|
Name |
Accession |
Description |
Interval |
E-value |
| IFT81_CH |
pfam18383 |
Intraflagellar transport 81 calponin homology domain; This is the N-terminal domain found in ... |
3-126 |
2.39e-67 |
|
Intraflagellar transport 81 calponin homology domain; This is the N-terminal domain found in IFT81 proteins. Crystal structure analysis revealed that IFT81-N adopts the fold of a calponin homology (CH) domain with structural similarity to the kinetochore complex component NDC80 with microtubule (MT)-binding properties. Functional analysis show that IFT74 and IFT81 form a tubulin-binding module required for ciliogenesis. It is suggested that IFT81-N binds the globular domain of tubulin to provide specificity, and IFT74-N recognizes the beta-tubulin tail to increase affinity.
Pssm-ID: 465736 Cd Length: 124 Bit Score: 216.35 E-value: 2.39e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 3 DQIKFIVDSLNKEPFKKNYNLITFDSLGPMQLLQVLNDVLAEIDPKQDVDIREETPEQTAKRMLSLLGILKYKPPGNATD 82
Cdd:pfam18383 1 ENLKFIVTELNKEPFNKNYNLITFDSLSPEQLLQVLNDVLAEIDPKQKVDIREESPEETAIRILEALRILKYKPPPDIDD 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1958669302 83 MSTFRQGLVIGSKPVIYPVLHWLLQRSSELKKRAYLARFLIKLE 126
Cdd:pfam18383 81 PSAFRQGLVRGEKLVIYPILYWLLSNVEELKKRAYLARFLVKVE 124
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
138-651 |
2.65e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 138 ADTNKQYEELMEAFKALHKECEQLKTSgfstaEIRRDISAMEEEKDQLMKRVERLKKRVETVQNHQRmlKIARQLRVEKE 217
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAEEAKKAD-----EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE--AAADEAEAAEE 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 218 REEFLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRHAAADAKPESLMKRLEEEIKfnsymVTEKFPKELESKKKELHFLQK 297
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK-----KADEAKKKAEEKKKADEAKKK 1439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 298 V--------VSEPAMGHSDLLELESKVNEV-NAEINQLIEKKMMRNEPIEGKLSLYRQQASIISRKKEAK--AEELQETK 366
Cdd:PTZ00121 1440 AeeakkadeAKKKAEEAKKAEEAKKKAEEAkKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKkkADEAKKAE 1519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 367 EKLASLEREVSVKTNQTREFDGTEVLKGDEFKRYVSKLRsKSTVFKKKHQIIAEFKAEFGLLQRTEELLKQRQETIQHQL 446
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK-KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVM 1598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 447 RTIEEKKGISGYSYTQEELERVSA--LKSEVDEMKG--RTLDDMSEMVKKLNSLVSEKKSALAPVIKELRQL---RQKCQ 519
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAeeLKKAEEEKKKveQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAeedKKKAE 1678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 520 ELTQECDEKRTQYDSCAAGLESNRsKLEQEVRGLREECLQEESkyhytncmIKNLEVQLRRATDEMKAYVSSDQQEKRKA 599
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAK-KAEELKKKEAEEKKKAEE--------LKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1958669302 600 IREQYTKNITEQenLGKKLREKQKAVRESHGPNMKQAKMWRDLEQLMECKKQ 651
Cdd:PTZ00121 1750 KKDEEEKKKIAH--LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
141-406 |
1.72e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 141 NKQYEELMEAFKALHKECE----QLKTSGFSTAEIRRDISAMEEEKDQLMKRVERLKKRVETVQnhqrmlkiaRQLRVEK 216
Cdd:TIGR02168 238 REELEELQEELKEAEEELEeltaELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE---------QQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 217 EREEFLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRHAAADAKPEslMKRLEEEIKfnsymVTEKFPKELESKKKElhfLQ 296
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE--LESLEAELE-----ELEAELEELESRLEE---LE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 297 KVVSEPAmghSDLLELESKVNEVNAEINQLIEKKMM--------RNEPIEGKLSLYRQQASIISRKKEAKAEELQETKEK 368
Cdd:TIGR02168 379 EQLETLR---SKVAQLELQIASLNNEIERLEARLERledrrerlQQEIEELLKKLEEAELKELQAELEELEEELEELQEE 455
|
250 260 270
....*....|....*....|....*....|....*...
