|
Name |
Accession |
Description |
Interval |
E-value |
| TMF_TATA_bd |
pfam12325 |
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ... |
973-1087 |
2.31e-31 |
|
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.
Pssm-ID: 432481 [Multi-domain] Cd Length: 115 Bit Score: 118.80 E-value: 2.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 973 LYDAVRMGAGSSIIENLQSQLKLREGEITHLQLEIGNLEKTRSIMAEELVKLTNQNDELEEKVKEIPKLRTQLRDLDQRY 1052
Cdd:pfam12325 1 SVSTSGAGPSVQLVERLSSTIRRLEGELASLKEELARLEAQRDEARQEIVKLMKENEELKELKKELEELEKELKELEQRY 80
|
90 100 110
....*....|....*....|....*....|....*
gi 110347443 1053 NTILQMYGEKAEEAEELRLDLEDVKNMYKTQIDEL 1087
Cdd:pfam12325 81 ETTLELLGEKSEEVEELKADVEDLKEMYREQVQQL 115
|
|
| TMF_DNA_bd |
pfam12329 |
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA ... |
542-615 |
5.46e-16 |
|
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes that contains at its N-terminal section a number of leucine zippers that could potentially form coiled coil structures.. The whole proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells.
Pssm-ID: 372049 [Multi-domain] Cd Length: 74 Bit Score: 73.49 E-value: 5.46e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110347443 542 SETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKE 615
Cdd:pfam12329 1 SSLEKLLKEKDEQIAQLMEEGEKLSKKELKLNNTIKKLRAKNKELEKEIAELKKKLEKLEKELENLEERLKRAE 74
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
454-752 |
2.01e-15 |
|
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: 81.64 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 454 LNEKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKE 533
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 534 ELATRLNS-SETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLD 612
Cdd:TIGR02168 762 EIEELEERlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 613 GKEEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSEAQEA--ALSREM 690
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELrrELEELR 921
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110347443 691 KAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEIGELQQRLQE 752
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
440-740 |
4.46e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.37 E-value: 4.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 440 ALSEKEDVCKTVEFLNEKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACK 519
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 520 ERDAAKKEIKNIKEELAtrlnssetadllkEKDEQIRGLMEEGEKLSKQQlhnsniiKKLRAKDKENENMVAKLNKKVKE 599
Cdd:COG1196 310 RRRELEERLEELEEELA-------------ELEEELEELEEELEELEEEL-------EEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 600 LEEELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKanAAKDS 679
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE--ALEEA 447
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110347443 680 EAQEAALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLR 740
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
429-922 |
7.65e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.80 E-value: 7.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 429 EQCEPAESQPEALSEKEDVCKTVEFLNEKLEKREAQLLSLSKEKALLEEAFDNL--KDEMFRVKEESSSISSLKDEFTQR 506
Cdd:PTZ00121 1258 EEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAeeAKKADEAKKKAEEAKKKADAAKKK 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 507 IAEAEKKVQLACKERDAAKKEIKNIKEEL-ATRLNSSET---ADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAK 582
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEEKAeAAEKKKEEAkkkADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK 1417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 583 DKENE-NMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHR-ENIKKLNSMVERQE--KDLGRLQVDMDELEEKNRSIQA 658
Cdd:PTZ00121 1418 KKADEaKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKaEEAKKKAEEAKKADeaKKKAEEAKKADEAKKKAEEAKK 1497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 659 ALDSAYKELTDLHKANAAKDSE----AQEAALSREMKAKEELSAALEKAQEEARQQQEtlaiqvgDLRLALQRTEQAAAR 734
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKKAEeakkADEAKKAEEAKKADEAKKAEEKKKADELKKAE-------ELKKAEEKKKAEEAK 1570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 735 KEDYLRHEIGELQQRLQEAENRNQELSQSVSSTTRPL----LRQIEnlQATLGSQTSSWEKLEKNLSDRLGESQTLLAAA 810
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMkaeeAKKAE--EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 811 VERERAATEELLANKIQMSSMESQNSLlRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEYVRTLEETRKEKTL 890
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKKAEEDKK-KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
490 500 510
....*....|....*....|....*....|..
gi 110347443 891 LNSQLEMERMKVEQERKKAiftQETIKEKERK 922
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKA---EEAKKDEEEK 1756
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
462-801 |
8.88e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.21 E-value: 8.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 462 EAQLLSLSKEKALLEEaFDNLKDEMFRVKEESSSISslKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEELAT-RLN 540
Cdd:COG1196 199 ERQLEPLERQAEKAER-YRELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEElRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 541 SSETADLLKEKDEQIRGLMEEGEKLSKQQLHNsniikKLRAKDKENENmvaklnkkvKELEEELQHLKQVLDGKEEVEKQ 620
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARL-----EERRRELEERL---------EELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 621 HRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELtdLHKANAAKDSEAQEAALSREMKAKEELSAAL 700
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL--LEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 701 EKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEIGELQQRLQEAENRNQELSQSVSS--TTRPLLRQIENL 778
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEElaEAAARLLLLLEA 499
|
330 340
....*....|....*....|...
gi 110347443 779 QATLGSQTSSWEKLEKNLSDRLG 801
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGL 522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
439-909 |
2.45e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 439 EALSEKEDVCKTVEFLNEKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLAC 518
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 519 KERDAAKKEIKNIKEELATRLNS-SETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKV 597
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAaAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 598 KELEEELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSA-----YKELTDLHK 672
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAglrglAGAVAVLIG 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 673 ANAAKDSEAQEAALSREMKAKEELSAALEKAQEEARQQQETLA--IQVGDLRLALQRTEQAAARKEDYLRHEIGELQQRL 750
Cdd:COG1196 532 VEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtfLPLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 751 QEAENRNQELSQSVSSTTRPLL---RQIENLQATLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQ 827
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEaalRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 828 MSSMESQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEYVRTLEETRKEkTLLNSQLEMERMKVEQERK 907
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE-ALEELPEPPDLEELERELE 770
|
..
gi 110347443 908 KA 909
Cdd:COG1196 771 RL 772
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
510-806 |
6.64e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 6.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 510 AEKKVQLACKERDAAKKEI-KNIKEELATRLnssetADLLKEKDEQIRglmEEGEKLSKQQLHNSNIIKKLRAKDKENEN 588
Cdd:COG1196 196 GELERQLEPLERQAEKAERyRELKEELKELE-----AELLLLKLRELE---AELEELEAELEELEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 589 MVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELT 668
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 669 DLHK-----ANAAKDSEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEI 743
Cdd:COG1196 348 EAEEeleeaEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110347443 744 GELQQRLQEAENRNQELSQSVSSTTRpLLRQIENLQATLGSQTSSWEKLEKNLSDRLGESQTL 806
Cdd:COG1196 428 EALAELEEEEEEEEEALEEAAEEEAE-LEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
452-1087 |
2.23e-12 |
|
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: 71.63 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 452 EFLNEKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNI 531
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 532 KEELATRLNSS-ETADLLKEKDEQIRGLMEEgeklskqqlhnsniIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQV 610
Cdd:TIGR02168 322 EAQLEELESKLdELAEELAELEEKLEELKEE--------------LESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 611 LDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSEAQEAALSREM 690
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 691 KAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDylRHEIGELQQRLQEAENRNQELSQSVS----- 765
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN--QSGLSGILGVLSELISVDEGYEAAIEaalgg 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 766 ------------------------------------------STTRPLLRQIENLQATLGSQTSSWEKLEKNLSDRLG-- 801
Cdd:TIGR02168 546 rlqavvvenlnaakkaiaflkqnelgrvtflpldsikgteiqGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGgv 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 802 -------ESQTLLAAAVERERAATEE-LLANK---IQMSSMESQNSLL--RQENSRFQAQLESEKNRLCKLEDENNRYQV 868
Cdd:TIGR02168 626 lvvddldNALELAKKLRPGYRIVTLDgDLVRPggvITGGSAKTNSSILerRREIEELEEKIEELEEKIAELEKALAELRK 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 869 ELENLKDEYV---RTLEETRKEKTLLNSQLEMERMKVEQERKKAIFTQETIKEKERKPFSVSSTPTMSRSSSISGVD--- 942
Cdd:TIGR02168 706 ELEELEEELEqlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAeie 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 943 -----MAGLQTSFLSQDESHD-----HSFGPMPISANGSNLYDAV-RMGAGSSIIENLQSQLKLREGEITHLQLEIGNLE 1011
Cdd:TIGR02168 786 eleaqIEQLKEELKALREALDelraeLTLLNEEAANLRERLESLErRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 1012 KTRSIMAEELVKLTN---------------------QNDELEEKVKEI----PKLRTQLRDLDQRYNTILQMYGEKAEE- 1065
Cdd:TIGR02168 866 ELIEELESELEALLNerasleealallrseleelseELRELESKRSELrrelEELREKLAQLELRLEGLEVRIDNLQERl 945
|
730 740
....*....|....*....|..
gi 110347443 1066 AEELRLDLEDVKNMYKTQIDEL 1087
Cdd:TIGR02168 946 SEEYSLTLEEAEALENKIEDDE 967
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
439-1087 |
2.39e-12 |
|
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: 71.63 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 439 EALSEKEDVCKTVEFLNEKLEKREAQLLSLSKEKALLEEAFDNLKDEMFrvkeesssisslkdEFTQRIAEAEKKVQLAC 518
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY--------------ALANEISRLEQQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 519 KERDAAKKEIKNIKEELATRLNSS-ETADLLKEKDEQIRGLMEEgeklskqqlhnsniIKKLRAKDKENENMVAKLNKKV 597
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLdELAEELAELEEKLEELKEE--------------LESLEAELEELEAELEELESRL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 598 KELEEELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAK 677
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 678 DSEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDylRHEIGELQQRLQEAENRN 757
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN--QSGLSGILGVLSELISVD 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 758 QELSQSVS-----------------------------------------------STTRPLLRQIENLQATLGSQTSSWE 790
Cdd:TIGR02168 533 EGYEAAIEaalggrlqavvvenlnaakkaiaflkqnelgrvtflpldsikgteiqGNDREILKNIEGFLGVAKDLVKFDP 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 791 KLEKNLSDRLG---------ESQTLLAAAVERERAATEE-LLANK---IQMSSMESQNSLL--RQENSRFQAQLESEKNR 855
Cdd:TIGR02168 613 KLRKALSYLLGgvlvvddldNALELAKKLRPGYRIVTLDgDLVRPggvITGGSAKTNSSILerRREIEELEEKIEELEEK 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 856 LCKLEDENNRYQVELENLKDEYV---RTLEETRKEKTLLNSQLEMERMKVEQERKKAIFTQETIKEKERKPFSVSSTPTM 932
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEqlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 933 SRSSSISGVD--------MAGLQTSFLSQDESHD-----HSFGPMPISANGSNLYDAV-RMGAGSSIIENLQSQLKLREG 998
Cdd:TIGR02168 773 AEEELAEAEAeieeleaqIEQLKEELKALREALDelraeLTLLNEEAANLRERLESLErRIAATERRLEDLEEQIEELSE 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 999 EITHLQLEIGNLEKTRSIMAEELVKLTNQNDELEEKVKEI----PKLRTQLRDLDQRYNTILQMYGEKAEEAEELRLDLE 1074
Cdd:TIGR02168 853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLrselEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
|
730
....*....|...
