQERAQWAQYRESADREIADLRRRLSEGQEEENLENEMKKAQEDAEKLRSVVMPMEKEIAALKDK--LT 203
Cdd:pfam02463 739 KLLKQKI-DEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEaeLL 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 204 EAEDKIKELEASKVKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKA 283
Cdd:pfam02463 818 EEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072346481 284 NDQFLE--SQRLLMRDMQRMEIVLTSEQLRQVEELKKKDQEDDEQQRLNNKRKDHKKTDAEEEAKIPVVCALTQEESSAQ 361
Cdd:pfam02463 898 EKKELEeeSQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNL 977
|
....*...
gi 2072346481 362 LSNEEFQE 369
Cdd:pfam02463 978 MAIEEFEE 985
|
|
| |