gi 1958669302 369 LASLEREVSVKTNQTREFDGTEVLKGDEFKRYVSKLRS 406
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
168-382 |
2.05e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 168 TAEIRRDISAMEEEKDQLMKRVERLKKRVETVQNHQRMLKIARQLRVEKEREEFLAQQKQEQKNQLFHAVQRLQRVQNQL 247
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 248 KSMRHAAADAKPESLMKRLEEEIkfnsymvtekfpKELESKKKElhfLQKVVSEpamGHSDLLELESKVNEVNAEINQLI 327
Cdd:COG3206 250 GSGPDALPELLQSPVIQQLRAQL------------AELEAELAE---LSARYTP---NHPDVIALRAQIAALRAQLQQEA 311
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958669302 328 EKKM--MRNEpiegKLSLYRQQASIISRKKEAKAE--ELQETKEKLASLEREVSVKTNQ 382
Cdd:COG3206 312 QRILasLEAE----LEALQAREASLQAQLAQLEARlaELPELEAELRRLEREVEVAREL 366
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
186-555 |
3.50e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 186 MKRVERLKKRVETVQNHQRMLKIARQLR--VEK-EREEFLAQQKQEQKNQLFHA-----VQRLQRVQNQLKSMRHAAADA 257
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELErqLKSlERQAEKAERYKELKAELRELelallVLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 258 kpESLMKRLEEEIKfnsyMVTEKFpKELESKKKELHflqkvvsepamghSDLLELESKVNEVNAEINQLIEKKMMRNEpi 337
Cdd:TIGR02168 252 --EEELEELTAELQ----ELEEKL-EELRLEVSELE-------------EEIEELQKELYALANEISRLEQQKQILRE-- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 338 egKLSLYRQQASIISRKKEAKAEELQETKEKLASLEREVSVKTNQTREFDgtevlkgDEFKRYVSKLRSKSTVFKKKHQI 417
Cdd:TIGR02168 310 --RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE-------AELEELEAELEELESRLEELEEQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 418 IAEFKAEFGLLQRTEELLKQRQETIQHQLRTIEEKKgisgysytQEELERVSALKSEVDEMKGRTLDDMSEMVKKLNSLV 497
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRR--------ERLQQEIEELLKKLEEAELKELQAELEELEEELEEL 452
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958669302 498 SEKKSALAPVIKELRQLRQKCQELTQECDEKRTQYDSCAAGLESNRSKLEQEVRGLRE 555
Cdd:TIGR02168 453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
170-651 |
3.82e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 170 EIRRdisAMEEEKDQLMKRVERLKKRVETVQNHQRMLKIARQLRVEKEREEFLAQQKQEQKNQLFHAVQRLQRVQNQLKS 249
Cdd:PTZ00121 1216 EARK---AEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 250 --MRHAAADAKPESLMKRLEEEIKfnsymvTEKFPKELESKKKELHFLQKVVSEPAMGHsdllelESKVNEVNAEINQLi 327
Cdd:PTZ00121 1293 deAKKAEEKKKADEAKKKAEEAKK------ADEAKKKAEEAKKKADAAKKKAEEAKKAA------EAAKAEAEAAADEA- 1359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 328 EKKMMRNEPIEGKLSLYRQQASIISRKKEA--KAEELQETKEKLASLEREVSVKTNQTREFDgtEVLKGDEFKRYVSKLR 405
Cdd:PTZ00121 1360 EAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkKADEAKKKAEEDKKKADELKKAAAAKKKAD--EAKKKAEEKKKADEAK 1437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 406 SKSTVFKKKHQiiAEFKAEFGllQRTEELLKQRQETiqhqlRTIEEKKGISGYSYTQEELERvsalKSEVDEMKGRTLDD 485
Cdd:PTZ00121 1438 KKAEEAKKADE--AKKKAEEA--KKAEEAKKKAEEA-----KKADEAKKKAEEAKKADEAKK----KAEEAKKKADEAKK 1504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 486 MSEMVKKLNSLvseKKSALAPVIKELRQLRQKCQELTQECDEKRTQYDSCAAGLESNRSkleQEVRGLREECLQEESKYH 565
Cdd:PTZ00121 1505 AAEAKKKADEA---KKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKA---EEKKKAEEAKKAEEDKNM 1578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 566 YTNCMIKNLEVQLRRATDEMKAYVSSDQQEKRKAIREQYTKNITEQENLGKKLREKQKAVRESHGPNMKQAKMWRDLEQL 645
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
|
....*.
gi 1958669302 646 MECKKQ 651
Cdd:PTZ00121 1659 NKIKAA 1664
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
139-627 |
4.38e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 139 DTNKQYEELMEAFKALHKECEQLKTSGFSTAEIRRDISAMEEEKDQLMKRVERLKKRVETVQNHQRMLKiARQLRVEKER 218
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLE-KEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 219 EEFLAQQKQEQKNQlfhavQRLQRVQNQLKSMRHAAADAKP-----ESLMKRLEE-EIKFNSYMVTEKFPKELESKKKEL 292
Cdd:PRK03918 238 EEIEELEKELESLE-----GSKRKLEEKIRELEERIEELKKeieelEEKVKELKElKEKAEEYIKLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 293 HFLQKVVSEPAMGHSDLL-ELESKVNEVNaEINQLIEKKMMRNEPIEGKLSLYRQQASI--------------------- 350
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIkELEEKEERLE-ELKKKLKELEKRLEELEERHELYEEAKAKkeelerlkkrltgltpeklek 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 351 ----ISRKKEAKAEELQETKEKLASLEREVSVKTNQTREFDG------------TEVLKGDEFKRYVSKLRSKSTVFKKK 414
Cdd:PRK03918 392 eleeLEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelTEEHRKELLEEYTAELKRIEKELKEI 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 415 HQIIAEFKAEF----GLLQRTEELLKQRqeTIQHQLRTIEEKKGISGYSYTQEELERVSALKSEVDEMKGRtLDDMSEMV 490
Cdd:PRK03918 472 EEKERKLRKELreleKVLKKESELIKLK--ELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGE-IKSLKKEL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 491 KKLNSLvsekKSALAPVIKELRQLRQKCQELTQECDEKRTqydSCAAGLESNRSKLE-------------QEVRGLREEC 557
Cdd:PRK03918 549 EKLEEL----KKKLAELEKKLDELEEELAELLKELEELGF---ESVEELEERLKELEpfyneylelkdaeKELEREEKEL 621
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 558 LQEESKYHYTNCMIKNLEVQLRRATDEMKAYVSSDQQEKRKAIREQYTKNITEQENLGKKLREKQKAVRE 627
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREE 691
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
337-492 |
1.32e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 337 IEGKLSLYRQQASIIsrKKEAKAEELQETKEKLASLEREVSvktNQTREFDGTEVLKGDEFKRYVSKLRSKSTVFKKKHQ 416
Cdd:PRK12704 29 AEAKIKEAEEEAKRI--LEEAKKEAEAIKKEALLEAKEEIH---KLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 417 IIAEFKAEfglLQRTEELLKQRQETIQHQLRTIEEKkgisgYSYTQEELERVSALKSE------VDEMKGRTLDDMSEMV 490
Cdd:PRK12704 104 LLEKREEE---LEKKEKELEQKQQELEKKEEELEEL-----IEEQLQELERISGLTAEeakeilLEKVEEEARHEAAVLI 175
|
..