gi 110347443 1075 DVKNMYKTQIDEL 1087
Cdd:TIGR02168 933 GLEVRIDNLQERL 945
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
590-922 |
4.31e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 4.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 590 VAKLNKKVKELEEEL----QHLKQVLDGKEEVEKQhrenIKKLnsmvERQEKDLGRLQVDMDELEEKnrsiQAALDSAYK 665
Cdd:COG1196 167 ISKYKERKEEAERKLeateENLERLEDILGELERQ----LEPL----ERQAEKAERYRELKEELKEL----EAELLLLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 666 ELTDLHKANAAKDSEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAaRKEDYLRHEIGE 745
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE-QDIARLEERRRE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 746 LQQRLQEAENRNQELSQSVSSttrpLLRQIENLQATLGSQTSSWEKLEKNLSdrlgESQTLLAAAVERERAATEELLANK 825
Cdd:COG1196 314 LEERLEELEEELAELEEELEE----LEEELEELEEELEEAEEELEEAEAELA----EAEEALLEAEAELAEAEEELEELA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 826 IQMSSMESQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQ---VELENLKDEYVRTLEETRKEKTLLNSQLEMERMKV 902
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEealAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
330 340
....*....|....*....|
gi 110347443 903 EQERKKAIFTQETIKEKERK 922
Cdd:COG1196 466 AELLEEAALLEAALAELLEE 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
584-896 |
1.21e-11 |
|
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: 69.32 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 584 KENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALdsa 663
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL--- 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 664 yKELTDLHKANAAKDSEAQEAALSREMKaKEELSAALEKAQEEARQQQETLAIQVGDLRLaLQRTEQAAARKEDYLRHEI 743
Cdd:TIGR02168 757 -TELEAEIEELEERLEEAEEELAEAEAE-IEELEAQIEQLKEELKALREALDELRAELTL-LNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 744 GELQQRLQEAENRNQELSQsvssttrpllrQIENLQATLGSQTSSWEKLEKNL---SDRLGESQTLLAAAVERERAATEE 820
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSE-----------DIESLAAEIEELEELIEELESELealLNERASLEEALALLRSELEELSEE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 821 LLANKIQMSSMESQNSLLRQENSRFQAQLESEKNRLCKLEDE-NNRYQVELENLKDEYVRT---LEETRKEKTLLNSQLE 896
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIeddEEEARRRLKRLENKIK 982
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
368-922 |
1.71e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 368 KTVESAEGKSEEVNETLVIPTEEAEMEESGRSATPVNCEQ---PDILVSSTPINEGQTV--------LDKVAEQCEPAES 436
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEarkADELKKAEEKKKADEAkkaeekkkADEAKKKAEEAKK 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 437 QPEALSEKEDVCKTVEFLNEKLEKReaqllslsKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQL 516
Cdd:PTZ00121 1317 ADEAKKKAEEAKKKADAAKKKAEEA--------KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 517 ACKERDAAKK---EIKNIKEELATRLNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKL 593
Cdd:PTZ00121 1389 EKKKADEAKKkaeEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 594 NKKVKELEEELQHLKQVLDGK---EEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDEL---EEKNRSIQAALDSAYKEL 667
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKkkaEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAkkaEEAKKADEAKKAEEKKKA 1548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 668 TDLHKANAAKDSEAQEAAlSREMKAKEELSAALEKAqEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEIGELQ 747
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKA-EEAKKAEEDKNMALRKA-EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 748 QRLQEAENRNQELSQSVSSTTRP-LLRQIENLQATLGSQTSSWEKLEKNLSDRLGESqtllaaavereraatEELLANKI 826
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAeELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA---------------EEDEKKAA 1691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 827 QMSSMESQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEYVRTLEETRKE----KTLLNSQLEMERMKV 902
Cdd:PTZ00121 1692 EALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDeeekKKIAHLKKEEEKKAE 1771
|
570 580
....*....|....*....|
gi 110347443 903 EQERKKAIFTQETIKEKERK 922
Cdd:PTZ00121 1772 EIRKEKEAVIEEELDEEDEK 1791
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
458-928 |
2.38e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.17 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 458 LEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVqlacKERDAAKKEIKNIKEELAT 537
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 538 RLNSSETAD-LLKEKDEQIRGLMEEGEKLSKQQLHnsniIKKLRAKDKENEnmvaKLNKKVKELEEELQHLKQVLDGKEE 616
Cdd:PRK03918 250 LEGSKRKLEeKIRELEERIEELKKEIEELEEKVKE----LKELKEKAEEYI----KLSEFYEEYLDELREIEKRLSRLEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 617 VEKQHRENIKKLNSMVERQEKDLGR---LQVDMDELEEKNRSIQAALdSAYKELTDLHKANAAKDSEAQEAALSREMKAK 693
Cdd:PRK03918 322 EINGIEERIKELEEKEERLEELKKKlkeLEKRLEELEERHELYEEAK-AKKEELERLKKRLTGLTPEKLEKELEELEKAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 694 EELSAALEKAQEEARQqqetLAIQVGDLRLALQRTEQAAAR------------KEDYLRH---EIGELQQRLQEAENRNQ 758
Cdd:PRK03918 401 EEIEEEISKITARIGE----LKKEIKELKKAIEELKKAKGKcpvcgrelteehRKELLEEytaELKRIEKELKEIEEKER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 759 EL------------SQSVSSTTRPLLRQIENLQATLGS--------QTSSWEKLEKNLSDRLGESQTLLAAAVERERAAT 818
Cdd:PRK03918 477 KLrkelrelekvlkKESELIKLKELAEQLKELEEKLKKynleelekKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 819 EELLANKIQMSSMESQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYqVELENLKDEYVRTLEETRKEKTLLNSQLEM- 897
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEY-LELKDAEKELEREEKELKKLEEELDKAFEEl 635
|
490 500 510
....*....|....*....|....*....|....*...
gi 110347443 898 -------ERMKVEQERKKAIFTQETIKEKERKPFSVSS 928
Cdd:PRK03918 636 aetekrlEELRKELEELEKKYSEEEYEELREEYLELSR 673
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
507-806 |
4.09e-11 |
|
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: 67.39 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 507 IAEAEKKVQLACKERDAAKK--EIKNIKEELATRLnsseTADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDK 584
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERykELKAELRELELAL----LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 585 ENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAY 664
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 665 KELTDLHKANAAKdsEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARkedyLRHEIG 744
Cdd:TIGR02168 351 EELESLEAELEEL--EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER----LQQEIE 424
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110347443 745 ELQQRLQEAEnrNQELSQSVSSTTRPLLRQI---ENLQATLGSQTSSWEKLEKNLSDRLGESQTL 806
Cdd:TIGR02168 425 ELLKKLEEAE--LKELQAELEELEEELEELQeelERLEEALEELREELEEAEQALDAAERELAQL 487
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
417-764 |
6.34e-11 |
|
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: 67.02 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 417 INEGQTVLDKVAEQCEPAESQPEALSEKEDVcKTVEFLNEKlEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSI 496
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERYQALLKEKREY-EGYELLKEK-EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 497 SSLKDEFTQRIAEaekkvqLACKERDAAKKEIKNIKEELA-TRLNSSETADLLKEKDEQIRGLMEEgekLSKQQLHNSNI 575
Cdd:TIGR02169 271 EQLLEELNKKIKD------LGEEEQLRVKEKIGELEAEIAsLERSIAEKERELEDAEERLAKLEAE---IDKLLAEIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 576 IKKLRAKDKEnenmVAKLNKKVKELEEELQHLKQVLdgkEEVEKQHRENIKKLNSMVERQEKdlgrLQVDMDELEEKNRS 655
Cdd:TIGR02169 342 EREIEEERKR----RDKLTEEYAELKEELEDLRAEL---EEVDKEFAETRDELKDYREKLEK----LKREINELKRELDR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 656 IQAALDSAYKELTDLHkaNAAKDSEAQEAALSREMKAKEElsaalekAQEEARQQQETLAIQVGDLRLALQRTEQAAARK 735
Cdd:TIGR02169 411 LQEELQRLSEELADLN--AAIAGIEAKINELEEEKEDKAL-------EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
330 340
....*....|....*....|....*....
gi 110347443 736 EDylrhEIGELQQRLQEAENRNQELSQSV 764
Cdd:TIGR02169 482 EK----ELSKLQRELAEAEAQARASEERV 506
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
428-922 |
2.40e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.16 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 428 AEQCEPAESQPEALSEK--EDVCKTVEFLNEKLEKREAQLLSLSKEKALLEEAfdnlkdemfRVKEESSSISSLKDEfTQ 505
Cdd:PTZ00121 1208 AEEERKAEEARKAEDAKkaEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEA---------RMAHFARRQAAIKAE-EA 1277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 506 RIAEAEKKVQLACKERDAAKKEIKNIKEELATRLNSSETADLLKEKDEQIRGLMEEGEKLSKQQlHNSNIIKKLRAKDKE 585
Cdd:PTZ00121 1278 RKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA-KKAAEAAKAEAEAAA 1356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 586 NENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQVD---MDELEEKNRSIQAAlDS 662
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAkkkADEAKKKAEEKKKA-DE 1435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 663 AYKELTDLHKANAAKdSEAQEAALSREMKAKEE---LSAALEKAQEEARQQQEtlaiqvgdlrlaLQRTEQAAARKEDYL 739
Cdd:PTZ00121 1436 AKKKAEEAKKADEAK-KKAEEAKKAEEAKKKAEeakKADEAKKKAEEAKKADE------------AKKKAEEAKKKADEA 1502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 740 RHEIGELQQ----RLQEAENRNQELSQSVSSTTRPLLRQIENLQAtlGSQTSSWEKLEKNLSDRLGESQTLLAAAVERER 815
Cdd:PTZ00121 1503 KKAAEAKKKadeaKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK--ADELKKAEELKKAEEKKKAEEAKKAEEDKNMAL 1580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 816 AATEEllANKIQMSSMESQNSLLRQENSRFQAQLESEKNRLCKLE-----DENNRYQVELENLKDEYVRTLEETRKEKTL 890
Cdd:PTZ00121 1581 RKAEE--AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEelkkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
|
490 500 510
....*....|....*....|....*....|..
gi 110347443 891 LNSQLEMERMKVEQERKKAiftQETIKEKERK 922
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKA---EEAKKAEEDE 1687
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
673-909 |
2.92e-10 |
|
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: 63.63 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 673 ANAAKDSEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDylrhEIGELQQRLQE 752
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA----ELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 753 AENRNQELSQSVSSTTRPLLRQIENLQATLGSQTSSWEKLEKNLsdrlgesqTLLAAAVERERAATEELLANKIQMSSME 832
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL--------QYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110347443 833 SQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEYVRTLEETRKEKTLLNSQLEMERMKVEQERKKA 909
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
578-922 |
4.27e-10 |
|
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: 64.32 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 578 KLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQvdmdELEEKNRSIQ 657
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE----ELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 658 AALDSAYKELTDLhkanaAKDSEAQEAALSREMKAKEELSAAL-----EKAQEEARQQQETLAIQVGDLRlALQRTEQAA 732
Cdd:TIGR02169 751 QEIENVKSELKEL-----EARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLR-EIEQKLNRL 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 733 ARKEDYLRHEIGELQQRLQEAENRNQELSQsvssttrpllrQIENLQATLGSQTSSWEKLEKNLSDRLGEsqtlLAAAVE 812
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEK-----------EIENLNGKKEELEEELEELEAALRDLESR----LGDLKK 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 813 RERAATEELLANKIQMSSMESQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEyvRTLEETRKEKTLLN 892
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL--EDVQAELQRVEEEI 967
|
330 340 350
....*....|....*....|....*....|
gi 110347443 893 SQLEMERMKVEQERKKAIFTQETIKEKERK 922
Cdd:TIGR02169 968 RALEPVNMLAIQEYEEVLKRLDELKEKRAK 997
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
439-922 |
4.48e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 439 EALSEKEDVCKTVEFLNEKLEKREAQLLSLSKEKAL---LEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQ 515
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 516 LAcKERDAAKKEIKNIKEELATRLNSSETADLLKEKDEQIRGLM--EEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKL 593
Cdd:PRK03918 339 RL-EELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLtgLTPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 594 NKKVKELEEELQHLKQVLDG----KEEVEKQHRENIKklnsmvERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTD 669
Cdd:PRK03918 418 KKEIKELKKAIEELKKAKGKcpvcGRELTEEHRKELL------EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 670 LHKANAAKDSEAQEAALSREMKA--KEELsaalEKAQEEARQQQETLAIQVGDLRLALQRTEQAAA--RKEDYLRHEIGE 745
Cdd:PRK03918 492 ESELIKLKELAEQLKELEEKLKKynLEEL----EKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkKKLAELEKKLDE 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 746 LQQRLQEAENRNQELSQSvssttrpllrQIENLQATLGSQTSSWEKL--EKNLSDRLGESQTLLAAAVERERAATEELLA 823
Cdd:PRK03918 568 LEEELAELLKELEELGFE----------SVEELEERLKELEPFYNEYleLKDAEKELEREEKELKKLEEELDKAFEELAE 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 824 NKIQMSSMESQNSLLRQENSrfQAQLESEKNRLCKLEDENNRYQVELENLK---DEYVRTLEETRKEKTllnsqlEMERM 900
Cdd:PRK03918 638 TEKRLEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEkrrEEIKKTLEKLKEELE------EREKA 709
|
490 500
....*....|....*....|...
gi 110347443 901 KVEQER-KKAIFTQETIKEKERK 922
Cdd:PRK03918 710 KKELEKlEKALERVEELREKVKK 732
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
526-1087 |
5.50e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.50 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 526 KEIKNIKEELATRLNSSETAD-LLKEKDEQIRGLMEEGEKLSKQqlhnsniIKKLRAKDKENENMVAKLNKKVKELEEEL 604
Cdd:TIGR04523 40 KKLKTIKNELKNKEKELKNLDkNLNKDEEKINNSNNKIKILEQQ-------IKDLNDKLKKNKDKINKLNSDLSKINSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 605 QHLKQVLDGKE----EVEKQHREN---IKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANA-A 676
Cdd:TIGR04523 113 KNDKEQKNKLEvelnKLEKQKKENkknIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDkI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 677 KDSEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEIGELQQRLQEAENR 756
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 757 NQELSQSVS--STTRPLLRQIENLQATLGSQTSswEKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSMESQ 834
Cdd:TIGR04523 273 QKELEQNNKkiKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 835 NSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEyVRTLEETRKEKTLLNSQLEMERMKVEQERKKaiftqe 914
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ-INDLESKIQNQEKLNQQKDEQIKKLQQEKEL------ 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 915 tiKEKERKPFSVSSTPTMSRSSSISGVDmaglqTSFLSQDESHDhsfgpmpisangsnlydavrmgagsSIIENLQSQLK 994
Cdd:TIGR04523 424 --LEKEIERLKETIIKNNSEIKDLTNQD-----SVKELIIKNLD-------------------------NTRESLETQLK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 995 LREGEITHLQLEIGNLEKTRSIMAEELVKLTNQNDELEEKVK----EIPKLRTQLRDLDQRYNTILQMYGEKAEEAEELR 1070
Cdd:TIGR04523 472 VLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKdltkKISSLKEKIEKLESEKKEKESKISDLEDELNKDD 551
|
570
....*....|....*..
gi 110347443 1071 LDLEdvKNMYKTQIDEL 1087
Cdd:TIGR04523 552 FELK--KENLEKEIDEK 566
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
545-922 |
9.67e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 9.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 545 ADLLKEKDEQIRGLMEEGEKlskqqlhnsniIKKLRAKDKENEnmvaklnkkvKELEEELQHLKQVLDGKEEVEKQhren 624
Cdd:TIGR02168 147 SEIIEAKPEERRAIFEEAAG-----------ISKYKERRKETE----------RKLERTRENLDRLEDILNELERQ---- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 625 IKKLnsmvERQEKDLGRLQVDMDELEEKNRSIQAA-LDSAYKELTDLhkANAAKDSEAQEAALSREMKAKEELSAALEKA 703
Cdd:TIGR02168 202 LKSL----ERQAEKAERYKELKAELRELELALLVLrLEELREELEEL--QEELKEAEEELEELTAELQELEEKLEELRLE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 704 QEEARQQQETLAIQVGDLRLALQRTE---QAAARKEDYLRHEIGELQQRLQEAENRNQELSQSVSStTRPLLRQIENLQA 780
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRLEqqkQILRERLANLERQLEELEAQLEELESKLDELAEELAE-LEEKLEELKEELE 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 781 TLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSMESQNSLLRQENSRFQAQLESEKNRLckle 860
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL---- 430
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110347443 861 dennryqveLENLKDEYVRTLEETRKEKTLLNSQLEMERMKVEQERKKAIFTQETIKEKERK 922
Cdd:TIGR02168 431 ---------EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
454-918 |
2.65e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.19 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 454 LNEKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKE 533
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKS 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 534 ELATrLNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDG 613
Cdd:TIGR04523 296 EISD-LNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 614 KEEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSEAQEaaLSREMKAK 693
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD--LTNQDSVK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 694 EELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDylrhEIGELQQRLQEAENRNQELSQSVSSttrpLLR 773
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEK----ELKKLNEEKKELEEKVKDLTKKISS----LKE 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 774 QIENLQAtlgsqtsswEKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSMESQNSLLRQENSRFQ---AQLE 850
Cdd:TIGR04523 525 KIEKLES---------EKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQeliDQKE 595
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110347443 851 SEKNRLCKledENNRYQVELENLKDEyvrtLEETRKEKTLLNSQLEMERMKVEQERKKAIFTQETIKE 918
Cdd:TIGR04523 596 KEKKDLIK---EIEEKEKKISSLEKE----LEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKE 656
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
454-687 |
3.72e-09 |
|
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: 60.16 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 454 LNEKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKE 533
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 534 ELATRL-----NSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKEnenmvakLNKKVKELEEELQHLK 608
Cdd:COG4942 105 ELAELLralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-------LAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110347443 609 QVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSEAQEAALS 687
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
439-800 |
6.93e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.05 E-value: 6.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 439 EALSEKEDVCKTVEFLNEKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLAC 518
Cdd:PRK02224 360 ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 519 KERDAAKKEIKNIK-EELATRLNSSETADLLKEKDEQIRGLMEEGEKLSKQQlhnsniikklrakdkenENMVAKLN--K 595
Cdd:PRK02224 440 ERVEEAEALLEAGKcPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEV-----------------EEVEERLEraE 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 596 KVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANA 675
Cdd:PRK02224 503 DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 676 AKDSEAQEAALSREMKAK-EELSAALEKAQEEARQQQEtlaiqvgdlrLALQRTEQAAARKE--DYLRHEIGElqQRLQE 752
Cdd:PRK02224 583 ELKERIESLERIRTLLAAiADAEDEIERLREKREALAE----------LNDERRERLAEKRErkRELEAEFDE--ARIEE 650
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 110347443 753 AENRNQELSQ---SVSSTTRPLLRQIENLQATLGSQTSSWEKLEkNLSDRL 800
Cdd:PRK02224 651 AREDKERAEEyleQVEEKLDELREERDDLQAEIGAVENELEELE-ELRERR 700
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
474-1067 |
1.14e-08 |
|
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: 59.36 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 474 LLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDA-------AKKEIKNIKEELATRLNSSETAD 546
Cdd:pfam15921 79 VLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAmadirrrESQSQEDLRNQLQNTVHELEAAK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 547 LLKEkdEQIRGLMEEGEKLSKQQLHNSNIIKKLRA-----------KDKENENMV--------AKLNKKVKELEEELQHL 607
Cdd:pfam15921 159 CLKE--DMLEDSNTQIEQLRKMMLSHEGVLQEIRSilvdfeeasgkKIYEHDSMStmhfrslgSAISKILRELDTEISYL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 608 K-QVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRL----QVDMDELEEKNRSIQAALDSAYKELTDLHkanaaKDSEAQ 682
Cdd:pfam15921 237 KgRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLisehEVEITGLTEKASSARSQANSIQSQLEIIQ-----EQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 683 EAALSREMKAKEELSAALEKAQEEARQQQETlAIQVGDLRLALQRTEQAAARKE-DYLRHEIG----ELQQRLQEAENRN 757
Cdd:pfam15921 312 NSMYMRQLSDLESTVSQLRSELREAKRMYED-KIEELEKQLVLANSELTEARTErDQFSQESGnlddQLQKLLADLHKRE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 758 QELSQSVSSTTRPLLRQIENlqatlgsqTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELlanKIQMSSMESQNSL 837
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGN--------SITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQM---ERQMAAIQGKNES 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 838 LRQENSrFQAQLESEKNRLCKLEDENNRYQVELENLK----------DEYVRTLEETRKEKTLLNSQLEMERMKVEQERK 907
Cdd:pfam15921 460 LEKVSS-LTAQLESTKEMLRKVVEELTAKKMTLESSErtvsdltaslQEKERAIEATNAEITKLRSRVDLKLQELQHLKN 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 908 KAIFTQETIKEKERKPFSVSSTPTMsrsssisgVDMAGLQTSFLSQ-DESHDHSFGPMPIS-ANGSNLYDAVRMGAGSSI 985
Cdd:pfam15921 539 EGDHLRNVQTECEALKLQMAEKDKV--------IEILRQQIENMTQlVGQHGRTAGAMQVEkAQLEKEINDRRLELQEFK 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 986 IENLQSQLKLREGEITHLQLEignLEKTRSIMA--EELVKLTNQNDELEEKVKEIPKLRTQLRDLDQRYNTILQMYGEKA 1063
Cdd:pfam15921 611 ILKDKKDAKIRELEARVSDLE---LEKVKLVNAgsERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKS 687
|
....
gi 110347443 1064 EEAE 1067
Cdd:pfam15921 688 EEME 691
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
553-766 |
2.07e-08 |
|
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: 57.47 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 553 EQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSMV 632
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 633 ERQEKDLGRLQVDMDELEEKNRSI----QAALDSAYKELTDLHKANAAKDSEAQEaalsreMKAKEELSAALEKAQEEAR 708
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEE------LRADLAELAALRAELEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 110347443 709 QQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEIGELQQRLQEAENRNQELSQSVSS 766
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
438-1090 |
3.11e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.93 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 438 PEALSEKEDVcKTVEFLNEKLEKREAQLLSLSKEKALLEEAFDNLKDEM-FRVKEESSSISSLKDEFTQRIAEAEKKVQL 516
Cdd:pfam12128 241 PEFTKLQQEF-NTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELnQLLRTLDDQWKEKRDELNGELSAADAAVAK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 517 ACKERDAAKKEIKNIKEELAtrlnssETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKklRAKDKENENMVAKLNKK 596
Cdd:pfam12128 320 DRSELEALEDQHGAFLDADI------ETAAADQEQLPSWQSELENLEERLKALTGKHQDVT--AKYNRRRSKIKEQNNRD 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 597 VKELEEELQHLKqvldgkEEVEKQHREnikkLNSMVERQEKDLgrlqvdMDELEEKNRSIQaalDSAYKELTDLHKANAA 676
Cdd:pfam12128 392 IAGIKDKLAKIR------EARDRQLAV----AEDDLQALESEL------REQLEAGKLEFN---EEEYRLKSRLGELKLR 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 677 KDSEAQEAALSREMKAKEELSAALEKAQEEARQQQEtlaiqvgdlrlALQRTEQAAARKEDYLRHEIGELQQRLQEAENR 756
Cdd:pfam12128 453 LNQATATPELLLQLENFDERIERAREEQEAANAEVE-----------RLQSELRQARKRRDQASEALRQASRRLEERQSA 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 757 NQELSQSVSSTTRPLLrqienlqATLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAATE------ELLANKIQMSS 830
Cdd:pfam12128 522 LDELELQLFPQAGTLL-------HFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGElnlygvKLDLKRIDVPE 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 831 MESQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKdeyvrtLEETRKEKTLLNSQLEMERMKVEQERKKAI 910
Cdd:pfam12128 595 WAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKAS------REETFARTALKNARLDLRRLFDEKQSEKDK 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 911 FTQETikeKERKPFSVSSTPTMSRSSSISGVDMAGLQTSFlsQDESHDHSfgpMPISANGSNLYDA--VRMGAGSSIIEN 988
Cdd:pfam12128 669 KNKAL---AERKDSANERLNSLEAQLKQLDKKHQAWLEEQ--KEQKREAR---TEKQAYWQVVEGAldAQLALLKAAIAA 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 989 LQSQLKlreGEITHLQLEIGNLEKTRSIMAEELVKLTNQNDELEEKVKEIPKLRTQLRDLDQRYN-TILQMYGEKAEEAE 1067
Cdd:pfam12128 741 RRSGAK---AELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQeTWLQRRPRLATQLS 817
|
650 660
....*....|....*....|...
gi 110347443 1068 ELRLDLEDVKNMYKTQIDELLRQ 1090
Cdd:pfam12128 818 NIERAISELQQQLARLIADTKLR 840
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
587-782 |
5.08e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 587 ENMVAKLNKKVKELEEELQHLKQ---VLDGKEEvEKQHRENIKKLNSmverqekDLGRLQVDMDELEEKNRSIQAALDSA 663
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQkngLVDLSEE-AKLLLQQLSELES-------QLAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 664 YKELTDLHKANAAKDSEAQEAALSREMkakEELSA-------ALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKE 736
Cdd:COG3206 253 PDALPELLQSPVIQQLRAQLAELEAEL---AELSArytpnhpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQARE 329
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 110347443 737 DYLRHEIGELQQRLQEAENRNQELSQsvssttrpLLRQIENLQATL 782
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEAELRR--------LEREVEVARELY 367
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
439-730 |
6.97e-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: 6.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 439 EALSEKEDVCKTVEFLNEKLEKREAQLLSLskEKALLEEAFDNLKDEMFRVKEESSSISSlkdeftqRIAEAEKKVQLAC 518
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEA-------RLREIEQKLNRLT 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 519 KERDAAKKEIKNIKEELatrlnssetaDLLKEKDEQIRglmeegeklskQQLHNSNIikKLRAKDKEnenmVAKLNKKVK 598
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQR----------IDLKEQIKSIE-----------KEIENLNG--KKEELEEE----LEELEAALR 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 599 ELEEELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALD---SAYKELTDLHKANA 675
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGedeEIPEEELSLEDVQA 958
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 110347443 676 AKdsEAQEAALSR----EMKAKEELSAAlEKAQEEARQQQETLAIQVGDLRLALQRTEQ 730
Cdd:TIGR02169 959 EL--QRVEEEIRAlepvNMLAIQEYEEV-LKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
463-699 |
7.10e-08 |
|
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: 55.93 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 463 AQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEELATrlNSS 542
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE--LEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 543 ETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIkKLRAKD-KENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQH 621
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLAL-LLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110347443 622 RENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKanAAKDSEAQEAALSREMKAKEELSAA 699
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ--EAEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
548-732 |
9.60e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 55.94 E-value: 9.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 548 LKEKDEQIRGLMEEGEKLSKQQLHNsniiKKLRAKDkENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKK 627
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKE----ALLEAKE-EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 628 LNSMVERQEKDLGRLQVDMDELEEKNRSIQAaldsayKELTDLHKANAAKDSEAQEAALSR-EMKAKEELSAALEKAQEE 706
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEKKEEELEELIE------EQLQELERISGLTAEEAKEILLEKvEEEARHEAAVLIKEIEEE 181
|
170 180
....*....|....*....|....*...
gi 110347443 707 ARQQQETLAIQVgdLRLALQR--TEQAA 732
Cdd:PRK12704 182 AKEEADKKAKEI--LAQAIQRcaADHVA 207
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
520-913 |
1.00e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 56.60 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 520 ERDAAKKEIKNIKEELATRLNSSETadlLKEKDE----QIRGLMEEGEKLSKQQLHNSNIikklRAKDKENENMVAKLNK 595
Cdd:TIGR01612 1112 EINKIKDDIKNLDQKIDHHIKALEE---IKKKSEnyidEIKAQINDLEDVADKAISNDDP----EEIEKKIENIVTKIDK 1184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 596 KvKELEEELqhlKQVLDGKEEVEKQhRENIKKLNSMVERQEKDLGRLQVD-MDELEEKNRSIQAALDSAYKELTDLHKAN 674
Cdd:TIGR01612 1185 K-KNIYDEI---KKLLNEIAEIEKD-KTSLEEVKGINLSYGKNLGKLFLEkIDEEKKKSEHMIKAMEAYIEDLDEIKEKS 1259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 675 AAKDSE-AQEAALSREMKAKEELSAALEKAQEEARQQQETLAiqvgDLRLALQRTEQAAARKEDyLRHEIGELQQRLQEA 753
Cdd:TIGR01612 1260 PEIENEmGIEMDIKAEMETFNISHDDDKDHHIISKKHDENIS----DIREKSLKIIEDFSEESD-INDIKKELQKNLLDA 1334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 754 ENRNQELSQSVSSTTRPL----LRQIENLQATLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAAT-----EELLAN 824
Cdd:TIGR01612 1335 QKHNSDINLYLNEIANIYnilkLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEEckskiESTLDD 1414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 825 K-----IQmSSMESQNSLLRQE---NSRFQAQLESEKNRLC---KLEDENNRYQVELENLKD----EYVRTLEETRKEKT 889
Cdd:TIGR01612 1415 KdidecIK-KIKELKNHILSEEsniDTYFKNADENNENVLLlfkNIEMADNKSQHILKIKKDnatnDHDFNINELKEHID 1493
|
410 420
....*....|....*....|....*
gi 110347443 890 LLNS-QLEMERMKVEQERKKAIFTQ 913
Cdd:TIGR01612 1494 KSKGcKDEADKNAKAIEKNKELFEQ 1518
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
519-773 |
1.09e-07 |
|
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: 55.54 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 519 KERDAAKKEIKNIKEELAtrlnssETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVK 598
Cdd:COG4942 20 DAAAEAEAELEQLQQEIA------ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 599 ELEEELQHLKQVLdgKEEVEKQHRENIKKLNSMVERQEkDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLhkanaakd 678
Cdd:COG4942 94 ELRAELEAQKEEL--AELLRALYRLGRQPPLALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRADLAEL-------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 679 sEAQEAALSREMKAKEelsaALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEIGELQQRLQEAENRNQ 758
Cdd:COG4942 163 -AALRAELEAERAELE----ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
250
....*....|....*
gi 110347443 759 ELSQSVSSTTRPLLR 773
Cdd:COG4942 238 AAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
472-888 |
2.41e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 472 KALLEEAFDNLKDEMFRVKEESSSISSLK-DEFTQRIAEAEKKVQlACKERDAAKKEIKNIKEELATRLNSSETADLLKE 550
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKElKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 551 KDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLdgkEEVEKQHRENIKKLNS 630
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELL---EQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 631 MVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSEAQEAALS----------------------- 687
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallallglggsllsliltiagvl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 688 ------------REMKAKEELSAALEKAQEEARQ---QQETLAIQVGDLRLALQRTEQAAARkedyLRHEIGELQQRLQE 752
Cdd:COG4717 280 flvlgllallflLLAREKASLGKEAEELQALPALeelEEEELEELLAALGLPPDLSPEELLE----LLDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 753 AENRNQELSQSVSSTTRP--------------------------LLRQIENLQATLGSQTSSWEKL-----EKNLSDRLG 801
Cdd:COG4717 356 AEELEEELQLEELEQEIAallaeagvedeeelraaleqaeeyqeLKEELEELEEQLEELLGELEELlealdEEELEEELE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 802 ESQTLLAAAVERERAATEELLANKIQMSSMESQNSLlrqenSRFQAQLESEKNRLCKLEDENNRYQVELENLKdeyvRTL 881
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEEDGEL-----AELLQELEELKAELRELAEEWAALKLALELLE----EAR 506
|
....*..