gi 1958669302 491 KK 492
Cdd:PRK12704 176 KE 177
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-555 |
2.73e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 263 MKRLEEEIKFNSYMVTEKfPKELESKKKELHFLQKVVSEPAmghSDLLELESKVNEVNAEINQL---IEKKMMRNEPIEG 339
Cdd:TIGR02168 679 IEELEEKIEELEEKIAEL-EKALAELRKELEELEEELEQLR---KELEELSRQISALRKDLARLeaeVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 340 KLSLYRQQASIISRKKEAKAEELQETKEKLASLEREVsvktnqtrefdgtevlkgDEFKRYVSKLRSKSTVFKKKHQiia 419
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI------------------EQLKEELKALREALDELRAELT--- 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 420 EFKAEFGLLQRTEELLKQRQETIQHQLRTIEEKKGIsgysyTQEELERVSA----LKSEVDEMKgRTLDDMSEMVKKLNS 495
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEE-----LSEDIESLAAeieeLEELIEELE-SELEALLNERASLEE 887
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 496 LVSEKKSALAPVIKELRQLRQKCQELTQECDEKRTQydscAAGLESNRSKLEQEVRGLRE 555
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEELREK----LAQLELRLEGLEVRIDNLQE 943
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
133-647 |
4.01e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 133 QDETVADTNKQYEELMEAFKALHKECEQLKtSGFSTAE-----IRRDISAMEEEKDQLMKRVERLKKRVE-TVQNHQRML 206
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELE-SRLEELEeqletLRSKVAQLELQIASLNNEIERLEARLErLEDRRERLQ 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 207 KIARQLRVEKEREEFLAQQKQ--EQKNQLFHAVQRLQRVQNQLKSMRHAAADAKPESLMKRLEEEIKFNSYMVTEKFPKE 284
Cdd:TIGR02168 421 QEIEELLKKLEEAELKELQAEleELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 285 LESKKKELHFLQKVVSEPAMGH---SDLLELESK--------------------VNEVNAEINQLIEKKMMRNEPIEGKL 341
Cdd:TIGR02168 501 LEGFSEGVKALLKNQSGLSGILgvlSELISVDEGyeaaieaalggrlqavvvenLNAAKKAIAFLKQNELGRVTFLPLDS 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 342 SLYRQ-QASIISRKKEAK-----AEELQETKEK----LASLEREVSVKTNQTrefDGTEVLKgdefkryvsKLRSKSTVF 411
Cdd:TIGR02168 581 IKGTEiQGNDREILKNIEgflgvAKDLVKFDPKlrkaLSYLLGGVLVVDDLD---NALELAK---------KLRPGYRIV 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 412 KKKHQII--------AEFKAEFGLLQRTEELLKQRQETIQHQLRTIEEKKGISGYSYTQEELERVSALKSEVDEMKGRTL 483
Cdd:TIGR02168 649 TLDGDLVrpggvitgGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI 728
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 484 DDMSEMVKKL----------NSLVSEKKSALAPVIKELRQLRQKCQELTQECDEKRTQYDSCAAGLESNRSKLEQEVRGL 553
Cdd:TIGR02168 729 SALRKDLARLeaeveqleerIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 554 REECLQEESKYHYTNCMIKNLEVQLRRATDEMKayVSSDQQEKRKAIREQYTKNITEQENLGKKLREKQKAV---RESHG 630
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLE--DLEEQIEELSEDIESLAAEIEELEELIEELESELEALlneRASLE 886
|
570
....*....|....*..
gi 1958669302 631 PNMKQAKmwRDLEQLME 647
Cdd:TIGR02168 887 EALALLR--SELEELSE 901
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
142-445 |
6.24e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.59 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 142 KQYEELMEAFKALHKEC-EQLKTSGFSTAEIRRDISAMEEEKdqlmkrverlkkrvETVQNHQRMLKIARQLRVEKEREE 220
Cdd:PRK10929 68 KQYQQVIDNFPKLSAELrQQLNNERDEPRSVPPNMSTDALEQ--------------EILQVSSQLLEKSRQAQQEQDRAR 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 221 -------FLAQQKQEQKNQLFHAVQRLQ----------RVQNQLKSMRHAAADAKPESL------------MKRLEEEIK 271
Cdd:PRK10929 134 eisdslsQLPQQQTEARRQLNEIERRLQtlgtpntplaQAQLTALQAESAALKALVDELelaqlsannrqeLARLRSELA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 272 FNSYmvtEKFPKELESKKKELHFLQKVVSEPAMGHSDLLEleskvnEVNAEINQLIEKKMMRNEPIEGKLSLYRQQASII 351
Cdd:PRK10929 214 KKRS---QQLDAYLQALRNQLNSQRQREAERALESTELLA------EQSGDLPKSIVAQFKINRELSQALNQQAQRMDLI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 352 SRKKEAKAEELQETKEKLASLeREvsvktnQTREFDGTEVLkGDEFKRYVSKLRSKStvfkkKHQIIAEFKAEFgLLQRT 431
Cdd:PRK10929 285 ASQQRQAASQTLQVRQALNTL-RE------QSQWLGVSNAL-GEALRAQVARLPEMP-----KPQQLDTEMAQL-RVQRL 350
|
330
....*....|....*..