gi 110347443 882 EETRKEK 888
Cdd:COG4717 507 EEYREER 513
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
454-922 |
2.94e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.80 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 454 LNEKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVqlackerdaaKKEIKNIKE 533
Cdd:pfam01576 136 LEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERL----------KKEEKGRQE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 534 -ELATRLNSSETADLlkekDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLd 612
Cdd:pfam01576 206 lEKAKRKLEGESTDL----QEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDL- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 613 gkeEVEKQHRENikklnsmVERQEKDLG-RLQVDMDELEEKNRSIQAALDSAYK---ELTDLHKA--NAAKDSEAQEAAL 686
Cdd:pfam01576 281 ---ESERAARNK-------AEKQRRDLGeELEALKTELEDTLDTTAAQQELRSKreqEVTELKKAleEETRSHEAQLQEM 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 687 S-REMKAKEELSAALEKAQ------EEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEIGELQQRLQEAENRNQE 759
Cdd:pfam01576 351 RqKHTQALEELTEQLEQAKrnkanlEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 760 LSQSVSSttrpLLRQIENLQATLGSQTSSWEKLEKNLS---DRLGESQTLLAAAVERERAATEELLANKIQMSSM----- 831
Cdd:pfam01576 431 LAEKLSK----LQSELESVSSLLNEAEGKNIKLSKDVSsleSQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLqeqle 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 832 ---------ESQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEYV-RTLEETRKEKTLLNSQLEMERMK 901
Cdd:pfam01576 507 eeeeakrnvERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEeKAAAYDKLEKTKNRLQQELDDLL 586
|
490 500
....*....|....*....|.
gi 110347443 902 VEQERKKAIFTqeTIKEKERK 922
Cdd:pfam01576 587 VDLDHQRQLVS--NLEKKQKK 605
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
417-1087 |
3.02e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 417 INEGQTVLDKVAEQCEPAESqpealsEKEdvcKTVEFLNEKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSI 496
Cdd:TIGR02169 186 IERLDLIIDEKRQQLERLRR------ERE---KAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 497 SSLKDEFTQRIAEAEKKV-QLACKERDAAKKEIKNIKEELAtrlnsSETADLLKEKDeQIRGLMEEGEKLSKQQLHNSNI 575
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLeELNKKIKDLGEEEQLRVKEKIG-----ELEAEIASLER-SIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 576 IKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGK----EEVEKQHRENIKKLNSMVERQEKdlgrLQVDMDELEE 651
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLraelEEVDKEFAETRDELKDYREKLEK----LKREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 652 KNRSIQAALDSAYKELTDLHkaNAAKDSEAQEAALSREMKAKEElsaalekAQEEARQQQETLAIQVGDLRLALQRTEQA 731
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLN--AAIAGIEAKINELEEEKEDKAL-------EIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 732 AARKEDylrhEIGELQQRLQEAENRNQELSQSVSSTTRPLLRQIENLQATLG--SQTSSWEK-----LEKNLSDRL---- 800
Cdd:TIGR02169 478 YDRVEK----ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGtvAQLGSVGEryataIEVAAGNRLnnvv 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 801 ------------------GESQTLLAAAVERERAATEELLANK---------------------------IQMSSMESQN 835
Cdd:TIGR02169 554 veddavakeaiellkrrkAGRATFLPLNKMRDERRDLSILSEDgvigfavdlvefdpkyepafkyvfgdtLVVEDIEAAR 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 836 SLL----------------------------RQENSRFQ-AQLESEKNRLCKLEDENNRYQVEL---ENLKDEYVRTLEE 883
Cdd:TIGR02169 634 RLMgkyrmvtlegelfeksgamtggsraprgGILFSRSEpAELQRLRERLEGLKRELSSLQSELrriENRLDELSQELSD 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 884 TRKEKTLLNSQLEMERMKVEQERKKAIFTQETIKEKERKpfsvsstptmsrsssisgvdmaglqtsflsqdeshdhsfgp 963
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE----------------------------------------- 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 964 mpisangsnlydavrmgagssiIENLQSQLKLREGEITHLQLEIGNLEKT-----RSIMAEELVKLTNQNDELEEKVKEI 1038
Cdd:TIGR02169 753 ----------------------IENVKSELKELEARIEELEEDLHKLEEAlndleARLSHSRIPEIQAELSKLEEEVSRI 810
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 110347443 1039 pklRTQLRDLDQRYN--TILQMYGEKA-EEAEELRLDLEDVKNMYKTQIDEL 1087
Cdd:TIGR02169 811 ---EARLREIEQKLNrlTLEKEYLEKEiQELQEQRIDLKEQIKSIEKEIENL 859
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
454-922 |
4.65e-07 |
|
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: 54.35 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 454 LNEKLEKREAQLLSLSKEKALLEEAFDNLKDE-MFRVKEESSSISSLKDE-------FTQRIAEAEKKVQLACKE----- 520
Cdd:pfam15921 283 LTEKASSARSQANSIQSQLEIIQEQARNQNSMyMRQLSDLESTVSQLRSElreakrmYEDKIEELEKQLVLANSEltear 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 521 --RDAAKKEIKNIKEELATRLnssetADLLKeKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRaKDKENENMvaklnkKVK 598
Cdd:pfam15921 363 teRDQFSQESGNLDDQLQKLL-----ADLHK-REKELSLEKEQNKRLWDRDTGNSITIDHLR-RELDDRNM------EVQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 599 ELEEELQHLKQVLDGKEEVE----KQHRENIKKLNSMVERQEKDLGRLQVDMDEL---------------------EEKN 653
Cdd:pfam15921 430 RLEALLKAMKSECQGQMERQmaaiQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakkmtlessertvsdltaslQEKE 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 654 RSIQAA----------LDSAYKELTDL-----HKANAAKDSEAQEAALSREMKAKEELSAALEKAQEEARQQQET----- 713
Cdd:pfam15921 510 RAIEATnaeitklrsrVDLKLQELQHLknegdHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTagamq 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 714 -----LAIQVGDLRLALQRTEQAAARKEDYLRheigELQQRLQEAENRNQELSQSVSSTTRP----------LLRQIENL 778
Cdd:pfam15921 590 vekaqLEKEINDRRLELQEFKILKDKKDAKIR----ELEARVSDLELEKVKLVNAGSERLRAvkdikqerdqLLNEVKTS 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 779 QATLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSMESQNSLLRQENSRFQAQLESEKNRLCK 858
Cdd:pfam15921 666 RNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDA 745
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110347443 859 LEDENNRYQVELENLKDEYVRTLEETRKektllnsqLEMERMKVEQERKKAIFTQETIKEKERK 922
Cdd:pfam15921 746 LQSKIQFLEEAMTNANKEKHFLKEEKNK--------LSQELSTVATEKNKMAGELEVLRSQERR 801
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
470-1087 |
4.85e-07 |
|
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: 54.35 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 470 KEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEELATRLNSSETADLLK 549
Cdd:pfam15921 103 KQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSH 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 550 EKD-EQIRGLMEEGEKLSKQQLHNSNIIKKLRAKdkeneNMVAKLNKKVKELEEELQHLK-QVLDGKEEVEKQHRENIKK 627
Cdd:pfam15921 183 EGVlQEIRSILVDFEEASGKKIYEHDSMSTMHFR-----SLGSAISKILRELDTEISYLKgRIFPVEDQLEALKSESQNK 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 628 LNSMVERQEKDLGRL----QVDMDELEEKNRSIQAALDSAYKELTDLHKanaakDSEAQEAALSREMKAKEELSAALEKA 703
Cdd:pfam15921 258 IELLLQQHQDRIEQLisehEVEITGLTEKASSARSQANSIQSQLEIIQE-----QARNQNSMYMRQLSDLESTVSQLRSE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 704 QEEARQQQETlAIQVGDLRLALQRTEQAAARKE-DYLRHEIG----ELQQRLQEAENRNQELSQSVSSTTRPLLRQIENl 778
Cdd:pfam15921 333 LREAKRMYED-KIEELEKQLVLANSELTEARTErDQFSQESGnlddQLQKLLADLHKREKELSLEKEQNKRLWDRDTGN- 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 779 qatlgsqTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELlanKIQMSSMESQNSLLRQENSrFQAQLESEKNRLCK 858
Cdd:pfam15921 411 -------SITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQM---ERQMAAIQGKNESLEKVSS-LTAQLESTKEMLRK 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 859 LEDEnnryqvelenlkdeyvrtleetrkektllnsqLEMERMKVEQERKKAIFTQETIKEKERKPFSVSSTPTMSRSSsi 938
Cdd:pfam15921 480 VVEE--------------------------------LTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSR-- 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 939 sgVDMAGLQTSFLSQDESHdhsfgpmpiSANGSNLYDAVR--MGAGSSIIENLQSQLKLREGEITH-------LQLEIGN 1009
Cdd:pfam15921 526 --VDLKLQELQHLKNEGDH---------LRNVQTECEALKlqMAEKDKVIEILRQQIENMTQLVGQhgrtagaMQVEKAQ 594
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110347443 1010 LEKTRSIMAEELVKLTNQNDELEEKVKEipkLRTQLRDLDQRYNTILQMYGEKAEEAEELRLDLEDVKNMYKTQIDEL 1087
Cdd:pfam15921 595 LEKEINDRRLELQEFKILKDKKDAKIRE---LEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNEL 669
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
614-942 |
1.12e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 614 KEEVEkQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELtdLHKANAAKDS----EAQEAALSRE 689
Cdd:TIGR02169 176 LEELE-EVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYEL--LKEKEALERQkeaiERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 690 MKAKEELSAALEKAQEEARQQQETLAIQVGDL----RLALQRTEQAAARKEDYLRHEIGELQQRLQEAENRNQELS---Q 762
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEaeiD 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 763 SVSSTTRPLLRQIENLQATLGSQTSSWEKLEKNLSD---RLGESQTLLAAAVERERAATEELLANKIQMSSMESQNSLLR 839
Cdd:TIGR02169 333 KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDlraELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 840 QENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEyVRTLEETRKEktlLNSQLEMERMKVEQERKKAIFTQETIKEK 919
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE-IKKQEWKLEQ---LAADLSKYEQELYDLKEEYDRVEKELSKL 488
|
330 340
....*....|....*....|...
gi 110347443 920 ERKPFSVSSTPTMSRSSSISGVD 942
Cdd:TIGR02169 489 QRELAEAEAQARASEERVRGGRA 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
649-891 |
2.72e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 649 LEEknRSIQAALDSAYKELTDLHKA-NAAKDSEAQEAALSREMKAKEELSAALEKAqEEARQQQETLAIQVGDLRLALQR 727
Cdd:COG4913 218 LEE--PDTFEAADALVEHFDDLERAhEALEDAREQIELLEPIRELAERYAAARERL-AELEYLRAALRLWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 728 TEQAAARKE-DYLRHEIGELQQRLQEAENRNQELSQSVSS----TTRPLLRQIENLQATLGSQTSSWEKLEKNLsDRLGE 802
Cdd:COG4913 295 AELEELRAElARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALL-AALGL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 803 SQTLlaaavereraaTEELLANkiqmssmesqnslLRQENSRFQAQLESEKNRLckledENNRYQ--VELENLKDEyvrt 880
Cdd:COG4913 374 PLPA-----------SAEEFAA-------------LRAEAAALLEALEEELEAL-----EEALAEaeAALRDLRRE---- 420
|
250
....*....|.
gi 110347443 881 LEETRKEKTLL 891
Cdd:COG4913 421 LRELEAEIASL 431
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
439-710 |
2.76e-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: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 439 EALSEKEDVCKTVEFLNEKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLAC 518
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 519 KERDAAKKEIKNIKEELATRLNssetadLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVK 598
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLN------ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 599 ELEEELQHLKQVLDGKEEVEKQ-HRENIKKLNSMVERQEKDLGRLQVDMDELEEKNrsiQAALDsAYKELTDLHKANAAK 677
Cdd:TIGR02168 933 GLEVRIDNLQERLSEEYSLTLEeAEALENKIEDDEEEARRRLKRLENKIKELGPVN---LAAIE-EYEELKERYDFLTAQ 1008
|
250 260 270
....*....|....*....|....*....|...
gi 110347443 678 DSEAQEaalsremkAKEELSAALEKAQEEARQQ 710
Cdd:TIGR02168 1009 KEDLTE--------AKETLEEAIEEIDREARER 1033
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
583-1069 |
4.18e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 583 DKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLnsmvERQEKDLGRLQVDMDELEEKNRSIQAALDs 662
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL----EELEEELEELEAELEELREELEKLEKLLQ- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 663 AYKELTDLHKANAAKDSEAQEA-ALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRH 741
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLeELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 742 EIGELQQRLQEAENRNQELSQSVSSTTRPLLRQIENlqatlgsqtsswEKLEKNLSDRLGESQTLLAAAVERERAATEEL 821
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALE------------ERLKEARLLLLIAAALLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 822 LANKIQMSSmeSQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEYvrTLEETRKEKTLLNSQLEMERMK 901
Cdd:COG4717 275 IAGVLFLVL--GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAL--GLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 902 VEQERKKAIFTQETIKEKERKpfsvsstptmsrsssisgvdmagLQTSFLSQDESHDHSFGpmpisangSNLYDAVRMGA 981
Cdd:COG4717 351 ELLREAEELEEELQLEELEQE-----------------------IAALLAEAGVEDEEELR--------AALEQAEEYQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 982 GSSIIENLQSQLKLREGEITHLqLEIGNLEKTRSIMAEELVKLTNQNDELEEKVKEIPKLRTQLRDL--DQRYNTILQMY 1059
Cdd:COG4717 400 LKEELEELEEQLEELLGELEEL-LEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQEL 478
|
490
....*....|
gi 110347443 1060 GEKAEEAEEL 1069
Cdd:COG4717 479 EELKAELREL 488
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
546-789 |
5.12e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 546 DLLKEKDEQIRGLMEEGEKLSKQqlhnsniIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENI 625
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAE-------LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 626 KKLNSMVERQEKDLGRLQV-----DMDELEEKNRSIQAALDSAYKELTDLHKANAAKdsEAQEAALSREMKAKEELSAAL 700
Cdd:COG3883 89 GERARALYRSGGSVSYLDVllgseSFSDFLDRLSALSKIADADADLLEELKADKAEL--EAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 701 EKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEIGELQQRLQEAENRNQELSQSVSSTTRPLLRQIENLQA 780
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
....*....
gi 110347443 781 TLGSQTSSW 789
Cdd:COG3883 247 AGAGAAGAA 255
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
462-719 |
5.17e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 462 EAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEELATRLNS 541
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 542 SETADLLKEKDEQIRG------LMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKE 615
Cdd:COG3883 95 LYRSGGSVSYLDVLLGsesfsdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 616 EVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSEAQEAALSREMKAKEE 695
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
|
250 260
....*....|....*....|....
gi 110347443 696 LSAALEKAQEEARQQQETLAIQVG 719
Cdd:COG3883 255 AGAAAGSAGAAGAAAGAAGAGAAA 278
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
480-920 |
5.20e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.88 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 480 DNLKDEM-FRVKEESSSISSLKDEFTQRIAEAEKKVQL---ACKERDAAKKEIKNIKEELATRLNSSEtaDLLKEKDEQI 555
Cdd:pfam05483 207 ENARLEMhFKLKEDHEKIQHLEEEYKKEINDKEKQVSLlliQITEKENKMKDLTFLLEESRDKANQLE--EKTKLQDENL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 556 RGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDgkeEVEKQHRENIKKLNSMVERQ 635
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELN---KAKAAHSFVVTEFEATTCSL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 636 EKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSE--------AQEAALSREMKAKEELSAALEKAQEEA 707
Cdd:pfam05483 362 EELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVEleelkkilAEDEKLLDEKKQFEKIAEELKGKEQEL 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 708 RQQQETLAIQVGDLRLALQRTEQAaarkEDYLRHEIGELQQRLQEAENRN--------------QELSQSVSSTTRPL-- 771
Cdd:pfam05483 442 IFLLQAREKEIHDLEIQLTAIKTS----EEHYLKEVEDLKTELEKEKLKNieltahcdklllenKELTQEASDMTLELkk 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 772 ---------------LRQIENLQATLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSMESQNS 836
Cdd:pfam05483 518 hqediinckkqeermLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCN 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 837 LLR--------------QENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEYVRTLEETRKEktLLNSQLEMERMKV 902
Cdd:pfam05483 598 NLKkqienknknieelhQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKE--IEDKKISEEKLLE 675
|
490
....*....|....*...
gi 110347443 903 EQERKKAIFTQETIKEKE 920
Cdd:pfam05483 676 EVEKAKAIADEAVKLQKE 693
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
697-922 |
5.50e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 697 SAALEKAQEEARQQQETLAIQVGDLRLALQRTEQaaarKEDYLRHEIGELQQRLQEAENRNQELSQsvssttrpllrQIE 776
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKK----EEKALLKQLAALERRIAALARRIRALEQ-----------ELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 777 NLQATLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSMESQNSLLRQENSRFQAQLESEKNRL 856
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110347443 857 CKLEDEnnryQVELENLKDEYVRTLEETRKEKTLLNSQLEMERMKVEQERKKAIFTQETIKEKERK 922
Cdd:COG4942 160 AELAAL----RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
591-765 |
7.19e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 7.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 591 AKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLnsmverqEKDLGRLQVDMDELEEKNRSIQAALDSA--YKELT 668
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-------EKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 669 dlhkanaakdseaqeaALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEIGELQQ 748
Cdd:COG1579 93 ----------------ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170
....*....|....*..
gi 110347443 749 RLQEAENRNQELSQSVS 765
Cdd:COG1579 157 ELEELEAEREELAAKIP 173
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
556-807 |
7.53e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 50.30 E-value: 7.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 556 RGLMEEGEKLSKQQLHNS-NIIKKLRAKDKENENMVAKLN---KKVKELEEELQHLKQVLDgkEEVEKQHR-ENIKKLNS 630
Cdd:PRK11281 51 QKLLEAEDKLVQQDLEQTlALLDKIDRQKEETEQLKQQLAqapAKLRQAQAELEALKDDND--EETRETLStLSLRQLES 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 631 MVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHK-----ANAAKDSEAQEAALSREMKAKEELSAALEKAQE 705
Cdd:PRK11281 129 RLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQrlqqiRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 706 EARQQQETLAIQVGDLrLALQRTEQAAarKEDYLRHEIGELQ-----QRLQEAENRNQELSQS---VSSTTRPLL-RQIE 776
Cdd:PRK11281 209 DLQRKSLEGNTQLQDL-LQKQRDYLTA--RIQRLEHQLQLLQeainsKRLTLSEKTVQEAQSQdeaARIQANPLVaQELE 285
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 110347443 777 N--------LQATLGSQTSSWEKLE-KNLSDRLGESQTLL 807
Cdd:PRK11281 286 InlqlsqrlLKATEKLNTLTQQNLRvKNWLDRLTQSERNI 325
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
624-800 |
8.63e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 8.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 624 NIKKLnsmvERQEKDLGRLQVDMDELEEKNRSIQAALD------SAYKELTDLhkANAAKDSEAQEAALSREMKAKEELS 697
Cdd:COG4913 608 NRAKL----AALEAELAELEEELAEAEERLEALEAELDalqerrEALQRLAEY--SWDEIDVASAEREIAELEAELERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 698 A------ALEKAQEEARQQQETLAIQVGDLRLALQRTEQaaarkedylrhEIGELQQRLQEAENRNQELSQSVSSTTRPL 771
Cdd:COG4913 682 AssddlaALEEQLEELEAELEELEEELDELKGEIGRLEK-----------ELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
170 180 190
....*....|....*....|....*....|....*....
gi 110347443 772 L----------RQIENLQATLGSQTSSWEKLEKNLSDRL 800
Cdd:COG4913 751 LeerfaaalgdAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
422-908 |
8.81e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 8.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 422 TVLDKVAEQCEPAESQPEALSEKEDVcKTVEFLNEKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLK- 500
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEKEEKDLH-ERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEa 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 501 --DEFTQRIAEAEKkvqlackERDAAKKEIKNIKEELATRlnssetadllkekDEQIRGLMEEGEKLSkqqlhnsniikk 578
Cdd:PRK02224 259 eiEDLRETIAETER-------EREELAEEVRDLRERLEEL-------------EEERDDLLAEAGLDD------------ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 579 lrAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQA 658
Cdd:PRK02224 307 --ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRRE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 659 ALDSAYKELTDLHKANAAKDSEAQEAALSREMKAKE---------ELSAALEKAQEEARQQQETLAiqVGDLRLALQRTE 729
Cdd:PRK02224 385 EIEELEEEIEELRERFGDAPVDLGNAEDFLEELREErdelrereaELEATLRTARERVEEAEALLE--AGKCPECGQPVE 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 730 QA--AARKEDYlRHEIGELQQRLQEAENRNQELSQSVSSTTRplLRQIENLQATLGSQTSSWEKLEKNLSDRLGESQTLL 807
Cdd:PRK02224 463 GSphVETIEED-RERVEELEAELEDLEEEVEEVEERLERAED--LVEAEDRIERLEERREDLEELIAERRETIEEKRERA 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 808 AAAVERERAATEELLANKIQMSSMESQNSLLRQENSRFQAQLESEKNRLCKLEDENNRyQVELENLKDEYVRtLEETRKE 887
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTL-LAAIADAEDEIER-LREKREA 617
|
490 500
....*....|....*....|.
gi 110347443 888 KTLLNSQlEMERMKVEQERKK 908
Cdd:PRK02224 618 LAELNDE-RRERLAEKRERKR 637
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
691-922 |
9.33e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 9.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 691 KAKEELsaalekaqEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLrheigELQQRLQEAENrnQELSQSVSSttrp 770
Cdd:TIGR02169 174 KALEEL--------EEVEENIERLDLIIDEKRQQLERLRREREKAERYQ-----ALLKEKREYEG--YELLKEKEA---- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 771 LLRQIENLQATLGSQTSSWEKLEKNLSDRLGES----QTLLAAAVERERAATEELLANKIQMSSMESQNSLLRQENSRFQ 846
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLeeieQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 847 AQLESEKNRLCKLEDENNRYQVELENLKdeyvRTLEETRKEKTLLNSQ-------LEMERMKVEQERKKAIFTQETIKEK 919
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELE----REIEEERKRRDKLTEEyaelkeeLEDLRAELEEVDKEFAETRDELKDY 390
|
...
gi 110347443 920 ERK 922
Cdd:TIGR02169 391 REK 393
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
439-794 |
9.40e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 9.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 439 EALSEKEDVCKTVEFLNEKLEKREAQLLSLSKEKALLEEAFDNLKD--EMFRVKEESSSISSLKDEFTQRIAEAEKKVQL 516
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 517 ---ACKERDAAKKEIKNIKEELAT--RLNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVA 591
Cdd:COG4717 158 lreLEEELEELEAELAELQEELEEllEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 592 KLNKKvKELEEELQHLKQ----------------------------------VLDGKEEVEKQHRENIKKLNSMVERQEK 637
Cdd:COG4717 238 AAALE-ERLKEARLLLLIaaallallglggsllsliltiagvlflvlgllalLFLLLAREKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 638 DLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSEAQEAALSREMKAKEEL--------SAALEKAQEEARQ 709
Cdd:COG4717 317 EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALlaeagvedEEELRAALEQAEE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 710 QQETLAiQVGDLRLALQ-----RTEQAAARKEDYLRHEIGELQQRLQEAENRNQELSQSvssttrplLRQIENLQATLGS 784
Cdd:COG4717 397 YQELKE-ELEELEEQLEellgeLEELLEALDEEELEEELEELEEELEELEEELEELREE--------LAELEAELEQLEE 467
|
410
....*....|
gi 110347443 785 QTSSWEKLEK 794
Cdd:COG4717 468 DGELAELLQE 477
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
424-688 |
1.38e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 424 LDKVAEQCEPAESQPEALSEKEDVCKTVEFLNEKLEKREAQLLSLSKEKalleeaFDNLKDEMFRVKEEsssISSLKDEF 503
Cdd:PRK03918 478 LRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE------YEKLKEKLIKLKGE---IKSLKKEL 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 504 tQRIAEAEKKVQLACKERDAAKKEIKNIKEELATRLNSSEtaDLLKEKDEQIRGLMEEGEKL--SKQQLHNS-NIIKKLR 580
Cdd:PRK03918 549 -EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESV--EELEERLKELEPFYNEYLELkdAEKELEREeKELKKLE 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 581 AKDKENENMVAKLNKKVKELEEELQHLKQVLDGKE---------EVEKQH---RENIKKLNSMVERQEKDLGRLQVDMDE 648
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelreeylELSRELaglRAELEELEKRREEIKKTLEKLKEELEE 705
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 110347443 649 LEEKNRSIQaALDSAYKELTDLHKANAAKDSEAQEAALSR 688
Cdd:PRK03918 706 REKAKKELE-KLEKALERVEELREKVKKYKALLKERALSK 744
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
614-923 |
1.48e-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: 49.28 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 614 KEEVEKQ---HRENIKKLNSMVERQEKDLGRLQvdmdeleeknrsIQAALDSAYKELTDlhkanaaKDSEAQEAALSREM 690
Cdd:TIGR02168 174 RKETERKlerTRENLDRLEDILNELERQLKSLE------------RQAEKAERYKELKA-------ELRELELALLVLRL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 691 KAKEELSAALEKAQEEARQQQEtlaiqvgdlrlALQRTEQAAARKEDYLRHEIGELQQRLQEAENRNQELSQsvssttrp 770
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELE-----------ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN-------- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 771 llrQIENLQATLGSQTSSWEKLEKNLSDRLGESQTLLAAAvereraatEELLANKiqmSSMESQNSLLRQENSRFQAQLE 850
Cdd:TIGR02168 296 ---EISRLEQQKQILRERLANLERQLEELEAQLEELESKL--------DELAEEL---AELEEKLEELKEELESLEAELE 361
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110347443 851 SEKNRLCKLEDENNRYQVELENLKDEYVrtleETRKEKTLLNSQLEMERMKVEQERKKAIFTQETIKEKERKP 923
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLETLRSKVA----QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
528-924 |
1.87e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.20 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 528 IKNIKEELATRLNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHL 607
Cdd:pfam02463 604 NLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQE 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 608 KQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDsaYKELTDLHKANAAKDSEAQEAALS 687
Cdd:pfam02463 684 KAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEE--LKLLKQKIDEEEEEEEKSRLKKEE 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 688 REMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEIGELQQRLQEAENRNQELSQSVSST 767
Cdd:pfam02463 762 KEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALE 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 768 TRPLLRQIENLQATLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSMESQNSLLRQENSRFQA 847
Cdd:pfam02463 842 LKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEE 921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 848 QLESEKNRLCKLEDENNRYQVELENLKDEYVRTLEETRKEKTLLNSQ------------------------LEMERMKVE 903
Cdd:pfam02463 922 RIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAkeelgkvnlmaieefeekeerynkDELEKERLE 1001
|
410 420
....*....|....*....|.