gi 1958669302 432 --EELL-KQRQETIQHQ 445
Cdd:PRK10929 351 ryEDLLnKQPQLRQIRQ 367
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
128-644 |
1.02e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 128 PSEFLQDETVADTNKQYEELMEAFKALhkecEQLKTSGFSTAEirrdisaMEEEKDQLMKRVERLKkRVETVQNHQRMLK 207
Cdd:PTZ00121 1074 PSYKDFDFDAKEDNRADEATEEAFGKA----EEAKKTETGKAE-------EARKAEEAKKKAEDAR-KAEEARKAEDARK 1141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 208 IARQLRVEKEREEFLAQQKQE-QKNQLFHAVQRLQRVQNQLKS--MRHAAADAKPESlMKRLEEEIKFNSYMVTEKFPKE 284
Cdd:PTZ00121 1142 AEEARKAEDAKRVEIARKAEDaRKAEEARKAEDAKKAEAARKAeeVRKAEELRKAED-ARKAEAARKAEEERKAEEARKA 1220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 285 LESKKKELhfLQKVVsepamghsdllelESKVNEVNAEINQLIEKKMMRNEPIEGKLSLYRQQASIISRKKEAKAEELQE 364
Cdd:PTZ00121 1221 EDAKKAEA--VKKAE-------------EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK 1285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 365 TKEKLASLEREVSVKTNQTREF--DGTEVLKGDEFKRYVSKLRSKSTVFKKKHQiIAEFKAEFGLLQ---RTEELLKQRQ 439
Cdd:PTZ00121 1286 AEEKKKADEAKKAEEKKKADEAkkKAEEAKKADEAKKKAEEAKKKADAAKKKAE-EAKKAAEAAKAEaeaAADEAEAAEE 1364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 440 ETIQHQLRTIEEKKGISGYSYTQEELERVSALKSEVDEMKGRTLDDMSEMVKKLNSLVSEKKSALAPVIKELR---QLRQ 516
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKkkaEEAK 1444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 517 KCQELTQECDEKRTQYDSCAAGLESNRSkleQEVRGLREECLQEESKYHYTNCMIKNLEVQLRRATDEMKAYVSSDQQEK 596
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEEAKKA---DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA 1521
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1958669302 597 RKAIREQYTKNITEQENLgKKLREKQKAVRESHGPNMKQAKMWRDLEQ 644
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEA-KKAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
353-622 |
1.09e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 353 RKKEAKAEELQETKEKLASLEREVSVKTNQtREFDGTEVLKGDEFK---------RYVSKLRSKSTVFKKKHQIIAEFKA 423
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQ-LERLRREREKAERYQallkekreyEGYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 424 EFGLLQRTEELLKQRQETIQHQLRTIEE------KKGISGYSYTQEELERVSALKSEVD---EMKGRTLDDMSEMVKKLN 494
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEElnkkikDLGEEEQLRVKEKIGELEAEIASLErsiAEKERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 495 SLVSEKKSALAPVIKELRQLRQKCQELTQECDEKRTQYDSCAAGLESnrskLEQEVRGLREECLQEESKYHYTNCMIKNL 574
Cdd:TIGR02169 329 AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE----VDKEFAETRDELKDYREKLEKLKREINEL 404
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958669302 575 EVQLRRATDEMKAYVS--SDQQEKRKAIREQYTKNITEQENLGKKLREKQ 622
Cdd:TIGR02169 405 KRELDRLQEELQRLSEelADLNAAIAGIEAKINELEEEKEDKALEIKKQE 454
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
134-377 |
2.00e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 134 DETVADTNKQYEELMEAFKALHKECEQL---------KTSGFSTAEIRRDISAMEEEKDQLMKRVERLKKRVETVQNHQ- 203
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvkEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLa 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 204 RMLKIARQLRVEKEREEFLAQQKQEQKNQLFHAVQRLQRVqnqlkSMRHAAADAKPESLMKRLEeeikfnsyMVTEKFPK 283
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV-----DKEFAETRDELKDYREKLE--------KLKREINE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 284 ELESKKKELHFLQKVVSEPAMGHSDLLELESKVNEVNAEINQLIEKKmmrnEPIEGKLSLYRQQASIISRKKEAKAEELQ 363
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI----KKQEWKLEQLAADLSKYEQELYDLKEEYD 479
|
250
....*....|....