gi 110347443 904 QERKKAIFTQETIKEKERKPF 924
Cdd:pfam02463 1002 EEKKKLIRAIIEETCQRLKEF 1022
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
449-637 |
2.31e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 449 KTVEFLNEKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKV---------QLACK 519
Cdd:TIGR04523 482 QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkddfelkkENLEK 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 520 ERDAAKKEIKNIKEELATRLNSSETAD-LLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVK 598
Cdd:TIGR04523 562 EIDEKNKEIEELKQTQKSLKKKQEEKQeLIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKN 641
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 110347443 599 ELEEELQHLKQVLDG----KEEVEKQHRENIKKLNSMVERQEK 637
Cdd:TIGR04523 642 KLKQEVKQIKETIKEirnkWPEIIKKIKESKTKIDDIIELMKD 684
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
424-792 |
2.32e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 424 LDKVAEQCEPAESQPEALSEKEDVCKTVEFLNEKLEK---REAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLK 500
Cdd:COG4717 114 LREELEKLEKLLQLLPLYQELEALEAELAELPERLEEleeRLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 501 -DEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEELATRLNSSETADLLKEKDEQ-----IRGLMEEGEKLSKQQLHNSN 574
Cdd:COG4717 194 lQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArllllIAAALLALLGLGGSLLSLIL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 575 IIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKL--------NSMVERQEKDLGRLQVDM 646
Cdd:COG4717 274 TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAlglppdlsPEELLELLDRIEELQELL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 647 DELEEKNRsiQAALDSAYKELTDLHKANAAKDSEAQEAALSREMKAKE------ELSAALEKAQEEARQQQETLAIQVGD 720
Cdd:COG4717 354 REAEELEE--ELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQElkeeleELEEQLEELLGELEELLEALDEEELE 431
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110347443 721 LRLALQRTEQAAARKE-DYLRHEIGELQQRLQEAENrNQELSQsvssttrpLLRQIENLQATLGSQTSSWEKL 792
Cdd:COG4717 432 EELEELEEELEELEEElEELREELAELEAELEQLEE-DGELAE--------LLQELEELKAELRELAEEWAAL 495
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
531-612 |
2.79e-05 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 47.76 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 531 IKEELATRlNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENM---VAKLNKKVKELEEELQHL 607
Cdd:PRK05431 14 VKEALAKR-GFPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALiaeVKELKEEIKALEAELDEL 92
|
....*
gi 110347443 608 KQVLD 612
Cdd:PRK05431 93 EAELE 97
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
543-915 |
3.66e-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: 47.81 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 543 ETADLLKEKDEQIRGlMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEElqhlkqvlDGKEEVEKQHR 622
Cdd:pfam17380 297 EQERLRQEKEEKARE-VERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQE--------ERKRELERIRQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 623 ENIkklnSMVERQEKDLGRLQVdmdELEEKNRSIQAALDsaykeltdlhkanAAKDSEAQEAALSREMKAKEELSAALEK 702
Cdd:pfam17380 368 EEI----AMEISRMRELERLQM---ERQQKNERVRQELE-------------AARKVKILEEERQRKIQQQKVEMEQIRA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 703 AQEEARQQQetlaiqvgdlrlaLQRTEQAAARKEDYLRHEIGELQQRLQeaenrnqelsqsvssttrpLLRQIENLQatl 782
Cdd:pfam17380 428 EQEEARQRE-------------VRRLEEERAREMERVRLEEQERQQQVE-------------------RLRQQEEER--- 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 783 gsqtssweKLEKNLSDRLGESQTLLAAAVERERAatEELLANKIQMSSMESQNSLLRQENSRFQAQLESEKNRlcKLEDE 862
Cdd:pfam17380 473 --------KRKKLELEKEKRDRKRAEEQRRKILE--KELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERR--REAEE 540
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 110347443 863 NNRYQVELENLK--DEYVRTLEETRKEKTLLNSQLEMERMKVEQERKKAIFTQET 915
Cdd:pfam17380 541 ERRKQQEMEERRriQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATT 595
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
622-806 |
4.35e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 622 RENIKKLNSM---VERQEKDLGRLQvdmdELEEKNRSIQAALDsaykELTDLHKANAAKDSEAQEAALSREMKAKEELSA 698
Cdd:COG4913 231 VEHFDDLERAheaLEDAREQIELLE----PIRELAERYAAARE----RLAELEYLRAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 699 ALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEIGELQQRLQEAENRNQELSQ-------SVSSTTRPL 771
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEAllaalglPLPASAEEF 382
|
170 180 190
....*....|....*....|....*....|....*
gi 110347443 772 LRQIENLQATLGSQTSSWEKLEKNLSDRLGESQTL 806
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAALRDL 417
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
521-759 |
7.06e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 521 RDAAKKEIKNIKEELAtrlnssETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDK--ENENMVAKL---NK 595
Cdd:COG4913 612 LAALEAELAELEEELA------EAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaELEAELERLdasSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 596 KVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAA-LDSAYKELTDlhKAN 674
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALG--DAV 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 675 AAKDSEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAiqvGDLRLALQRTEQAAARKEDYLRHEIGELQQRLQEAE 754
Cdd:COG4913 764 ERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAET---ADLDADLESLPEYLALLDRLEEDGLPEYEERFKELL 840
|
....*
gi 110347443 755 NRNQE 759
Cdd:COG4913 841 NENSI 845
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
592-798 |
7.33e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 592 KLNK-KVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNsmvERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDL 670
Cdd:PHA02562 170 KLNKdKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQR---KKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 671 hkanaAKDSEAQEAALSREMKAKEELSAALEKAQEEARQQQE-------TLAIQVGDLRLALQRTEQAAARKE-DYLRHE 742
Cdd:PHA02562 247 -----VMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptcTQQISEGPDRITKIKDKLKELQHSlEKLDTA 321
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 743 IGELQQRLQEA--------------ENRNQELSQSVSSTTRpLLRQIENLQATLGSQTSSWEKLEKNLSD 798
Cdd:PHA02562 322 IDELEEIMDEFneqskkllelknkiSTNKQSLITLVDKAKK-VKAAIEELQAEFVDNAEELAKLQDELDK 390
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
456-727 |
7.88e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 456 EKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDeftqrIAEAEKKVQLACKERDAAKKEIKNIKeel 535
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE-----YSWDEIDVASAEREIAELEAELERLD--- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 536 atrlnssETADLLKEKDEQIRGLMEEGEKLSKQqlhnsniIKKLRAKdkenenmVAKLNKKVKELEEELQHLKQVLDGKE 615
Cdd:COG4913 682 -------ASSDDLAALEEQLEELEAELEELEEE-------LDELKGE-------IGRLEKELEQAEEELDELQDRLEAAE 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 616 EVEKQHREniKKLNSMVERQEKDLGRLQVdMDELEEKNRSIQAALDSAYKELTDLHKA------NAAKDSEAQEAALSRE 689
Cdd:COG4913 741 DLARLELR--ALLEERFAAALGDAVEREL-RENLEERIDALRARLNRAEEELERAMRAfnrewpAETADLDADLESLPEY 817
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 110347443 690 MKAKEELSA-ALEKAQEEARQQQETLAIQ-VGDLRLALQR 727
Cdd:COG4913 818 LALLDRLEEdGLPEYEERFKELLNENSIEfVADLLSKLRR 857
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
454-609 |
9.01e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 9.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 454 LNEKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLAC--KERDAAKKEIKNI 531
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEALQKEIESL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110347443 532 KEELAtrlnssetadllkEKDEQIRGLMEEGEKLSKQQlhnSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQ 609
Cdd:COG1579 102 KRRIS-------------DLEDEILELMERIEELEEEL---AELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
548-920 |
1.06e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 548 LKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELqhlkqvldgkEEVEKQHREnIKK 627
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL----------EKLEKEVKE-LEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 628 LNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLhkanaaKDSEAQEAALSREMKAKEELSAALEKAQEEA 707
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL------EEKVKELKELKEKAEEYIKLSEFYEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 708 RQQQETLAIQVGDLRLALQRTEQAAARKEdylrhEIGELQQRLQEAENRNQELSQSVS--STTRPLLRQIENLQATLGSQ 785
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEE-----RLEELKKKLKELEKRLEELEERHElyEEAKAKKEELERLKKRLTGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 786 TSswEKLEKnlsdrlgesqtLLAAAVERERAATEELLANKIQMSSMESQNSLLRQENSRfqaqLESEKNR--LCKLE-DE 862
Cdd:PRK03918 385 TP--EKLEK-----------ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE----LKKAKGKcpVCGRElTE 447
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 110347443 863 NNRyqvelENLKDEYVRTLEETRKEKTLLNSQLEMERMKVEQERKKAIFTQETIKEKE 920
Cdd:PRK03918 448 EHR-----KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKE 500
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
442-730 |
1.32e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 442 SEKEDVCKTVEFLNEKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKER 521
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 522 DAAKKEIKNIKEELatrlnsSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELE 601
Cdd:TIGR04523 471 KVLSRSINKIKQNL------EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 602 EELQHLKQVLDgKEEVEKQHRENIKKLNSMVERQekdlgrlqvdmDELEEKNRSIQAALDSAYKELTDLHKanaakdsea 681
Cdd:TIGR04523 545 DELNKDDFELK-KENLEKEIDEKNKEIEELKQTQ-----------KSLKKKQEEKQELIDQKEKEKKDLIK--------- 603
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 110347443 682 qeaalsrEMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQ 730
Cdd:TIGR04523 604 -------EIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQ 645
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
422-635 |
1.56e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 422 TVLDKVAEQCEPAESQPEALSEKEDVCKTVEF--LNEKLEKREAQLLS----------LSKEKALLEEAFDNLKDEMFRV 489
Cdd:PRK03918 496 IKLKELAEQLKELEEKLKKYNLEELEKKAEEYekLKEKLIKLKGEIKSlkkelekleeLKKKLAELEKKLDELEEELAEL 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 490 KEESSSIS-SLKDEFTQRIAEAEK------KVQLACKERDAAKKEIKNIKEEL-ATRLNSSETADLLKEKDEQIRGLM-- 559
Cdd:PRK03918 576 LKELEELGfESVEELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELdKAFEELAETEKRLEELRKELEELEkk 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 560 ---EEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVldgKEEVEK---------QHRENIKK 627
Cdd:PRK03918 656 yseEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA---KKELEKlekalerveELREKVKK 732
|
....*...
gi 110347443 628 LNSMVERQ 635
Cdd:PRK03918 733 YKALLKER 740
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
574-720 |
1.58e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 574 NIIKKLRA---KDKEN-ENMVAKLNKKVKELEEELQHLKQVLdgkEEVEKQHREnikklnsmVERQekdlgrlqvdMDEL 649
Cdd:PRK00409 502 NIIEEAKKligEDKEKlNELIASLEELERELEQKAEEAEALL---KEAEKLKEE--------LEEK----------KEKL 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 650 EEKNRSIQAALDSAYKELTDLHKANAA---KDSEAQEAALSREMKAKE------ELSAALEKAQEEAR-QQQETLAIQVG 719
Cdd:PRK00409 561 QEEEDKLLEEAEKEAQQAIKEAKKEADeiiKELRQLQKGGYASVKAHEliearkRLNKANEKKEKKKKkQKEKQEELKVG 640
|
.
gi 110347443 720 D 720
Cdd:PRK00409 641 D 641
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
468-753 |
1.64e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 45.79 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 468 LSKEKALLEEAFDNLKDemfrVKEEsssISSLKDEFTQRIAEAEKKVQLACkERDAAKKEIKNIKEELATRLNSsetadl 547
Cdd:pfam05701 126 LEVAKARHAAAVAELKS----VKEE---LESLRKEYASLVSERDIAIKRAE-EAVSASKEIEKTVEELTIELIA------ 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 548 LKEKDEQIRGLMEEGEKlskqqlhnsniiKKLRAKDKENENMVaKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKK 627
Cdd:pfam05701 192 TKESLESAHAAHLEAEE------------HRIGAALAREQDKL-NWEKELKQAEEELQRLNQQLLSAKDLKSKLETASAL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 628 LNSM----VERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLhKANAAKdsEAQEAALSRemKAKEELSAALEKA 703
Cdd:pfam05701 259 LLDLkaelAAYMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEV-KANIEK--AKDEVNCLR--VAAASLRSELEKE 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 110347443 704 QEE--ARQQQETLA-IQVGDLRLALQRTEQ---AAARKEDYLRHEIGELQQRLQEA 753
Cdd:pfam05701 334 KAElaSLRQREGMAsIAVSSLEAELNRTKSeiaLVQAKEKEAREKMVELPKQLQQA 389
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
482-708 |
1.66e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 482 LKDEMFRVKEESSSISSLKDEFT------QRIAEAEKKVQL------ACKERDAAKKEIkNIKEELATRLN---SSETAD 546
Cdd:COG4913 213 VREYMLEEPDTFEAADALVEHFDdlerahEALEDAREQIELlepireLAERYAAARERL-AELEYLRAALRlwfAQRRLE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 547 LLKEK----DEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENmvaklnKKVKELEEELQHLKQVLDGKEEVEKQHR 622
Cdd:COG4913 292 LLEAEleelRAELARLEAELERLEARLDALREELDELEAQIRGNGG------DRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 623 ENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKEL-TDLHKANAAKDSEAQE-AAL--------SREMKA 692
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAeAALRDLRRELRELEAEiASLerrksnipARLLAL 445
|
250
....*....|....*.
gi 110347443 693 KEELSAALEKAQEEAR 708
Cdd:COG4913 446 RDALAEALGLDEAELP 461
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
449-922 |
1.92e-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: 45.73 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 449 KTVEFLNEKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEI 528
Cdd:pfam02463 265 EKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKEL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 529 KNIKEELATRLNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIK-KLRAKDKENENMVAKLNKKVKELEEELQHL 607
Cdd:pfam02463 345 KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKeEELELKSEEEKEAQLLLELARQLEDLLKEE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 608 KQVLDGKEEvEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSI-------------QAALDSAYKELTDLHKAN 674
Cdd:pfam02463 425 KKEELEILE-EEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDllketqlvklqeqLELLLSRQKLEERSQKES 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 675 AAKDSEAQEAALSREMK------------AKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHE 742
Cdd:pfam02463 504 KARSGLKVLLALIKDGVggriisahgrlgDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLL 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 743 IGELQQRLQEAENRNQELSQSVSSTTRPLLRQIENLQATLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELL 822
Cdd:pfam02463 584 IPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSE 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 823 ANKI-QMSSMESQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEYVRTLEETRKEKTLLNSQ----LEM 897
Cdd:pfam02463 664 VKASlSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEelklLKQ 743
|
490 500
....*....|....*....|....*
gi 110347443 898 ERMKVEQERKKAIFTQETIKEKERK 922
Cdd:pfam02463 744 KIDEEEEEEEKSRLKKEEKEEEKSE 768
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
553-802 |
1.99e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 44.25 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 553 EQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGK----EEVEKQHRENIKKL 628
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEAleklEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 629 NSMVERQEKDlgrlqvdmdelEEKNRSIQAALDSAykeltdlhkANAAKDSEAQEAALSREMKakeELSAALEKAQEEAR 708
Cdd:pfam00261 81 KVLENRALKD-----------EEKMEILEAQLKEA---------KEIAEEADRKYEEVARKLV---VVEGDLERAEERAE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 709 QQQETLAIQVGDLRLA------LQRTEQAAARKEDYLRHEIGELQQRLQEAENRNQELSQSVSsttrPLLRQIENLQATL 782
Cdd:pfam00261 138 LAESKIVELEEELKVVgnnlksLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQ----KLEKEVDRLEDEL 213
|
250 260
....*....|....*....|
gi 110347443 783 GSQTSSWEKLEKNLSDRLGE 802
Cdd:pfam00261 214 EAEKEKYKAISEELDQTLAE 233
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
583-922 |
2.09e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 583 DKENENMVAKLNkkvkELEEELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLqvdmDELEEKNRSIQAALDS 662
Cdd:PRK02224 198 EKEEKDLHERLN----GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL----ETLEAEIEDLRETIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 663 AYKELTDLhkanAAKDSEAQEAALSREMKAKEELS-AALEKAQEEA-RQQQETLAIQVGDLRLAL--QRTEQAAARKE-D 737
Cdd:PRK02224 270 TEREREEL----AEEVRDLRERLEELEEERDDLLAeAGLDDADAEAvEARREELEDRDEELRDRLeeCRVAAQAHNEEaE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 738 YLRHEIGELQQRLQEAENRNQELSQSVSSTTRP----------LLRQIENLQATLGSQTSSWEKLE-------------- 793
Cdd:PRK02224 346 SLREDADDLEERAEELREEAAELESELEEAREAvedrreeieeLEEEIEELRERFGDAPVDLGNAEdfleelreerdelr 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 794 ----------KNLSDRLGESQTLLAA-------AVERERAATEELLANKIQMSSMESQNSLLRQENSRFQAQLESEKNrL 856
Cdd:PRK02224 426 ereaeleatlRTARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED-L 504
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110347443 857 CKLEDENNRYQVELENLK----------DEYVRTLEETRKEKTLLNSQLEMERMKVEQERKKAIFTQETIKEKERK 922
Cdd:PRK02224 505 VEAEDRIERLEERREDLEeliaerretiEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSK 580
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
442-922 |
2.26e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 442 SEKEDVCKTVEFLNEKLEKREaqlLSLSKEKALLEEAFDNLKD--EMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACK 519
Cdd:pfam10174 123 SEHERQAKELFLLRKTLEEME---LRIETQKQTLGARDESIKKllEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEV 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 520 ERDAAKKEIKNIKEELATRL----NSSETADL---LKEKDEQI-------RGLMEEGEKLSKQQLHNSNI----IKKL-- 579
Cdd:pfam10174 200 LLDQKEKENIHLREELHRRNqlqpDPAKTKALqtvIEMKDTKIsslerniRDLEDEVQMLKTNGLLHTEDreeeIKQMev 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 580 -RAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQA 658
Cdd:pfam10174 280 yKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKES 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 659 ALDSAYKELTDLhkaNAAKDSEAQEAALSREM-KAKEELSAALEKAQEEARQQQETLAIQVGDLR--------------L 723
Cdd:pfam10174 360 FLNKKTKQLQDL---TEEKSTLAGEIRDLKDMlDVKERKINVLQKKIENLQEQLRDKDKQLAGLKervkslqtdssntdT 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 724 ALQRTEQAAARKE---DYLRHEIG-ELQQRLQEAEN---RNQELSQSVSSTTRPLLRQ---IENLQATLGSQTSSWEK-- 791
Cdd:pfam10174 437 ALTTLEEALSEKEriiERLKEQRErEDRERLEELESlkkENKDLKEKVSALQPELTEKessLIDLKEHASSLASSGLKkd 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 792 ---------LEKNLSDRLGESQTLLAAAVERERAATEELLANKIQmsSMESQNSLLRQENSRFQAQLESEKNRLCKLEDE 862
Cdd:pfam10174 517 sklksleiaVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIR--LLEQEVARYKEESGKAQAEVERLLGILREVENE 594
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 863 NNRYQVELENLKDEYVRTLEETRKEKTLLNSQLEMERMKVEQERKKAIFTQETIKEKERK 922
Cdd:pfam10174 595 KNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQ 654
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
721-913 |
2.32e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 721 LRLALQRTEQAAARKEDYLRHEIGELQQRLQEAEN-----RNQELSQSVSSTTRPLLRQIENL-------QATLGSQTSS 788
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAaleefRQKNGLVDLSEEAKLLLQQLSELesqlaeaRAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 789 WEKLEKNLSDRLGESQTLLAAAVERERAATE-ELLANKIQMSSMESQNS----LLRQENSRFQAQLESEKNRLckLEDEN 863
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQQLRAQLaELEAELAELSARYTPNHpdviALRAQIAALRAQLQQEAQRI--LASLE 319
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 110347443 864 NRYQVeLENLKDEYVRTLEETRKE-KTLLNSQLEMERMKVEQERKKAIFTQ 913
Cdd:COG3206 320 AELEA-LQAREASLQAQLAQLEARlAELPELEAELRRLEREVEVARELYES 369
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
451-880 |
3.56e-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: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 451 VEFLNEKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKeesssisslkdefTQRIAEAEKKVQLACKERDAAKKEIKN 530
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNG-------------GDRLEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 531 IKEELAT-RLNSSETADLLKEKDEQIRGLMEEGEKLSKQqlhnsniikkLRAKDKENENMVAKLNKKVKELEEELQHLK- 608
Cdd:COG4913 364 LEALLAAlGLPLPASAEEFAALRAEAAALLEALEEELEA----------LEEALAEAEAALRDLRRELRELEAEIASLEr 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 609 ----------------------------------QVLDGKEE-----------------VEKQH-RENIKKLNSM----- 631
Cdd:COG4913 434 rksniparllalrdalaealgldeaelpfvgeliEVRPEEERwrgaiervlggfaltllVPPEHyAAALRWVNRLhlrgr 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 632 -----VERQEKDLGRLQVDMD----ELEEKNRSIQAALDSAYKELTDLHKANAAK------------------------- 677
Cdd:COG4913 514 lvyerVRTGLPDPERPRLDPDslagKLDFKPHPFRAWLEAELGRRFDYVCVDSPEelrrhpraitragqvkgngtrhekd 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 678 -------------DSEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAiqvgDLRLALQRTEQAAARKED--YLRHE 742
Cdd:COG4913 594 drrrirsryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQ----ERREALQRLAEYSWDEIDvaSAERE 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 743 IGELQQRLQEAENRNQELSQsvssttrpLLRQIENLQATLGSQTSSWEKLE----------KNLSDRLGESQTLLAAAVE 812
Cdd:COG4913 670 IAELEAELERLDASSDDLAA--------LEEQLEELEAELEELEEELDELKgeigrlekelEQAEEELDELQDRLEAAED 741
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110347443 813 RERAATEELLANKIqmssmesQNSLLRQENSRFQAQLEsekNRLCKLEDENNRYQVELENLKDEYVRT 880
Cdd:COG4913 742 LARLELRALLEERF-------AAALGDAVERELRENLE---ERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
647-759 |
3.92e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 647 DELEEKNRSIQaaldsaykELTD---LHKANAAkDSEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRL 723
Cdd:PRK09039 53 SALDRLNSQIA--------ELADllsLERQGNQ-DLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQ 123
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 110347443 724 AL----QRTEQAAARKEDY------LRHEIGELQQRLQEAENRNQE 759
Cdd:PRK09039 124 ELdsekQVSARALAQVELLnqqiaaLRRQLAALEAALDASEKRDRE 169
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
519-668 |
4.11e-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: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 519 KERDAAKKEIKNIKEELAtrlnssETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENEN--MVAKLNKK 596
Cdd:COG1579 17 SELDRLEHRLKELPAELA------ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110347443 597 VKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELT 668
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
438-568 |
4.83e-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: 42.99 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 438 PEALSEKEDvckTVEFLNEKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLK---------DEFTQRIA 508
Cdd:COG1579 30 PAELAELED---ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyealqkeiESLKRRIS 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 509 EAEKKVQLACKERDAAKKEIKNIKEELATRlnSSETADLLKEKDEQIRGLMEEGEKLSKQ 568
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAEL--EAELEEKKAELDEELAELEAELEELEAE 164
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
500-787 |
6.28e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.52 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 500 KDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEELATRLNSSETADLLKEKDEQIRGLMEEgekLSKQQLHNSNIIKKL 579
Cdd:pfam05622 9 KDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQ---LQEENFRLETARDDY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 580 RAKDKENENMVAKLNKKVKELE---EELQHLKQVLDgkeeVEKQHRENIKKLNSMVERQEK---DLGRLQVDMDELEEKN 653
Cdd:pfam05622 86 RIKCEELEKEVLELQHRNEELTslaEEAQALKDEMD----ILRESSDKVKKLEATVETYKKkleDLGDLRRQVKLLEERN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 654 -----------------RSIQAALDSAYKELTDLHKANAAKDSEAQEAALsrEMKAKEELSAALEKAQEEARQQQETLAI 716
Cdd:pfam05622 162 aeymqrtlqleeelkkaNALRGQLETYKRQVQELHGKLSEESKKADKLEF--EYKKLEEKLEALQKEKERLIIERDTLRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 717 QVGDLRLA-LQRTEQAAA---------------------------------------RKEDYLRHEIGELQQRLQEAENR 756
Cdd:pfam05622 240 TNEELRCAqLQQAELSQAdallspssdpgdnlaaeimpaeireklirlqhenkmlrlGQEGSYRERLTELQQLLEDANRR 319
|
330 340 350
....*....|....*....|....*....|....