gi 1958669302 364 ETKEKLASLEREVS 377
Cdd:TIGR02169 480 RVEKELSKLQRELA 493
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
313-563 |
3.14e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 313 ESKVNEVNAEINQLIEKKmmrnEPIEGKLSLYRQQASIISRKKEAKAEELQETKEKLASLEREvsvktnqtrefdgtevl 392
Cdd:COG3883 15 DPQIQAKQKELSELQAEL----EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE----------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 393 kgdefkryvsklrskstvfkkkhqiiaefkaefglLQRTEELLKQRQETIQHQLRTIEEKKGISGY-------SYTQEEL 465
Cdd:COG3883 74 -----------------------------------IAEAEAEIEERREELGERARALYRSGGSVSYldvllgsESFSDFL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 466 ERVSALKSEVDEMKgRTLDDMSEMVKKLNslvsEKKSALAPVIKELRQLRQKCQELTQECDEKRTQYDSCAAGLESNRSK 545
Cdd:COG3883 119 DRLSALSKIADADA-DLLEELKADKAELE----AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193
|
250
....*....|....*...
gi 1958669302 546 LEQEVRGLREECLQEESK 563
Cdd:COG3883 194 AEAQLAELEAELAAAEAA 211
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
138-556 |
3.81e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 138 ADTNKQYEELMEAFKALHKECEQLKTSGFSTAEIRRDISAM-------------EEEKDQLMKRVERLKKRVETVQNHQR 204
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlqllplyqelealEAELAELPERLEELEERLEELRELEE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 205 MLKIARQ--LRVEKEREEFLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRHAAADAKPEslMKRLEEEIKfnsYMVTEKFP 282
Cdd:COG4717 164 ELEELEAelAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE--LEELEEELE---QLENELEA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 283 KELESKKKELHFLQKVVSEpamghsdLLELESKVNEVNAEINQLIEKKMMRNEPIE-GKLSLYRQQASIISRKKEAKAEE 361
Cdd:COG4717 239 AALEERLKEARLLLLIAAA-------LLALLGLGGSLLSLILTIAGVLFLVLGLLAlLFLLLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 362 LQE--TKEKLASLEREVSVKTNQTREFDGTEVLKGDEFKRYVSKLRSK------STVFKKKHQIIAEFKAE-----FGLL 428
Cdd:COG4717 312 ALEelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELeeelqlEELEQEIAALLAEAGVEdeeelRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 429 QRTEEL--LKQRQETIQHQLRTIEEKKGISGYSYTQEEL-ERVSALKSEVDEMKGRtLDDMSEMVKKLNSLVSEKKSAla 505
Cdd:COG4717 392 EQAEEYqeLKEELEELEEQLEELLGELEELLEALDEEELeEELEELEEELEELEEE-LEELREELAELEAELEQLEED-- 468
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1958669302 506 pviKELRQLRQKCQELTQECDEKRTQYDSCAAGLEsnrsKLEQEVRGLREE 556
Cdd:COG4717 469 ---GELAELLQELEELKAELRELAEEWAALKLALE----LLEEAREEYREE 512
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
133-629 |
6.33e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 133 QDETVADTNKQYEELMEAFKALHKECEQLKTSgfsTAEIRRDISAMEEEKDQLMKRVERLKKRVETVQNHQR------ML 206
Cdd:PRK02224 228 QREQARETRDEADEVLEEHEERREELETLEAE---IEDLRETIAETEREREELAEEVRDLRERLEELEEERDdllaeaGL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 207 KIARQLRVEKEREEfLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRHAAADAKPESLMKR-----LEEEIKfNSYMVTEKF 281
Cdd:PRK02224 305 DDADAEAVEARREE-LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELReeaaeLESELE-EAREAVEDR 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 282 PKELESKKKELHFLQKVVS------EPAMGHSDLL-----ELESKVNEVNAEInQLIEKKMMRNEPI--EGKLSLYRQQA 348
Cdd:PRK02224 383 REEIEELEEEIEELRERFGdapvdlGNAEDFLEELreerdELREREAELEATL-RTARERVEEAEALleAGKCPECGQPV 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 349 siisrKKEAKAEELQETKEKLASLEREVS-VKTNQ-TREFDGTEVLKGDEFKRYVSKLRSKstvfkkkhqiiaefkaefg 426
Cdd:PRK02224 462 -----EGSPHVETIEEDRERVEELEAELEdLEEEVeEVEERLERAEDLVEAEDRIERLEER------------------- 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 427 lLQRTEELLKQRQETIQHQLRTIEEKKGISGY--SYTQEELERVSALKSEVDEMKGRTLD---DMSEMVKKLNSL--VSE 499
Cdd:PRK02224 518 -REDLEELIAERRETIEEKRERAEELRERAAEleAEAEEKREAAAEAEEEAEEAREEVAElnsKLAELKERIESLerIRT 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 500 KKSALAPVIKELRQLRQKCQELTQECDEKRTQYDScaagLESNRSKLEQEVRGLREECLQEESkyhytncmiKNLEVQLR 579
Cdd:PRK02224 597 LLAAIADAEDEIERLREKREALAELNDERRERLAE----KRERKRELEAEFDEARIEEAREDK---------ERAEEYLE 663
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1958669302 580 RATDEMKayvssDQQEKRKAIREQYTKNITEQENLgKKLREKQKAVRESH 629
Cdd:PRK02224 664 QVEEKLD-----ELREERDDLQAEIGAVENELEEL-EELRERREALENRV 707
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
134-457 |
1.28e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 134 DETVADTNKQYEELMEAFKALHKECEQLKTSgfsTAEIRRDISAMEEEKDQLMKRVERLKKRVEtvqnhqrmlKIARQLR 213
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAE---LEELRLELEELELELEEAQAEEYELLAELA---------RLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 214 VEKEREEFLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRHAAADAKPESLMKRLEEEikfnsymvtekfpkELESKKKELH 293
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA--------------EAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 294 FLQkvvsepamgHSDLLELESKVNEVNAEINQLIEKKMMRNEPIEGKLSLYRQQASIISRKKEAKAEELQETKEKLASLE 373
Cdd:COG1196 372 AEL---------AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 374 REVSVKTNQTREFDGTEVLKgdefkryvSKLRSKSTVFKKKHQIIAEFKAEFGLLQRTEELLKQRQETIQHQLRTIEEKK 453
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALL--------ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
....
gi 1958669302 454 GISG 457
Cdd:COG1196 515 LLAG 518
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
134-624 |
1.92e-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: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 134 DETVADTNKQYEELMEAFKALHKECEQLKT-----SGFSTAEIRRDISAMEEEKDQLMKRVERLKKRVETVQ-----NHQ 203
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAqirgnGGDRLEQLEREIERLERELEERERRRARLEALLAALGlplpaSAE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 204 RMLKIARQLRVEKEREEFLAQQKQEQKNQLFHAVQRLQR----VQNQLKSMRHAAA--DAKPESLMKRLEEEikfnsymv 277
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRelreLEAEIASLERRKSniPARLLALRDALAEA-------- 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 278 tekfpkeLESKKKELHFLQKVVsEPAMGHSD---------------LLELESKVNEVNAEINQLiekkmmrnePIEGKLS 342
Cdd:COG4913 453 -------LGLDEAELPFVGELI-EVRPEEERwrgaiervlggfaltLLVPPEHYAAALRWVNRL---------HLRGRLV 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 343 LYRqqasIISRKKEAKAEELQEtkeklASLEREVSVKTNQ---------TREFDGTEVLKGDEFKRY---VSK---LRSK 407
Cdd:COG4913 516 YER----VRTGLPDPERPRLDP-----DSLAGKLDFKPHPfrawleaelGRRFDYVCVDSPEELRRHpraITRagqVKGN 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 408 STVFKK--KHQI-------------IAEFKAEFGLLQRTEELLKQRQETIQHQLRTIEEKkgisgysytQEELERVSALK 472
Cdd:COG4913 587 GTRHEKddRRRIrsryvlgfdnrakLAALEAELAELEEELAEAEERLEALEAELDALQER---------REALQRLAEYS 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 473 SEvdemkgrtLDDMSEMVKKLNSLVSEKKSALA--PVIKELRQLRQKCQELTQECDEKRTQydscaagLESNRSKLEQEV 550
Cdd:COG4913 658 WD--------EIDVASAEREIAELEAELERLDAssDDLAALEEQLEELEAELEELEEELDE-------LKGEIGRLEKEL 722
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958669302 551 RGLREECLQEESKYHYtncMIKNLEVQLRRATDEMKAYVSSDQQEK--RKAIREQYTKNITEQENLGKKLREKQKA 624
Cdd:COG4913 723 EQAEEELDELQDRLEA---AEDLARLELRALLEERFAAALGDAVERelRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
133-396 |
2.09e-03 |
|
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: 41.58 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 133 QDETVADTNKQYEELMEAFKALHKECEQLKTSGFstaEIRRDISAMEEEKDQLMKRVERLKKRV------------ETVQ 200
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEQLRKELE---ELSRQISALRKDLARLEAEVEQLEERIaqlskelteleaEIEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 201 NHQRMLKIARQLRVEKEREEFLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRHAAADA--KPESLMKRLEEEIKFNSYMV- 277
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLreRLESLERRIAATERRLEDLEe 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 278 -TEKFPKELESKKKELHFLQKVVSEPAMGHSDLLELESKVNEVNAEINQLIEKKMMRNEPIEGKLSLYRQQASIISRKKE 356
Cdd:TIGR02168 846 qIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1958669302 357 AKAEELQETKEKLASLEREVSVKTNQTREFDGTEVLKGDE 396
Cdd:TIGR02168 926 QLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIED 965
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
139-615 |
2.12e-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: 41.26 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 139 DTNKQYEELMEAFKALHKECE--------QLKTSGFSTAEIRRDISAMEEEKDQLMKRVERLKKRVETVQNHQRMLKIAR 210
Cdd:pfam15921 423 DRNMEVQRLEALLKAMKSECQgqmerqmaAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 211 QLRVEKERE-EFLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRHAAADAKPESLmkrleeeikfnsymvtekfpkELESKK 289
Cdd:pfam15921 503 ASLQEKERAiEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKL---------------------QMAEKD 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 290 KELHFLQKVVSepamghsDLLELESKVNEVNAEInqLIEKKMMRNEPIEGKLSLyrQQASIISRKKEAKAEELQEtkeKL 369
Cdd:pfam15921 562 KVIEILRQQIE-------NMTQLVGQHGRTAGAM--QVEKAQLEKEINDRRLEL--QEFKILKDKKDAKIRELEA---RV 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 370 ASLEREVSVKTNQTREfdgtevlkgdefkryvsKLRSKSTVFKKKHQIIAEFK---AEFGLLQRTEELLKQRQETIQHQL 446
Cdd:pfam15921 628 SDLELEKVKLVNAGSE-----------------RLRAVKDIKQERDQLLNEVKtsrNELNSLSEDYEVLKRNFRNKSEEM 690
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 447 RTIEEKKGISGYSyTQEELERVSALKSEVDEMKGRTLDDMSEMVKK----------LNSLVSEKKSALAPVIKELRQLRQ 516
Cdd:pfam15921 691 ETTTNKLKMQLKS-AQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQitakrgqidaLQSKIQFLEEAMTNANKEKHFLKE 769
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 517 KCQELTQECDEKRTQYDSCAAGLESNRSkleQEvRGLREEclqeeskyhytncmIKNLEVQLRRATDEMKAYVSSDQQEK 596
Cdd:pfam15921 770 EKNKLSQELSTVATEKNKMAGELEVLRS---QE-RRLKEK--------------VANMEVALDKASLQFAECQDIIQRQE 831
|
490 500
....*....|....*....|.
gi 1958669302 597 RKAIR--EQYTKNITEQENLG 615
Cdd:pfam15921 832 QESVRlkLQHTLDVKELQGPG 852
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
284-634 |
3.14e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 284 ELESKKKELHFLQkvvsepamghSDLLELESKVNEVNAEINQLiekkmmrnepiEGKLSLYRQQASIISRKKEAKAEELQ 363
Cdd:TIGR02169 682 RLEGLKRELSSLQ----------SELRRIENRLDELSQELSDA-----------SRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 364 ETKEKLASLEREvsvKTNQTREFDGTEVLKGDefkryvsklrskstvfkkKHQIIAEFKAEFGLLQRteELLKQRQETIQ 443
Cdd:TIGR02169 741 ELEEDLSSLEQE---IENVKSELKELEARIEE------------------LEEDLHKLEEALNDLEA--RLSHSRIPEIQ 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 444 HQLRTIEEkkgisgysYTQEELERVSALKSEVDE--MKGRTLDDMSEMVKKLNSLVSEKKSALAPVIKELRQLRQKCQEL 521
Cdd:TIGR02169 798 AELSKLEE--------EVSRIEARLREIEQKLNRltLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 522 TQECDEKRTQYDSCAAGLESNRSKLEQEVRGLREECLQEESKYHYTNCMIKNLEVQLRRATDEMKAYvssdqqEKRKAIR 601
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI------EDPKGED 943
|
330 340 350
....*....|....*....|....*....|...
gi 1958669302 602 EQYTKNITEQENLGKKLREKQKAVRESHGPNMK 634
Cdd:TIGR02169 944 EEIPEEELSLEDVQAELQRVEEEIRALEPVNML 976
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
142-374 |
3.22e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 142 KQYEELMEAFKALHKECEQLKTsgfsTAEIRRDISAMEEEKDQLMkrverlkkRVETVQNHQRMLKIARQLRVEKEREEF 221
Cdd:COG4913 232 EHFDDLERAHEALEDAREQIEL----LEPIRELAERYAAARERLA--------ELEYLRAALRLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 222 LAQQKQEQKNQLFHAVQRLQRVQNQLKSMRHAAADAKPESLmKRLEEEIKfnsymVTEKFPKELESKKKELHFLQKVVSE 301
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRL-EQLEREIE-----RLERELEERERRRARLEALLAALGL 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958669302 302 PAMGHSDllELESKVNEVNAEINQLiekkmmrnepiEGKLSLYRQQASIISRKKEAKAEELQETKEKLASLER 374
Cdd:COG4913 374 PLPASAE--EFAALRAEAAALLEAL-----------EEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
141-578 |
3.41e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 141 NKQYEELMEAFKALHKECEQLKTSGFSTAEIRRDISAMEEEKDQLMKRVERLKKRVETVQNHQRMLKIARQLRVEKER-- 218
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlk 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 219 EEFLAQQKQEQKNQLFHAVQRLQRVQNQLKSM--RHAAADAKPESLMKRLEEEIKFNSYMVTEKFPKElESKKKELhfLQ 296
Cdd:PRK03918 379 KRLTGLTPEKLEKELEELEKAKEEIEEEISKItaRIGELKKEIKELKKAIEELKKAKGKCPVCGRELT-EEHRKEL--LE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 297 KVVSEPAMGHSDLLELESKVNEVNAEINQLiEKKMMRNEPIEGKLSLYRQQASIISRKKEAKAEELQETKEKLASLEREv 376
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEK- 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 377 svktnqtrefdgtevlkgdefkryVSKLRSKSTVFKKKHQIIAEFKAEFGLLQRTEELLKQRQETIQHQLrtieEKKGIS 456
Cdd:PRK03918 534 ------------------------LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL----EELGFE 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 457 GYSYTQEELERVSALKSEVDEMKG--RTLDDMSEMVKKLNSLVSEKKSALAPVIKELRQLRQKCQELTQECDEKRTQyds 534
Cdd:PRK03918 586 SVEELEERLKELEPFYNEYLELKDaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE--- 662
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1958669302 535 caaGLESNRSKLEQEVRGLREECLQEESKYHYTNCMIKNLEVQL 578
Cdd:PRK03918 663 ---ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
424-623 |
5.35e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 424 EFGLLQRTEELLKQRQETIQHQLRTIEEKkgisgysytqeeLERVSALKSEvdemkgrtldDMSEMVKKLNSLVSEKKSA 503
Cdd:PRK04863 936 QFEQLKQDYQQAQQTQRDAKQQAFALTEV------------VQRRAHFSYE----------DAAEMLAKNSDLNEKLRQR 993
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 504 LapviKELRQLRQKCQELTQECDEKRTQYDSCAAGLESNRSKLEQEVRglreECLQEESKYHYTNCmiKNLEVQLRRATD 583
Cdd:PRK04863 994 L----EQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQ----ELKQELQDLGVPAD--SGAEERARARRD 1063
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958669302 584 EMKAYVSSdQQEKRKAIREQYTKNITEQENLGKKLREKQK 623
Cdd:PRK04863 1064 ELHARLSA-NRSRRNQLEKQLTFCEAEMDNLTKKLRKLER 1102
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
311-534 |
6.08e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 311 ELESKVNEVNAEINQLIEKKMMRNepIEGKLSLYRQQASIISRKKEAKAEELQETKEKLASLEREVSVKTNQTREFDGTE 390
Cdd:COG3206 186 ELRKELEEAEAALEEFRQKNGLVD--LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 391 VLKG--DEFKRYVSKLRSKSTVFKKKHQIIAEFKAEfglLQRTEELLKQRQETIQHQLRtieekkgisgySYTQEELERV 468
Cdd:COG3206 264 VIQQlrAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEAQRILASLE-----------AELEALQARE 329
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958669302 469 SALKSEVDEMKGRtlddmsemvkklnslvsekksalapvIKELRQLRQKCQELTQECDEKRTQYDS 534
Cdd:COG3206 330 ASLQAQLAQLEAR--------------------------LAELPELEAELRRLEREVEVARELYES 369
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
174-324 |
6.40e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 39.64 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 174 DISAMEEEKDQLMKRVERLKKRVETVQNHQ-----RMLKIARQLR------VEKEREEflaqqKQEqknqlfhavqrLQR 242
Cdd:pfam10168 576 ELQSLEEERKSLSERAEKLAEKYEEIKDKQeklmrRCKKVLQRLNsqlpvlSDAEREM-----KKE-----------LET 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 243 VQNQLKSMRHAAADAKpeslMKRLEEEIKFNSYMVTEKfPKELESKKKELHFLQKVVSEpaMGhSDLLELESKVNEVNAE 322
Cdd:pfam10168 640 INEQLKHLANAIKQAK----KKMNYQRYQIAKSQSIRK-KSSLSLSEKQRKTIKEILKQ--LG-SEIDELIKQVKDINKH 711
|
..
gi 1958669302 323 IN 324
Cdd:pfam10168 712 VG 713
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
449-629 |
6.70e-03 |
|
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: 39.65 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 449 IEEKKGISGYSY-----------TQEELERVSALKSEVDEMKgRTLDDMSEMVKKLNSLVSEKKSA-LAPVIKELRQLRQ 516
Cdd:TIGR02168 161 FEEAAGISKYKErrketerklerTRENLDRLEDILNELERQL-KSLERQAEKAERYKELKAELRELeLALLVLRLEELRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 517 KCQELTQECDEKRTQYDSCAAGLESNRSKLEQ---EVRGLREECLQEESKYHYTNCMIKNLEVQLRRATDEMKAyvSSDQ 593
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEElrlEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN--LERQ 317
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958669302 594 QEKRKAIREQYTKNITEQENLGKKLREKQKAVRESH 629
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
228-479 |
9.05e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.14 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 228 EQKNQLFHAVQRLQRVQ-NQLKSMRHAAADAKPESLMKRLEEEI-KFNSYMVTEKFPKELESKKKELHF--LQKVVSEpa 303
Cdd:PRK05771 16 SYKDEVLEALHELGVVHiEDLKEELSNERLRKLRSLLTKLSEALdKLRSYLPKLNPLREEKKKVSVKSLeeLIKDVEE-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 304 mghsDLLELESKVNEVNAEINQL------IEKKMMRNEPIEG---KLSLYRQQASIIS---RKKEAKAEELQETKEKLAS 371
Cdd:PRK05771 94 ----ELEKIEKEIKELEEEISELeneikeLEQEIERLEPWGNfdlDLSLLLGFKYVSVfvgTVPEDKLEELKLESDVENV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 372 LERE---------VSVKTNQTREFDgtEVLKGDEFKRYvsKLRSKSTVFkkkhQIIAEFKaefgllQRTEELLKQRQEtI 442
Cdd:PRK05771 170 EYIStdkgyvyvvVVVLKELSDEVE--EELKKLGFERL--ELEEEGTPS----ELIREIK------EELEEIEKERES-L 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 1958669302 443 QHQLRTIEEKkgisgysYTQEELERVSALKSEVDEMK 479
Cdd:PRK05771 235 LEELKELAKK-------YLEELLALYEYLEIELERAE 264
|
|
| COG6 |
pfam06419 |
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi ... |
142-245 |
9.89e-03 |
|
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi complex, which is composed of eight different subunits and is required for normal golgi morphology and localization.
Pssm-ID: 461904 Cd Length: 611 Bit Score: 39.13 E-value: 9.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669302 142 KQYEELMEAFKALHKECEQLKTSGfstAEIRRDISAMEEEKDQLMKRVERLKKRVETVQNHQRMLKIAR---QLrveKER 218
Cdd:pfam06419 37 KEFGPVVEQLKRIETDVEKLNNSC---DEMRKRLSAAKEDTAPLLEEASSLQEQKKKIELKQKLLDAFLdkfTL---SEE 110
|
90 100
....*....|....*....|....*...
gi 1958669302 219 EEFLAQQKQEQKNQ-LFHAVQRLQRVQN 245
Cdd:pfam06419 111 EEAALTSGEEPVNDeFFKALAKVKKIHE 138
|
|
| |