gi 110347443 757 NQEL-SQSVSSTTRPLL--RQIENLQATLGSQTS 787
Cdd:pfam05622 320 KNELeTQNRLANQRILElqQQVEELQKALQEQGS 353
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
459-667 |
6.39e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.91 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 459 EKREAQLLSLSKEKALLEEA--FDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVqlackeRDAAKKEIKN--IKEE 534
Cdd:COG5022 855 LKAKKRFSLLKKETIYLQSAqrVELAERQLQELKIDVKSISSLKLVNLELESEIIELK------KSLSSDLIENleFKTE 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 535 LATRL-------NSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHL 607
Cdd:COG5022 929 LIARLkkllnniDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQY 1008
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110347443 608 KQVLDGKEEVEKQHREN--IKKLNSMVERQEKDLGRLQvDMDELEEKNRSIQAALDSAYKEL 667
Cdd:COG5022 1009 GALQESTKQLKELPVEVaeLQSASKIISSESTELSILK-PLQKLKGLLLLENNQLQARYKAL 1069
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
584-918 |
8.64e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 584 KENENMVAKLNKKvKELEEELQHLKQVLdgkeevekqhrENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAaldsa 663
Cdd:PRK11281 39 ADVQAQLDALNKQ-KLLEAEDKLVQQDL-----------EQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQA----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 664 ykELTDLhKANAAKDSEAQEAALSRemkakEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAArkedylrhEI 743
Cdd:PRK11281 102 --ELEAL-KDDNDEETRETLSTLSL-----RQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQA--------AL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 744 GELQQRLQEAENR--NQELSQSVSSTTRPLLRQIEnlQATLGSQTSSWEKLEKN---LSDrLGESQTLLAAAVERERAAT 818
Cdd:PRK11281 166 YANSQRLQQIRNLlkGGKVGGKALRPSQRVLLQAE--QALLNAQNDLQRKSLEGntqLQD-LLQKQRDYLTARIQRLEHQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 819 EELLANKIqmssmeSQNSLLRQENSRFQAQLESEKNRLckleDENNRYQVELE-NLK-DEYVrtLEETRKektlLNsQLE 896
Cdd:PRK11281 243 LQLLQEAI------NSKRLTLSEKTVQEAQSQDEAARI----QANPLVAQELEiNLQlSQRL--LKATEK----LN-TLT 305
|
330 340
....*....|....*....|..
gi 110347443 897 MERMKVEQERKKAIFTQETIKE 918
Cdd:PRK11281 306 QQNLRVKNWLDRLTQSERNIKE 327
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
486-699 |
8.93e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 8.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 486 MFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDA-AKKEIKNIKEELATRLNSSEtadllKEKDEQIRGLMEEGEK 564
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFEKELRERR-----NELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 565 LSKQQlhnsniiKKLRAKDKENENMVAKLNKKVKELEEelqhLKQVLDGKEEVEKQHRENIKKLNSMVERQEKdlgrlqv 644
Cdd:PRK12704 98 LDRKL-------ELLEKREEELEKKEKELEQKQQELEK----KEEELEELIEEQLQELERISGLTAEEAKEIL------- 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 110347443 645 dMDELEEKNRSIQAALDSAYKEltdlhkanaakdsEAQEAAlsrEMKAKEELSAA 699
Cdd:PRK12704 160 -LEKVEEEARHEAAVLIKEIEE-------------EAKEEA---DKKAKEILAQA 197
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
456-712 |
8.94e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 456 EKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEEL 535
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 536 atrlnsSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNK------KVKELEEELQHLKQ 609
Cdd:COG1340 81 ------DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEekelveKIKELEKELEKAKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 610 VLDGKEEVE------KQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLhKANAAKDSEAQE 683
Cdd:COG1340 155 ALEKNEKLKelraelKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEA-QEKADELHEEII 233
|
250 260
....*....|....*....|....*....
gi 110347443 684 AALSREMKAKEELSAALEKAQEEARQQQE 712
Cdd:COG1340 234 ELQKELRELRKELKKLRKKQRALKREKEK 262
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
457-627 |
8.95e-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: 42.22 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 457 KLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQlackerdAAKKEIKNIKEELA 536
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE-------EVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 537 TRLNSSETADLLKEKDEQIRglmeEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEE 616
Cdd:COG1579 84 NVRNNKEYEALQKEIESLKR----RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170
....*....|.
gi 110347443 617 VEKQHRENIKK 627
Cdd:COG1579 160 ELEAEREELAA 170
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
596-714 |
9.28e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 596 KVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQvdmDELEEKNRSIQaaldsAYKEltdlhKANA 675
Cdd:COG2433 386 IEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE---AELEEKDERIE-----RLER-----ELSE 452
|
90 100 110
....*....|....*....|....*....|....*....
gi 110347443 676 AKDSEAQEAALSREMKAKEELSAALEKAQEEARQQQETL 714
Cdd:COG2433 453 ARSEERREIRKDREISRLDREIERLERELEEERERIEEL 491
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
413-722 |
9.36e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 43.30 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 413 SSTPINEGQTVLDKVAEQCEPAESQPEALSEkedvcktvEFLNEKLEKREAQL---LSLSKEKALLEEAFDNLKDEMFRV 489
Cdd:PLN03229 427 VKTPVRELEGEVEKLKEQILKAKESSSKPSE--------LALNEMIEKLKKEIdleYTEAVIAMGLQERLENLREEFSKA 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 490 KEES--------SSISSLKDEFTQRIAEAEKKVQLACK-------ERDAAKKEIKNIKEELATRLNSsetadllKEKDEQ 554
Cdd:PLN03229 499 NSQDqlmhpvlmEKIEKLKDEFNKRLSRAPNYLSLKYKldmlnefSRAKALSEKKSKAEKLKAEINK-------KFKEVM 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 555 IRGLMEEGEKLSKQQLHNSniikKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQhrenikklNSMVER 634
Cdd:PLN03229 572 DRPEIKEKMEALKAEVASS----GASSGDELDDDLKEKVEKMKKEIELELAGVLKSMGLEVIGVTK--------KNKDTA 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 635 QEKDLGRLQVDMDEL-EEKNRSIQAALDSA-YKELTDLHKANAAKDSEAQEAALSREMKA-----KEELSAALEKAqeEA 707
Cdd:PLN03229 640 EQTPPPNLQEKIESLnEEINKKIERVIRSSdLKSKIELLKLEVAKASKTPDVTEKEKIEAleqqiKQKIAEALNSS--EL 717
|
330
....*....|....*
gi 110347443 708 RQQQETLAIQVGDLR 722
Cdd:PLN03229 718 KEKFEELEAELAAAR 732
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
454-671 |
1.04e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 454 LNEKLEKREAQLLSLsKEKAllEEAfDNLKDEMFRVKEE-SSSISSLKDEFTQRIAEAEKKVQlacKERDAAKKEIKNIK 532
Cdd:PRK00409 518 LNELIASLEELEREL-EQKA--EEA-EALLKEAEKLKEElEEKKEKLQEEEDKLLEEAEKEAQ---QAIKEAKKEADEII 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 533 EELATRLNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDK---ENENMVAKLNKKVKELEEELQ---- 605
Cdd:PRK00409 591 KELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEvkyLSLGQKGEVLSIPDDKEAIVQagim 670
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110347443 606 ----HLKQV-LDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQVDmDELEEKNRSIQAALDSAYKELTDLH 671
Cdd:PRK00409 671 kmkvPLSDLeKIQKPKKKKKKKPKTVKPKPRTVSLELDLRGMRYE-EALERLDKYLDDALLAGYGEVLIIH 740
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
506-760 |
1.08e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 506 RIAEAEKKVQLACKERDAAKKEIKNIKEEL---ATRLNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAK 582
Cdd:COG1196 541 EAALAAALQNIVVEDDEVAAAAIEYLKAAKagrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGD 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 583 DKENENMVAklnkkvkELEEELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRlqvdmdELEEKNRSIQAALDS 662
Cdd:COG1196 621 TLLGRTLVA-------ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA------ALLEAEAELEELAER 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 663 AYKELTDLHKAnaakdsEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHE 742
Cdd:COG1196 688 LAEEELELEEA------LLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
250
....*....|....*...
gi 110347443 743 IGELQQRLQEAENRNQEL 760
Cdd:COG1196 762 LEELERELERLEREIEAL 779
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
599-870 |
1.14e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.81 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 599 ELEEELQHLKQVLDGKEEVEKQHRENIKKLnsmverqEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKD 678
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIEL-------EKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 679 SEAQeaALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKedylRHEIGELQQRLQEAENRNQ 758
Cdd:pfam05557 76 ELNR--LKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQST----NSELEELQERLDLLKAKAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 759 ELSQ------SVSSTTRPLLRQIENLQATLGSQTsSWEKLEKNLSDRLGESQTLLAAAvereraatEELLANKIQMSSME 832
Cdd:pfam05557 150 EAEQlrqnleKQQSSLAEAEQRIKELEFEIQSQE-QDSEIVKNSKSELARIPELEKEL--------ERLREHNKHLNENI 220
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 110347443 833 SQNSLLRQENSRFQAQLESE---KNRLCKLEDENNRYQVEL 870
Cdd:pfam05557 221 ENKLLLKEEVEDLKRKLEREekyREEAATLELEKEKLEQEL 261
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
624-715 |
1.15e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 42.41 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 624 NIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKA-NAAKDSEAQEAAlsremKAKEELSAALEK 702
Cdd:TIGR04320 255 SLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKElANAQAQALQTAQ-----NNLATAQAALAN 329
|
90
....*....|...
gi 110347443 703 AQEEARQQQETLA 715
Cdd:TIGR04320 330 AEARLAKAKEALA 342
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
451-919 |
1.16e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 451 VEFLNEKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDE---FTQRIAEAEKKVQLACKERDaakkE 527
Cdd:PRK01156 199 LENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMknrYESEIKTAESDLSMELEKNN----Y 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 528 IKNIKEELATRLNSSETA-------------------DLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDkenen 588
Cdd:PRK01156 275 YKELEERHMKIINDPVYKnrnyindyfkykndienkkQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYD----- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 589 mvaKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELT 668
Cdd:PRK01156 350 ---DLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVS 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 669 DLhkaNAAKDSEAQ-EAALSREMKAKEELSA----ALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEI 743
Cdd:PRK01156 427 SL---NQRIRALREnLDELSRNMEMLNGQSVcpvcGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLK 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 744 gELQQRLQEAENRNQELSQSVSSTTRPLLRQIENLQATLGSQTSSWEKLEKNLsdrlgesqtllaaaverERAATEELLA 823
Cdd:PRK01156 504 -KRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRY-----------------KSLKLEDLDS 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 824 NKIQMSSMESQNSLLRQENSRfqAQLESEKNRLCKLEDENNRYQVELENLK----------DEYVRTLEETRKEKTLLNS 893
Cdd:PRK01156 566 KRTSWLNALAVISLIDIETNR--SRSNEIKKQLNDLESRLQEIEIGFPDDKsyidksireiENEANNLNNKYNEIQENKI 643
|
490 500
....*....|....*....|....*.
gi 110347443 894 QLEMERMKVEQERKKAIFTQETIKEK 919
Cdd:PRK01156 644 LIEKLRGKIDNYKKQIAEIDSIIPDL 669
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
569-933 |
1.24e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.64 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 569 QLHNSNIIKKLRAKDKENENMVAKLnKKVKELEEELQHLKQVLDGKEEVEKQ-----------HRENIKKLNSMVERQEK 637
Cdd:COG5185 211 ETGNLGSESTLLEKAKEIINIEEAL-KGFQDPESELEDLAQTSDKLEKLVEQntdlrleklgeNAESSKRLNENANNLIK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 638 DLGRLQVDMDELEEKNrSIQAALDSAYKELTDLH-KANAAKDSEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAI 716
Cdd:COG5185 290 QFENTKEKIAEYTKSI-DIKKATESLEEQLAAAEaEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVG 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 717 QVgdlrlALQRTEQAAARKEDYLRHEIGELQQRLQEAENRNQELSQSVSSTTRPLLRQIENLQATLGSQTSSWEKLEKNL 796
Cdd:COG5185 369 EV-----ELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLL 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 797 SDRLGESQTLLAAAVERERAATEEllANKIQMSSMESQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDE 876
Cdd:COG5185 444 NELISELNKVMREADEESQSRLEE--AYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQ 521
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 110347443 877 YVRTLEETRKEKTLLNSQLEmermkvEQERKKAIFTQETIKEKERKPFSVSSTPTMS 933
Cdd:COG5185 522 VAESLKDFMRARGYAHILAL------ENLIPASELIQASNAKTDGQAANLRTAVIDE 572
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
454-799 |
1.27e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 42.69 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 454 LNEKLEKREAQLLSLSKEKalLEEAFDNLKDEMFRVKEEsssisslkdeftqrIAEAEKKVQlackerdAAKKEIKNIKE 533
Cdd:NF033838 104 LNVLKEKSEAELTSKTKKE--LDAAFEQFKKDTLEPGKK--------------VAEATKKVE-------EAEKKAKDQKE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 534 ELATRLNSSETADLLKEKDEQIRGLMEEGEKLSKQQlhnsniikklrAKDKENENMVAKLNKKVKELEEELQHLKQVLDG 613
Cdd:NF033838 161 EDRRNYPTNTYKTLELEIAESDVEVKKAELELVKEE-----------AKEPRDEEKIKQAKAKVESKKAEATRLEKIKTD 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 614 KEEVEKQHREnikklnsMVERQEKDLGRLQVDMDELEE-KNRSIQAALDSAYKELTDLHKANAAKDSEAQEAALSREMKA 692
Cdd:NF033838 230 REKAEEEAKR-------RADAKLKEAVEKNVATSEQDKpKRRAKRGVLGEPATPDKKENDAKSSDSSVGEETLPSPSLKP 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 693 KEELSAAlEKAQEEARQQQEtlaiqvgDLRLALQRTEQAAARKEdyLRHEIGELQQRLQEAEnrnQELSQSVSSTTRPlL 772
Cdd:NF033838 303 EKKVAEA-EKKVEEAKKKAK-------DQKEEDRRNYPTNTYKT--LELEIAESDVKVKEAE---LELVKEEAKEPRN-E 368
|
330 340
....*....|....*....|....*..
gi 110347443 773 RQIENLQATLGSQTSSWEKLEKNLSDR 799
Cdd:NF033838 369 EKIKQAKAKVESKKAEATRLEKIKTDR 395
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
462-908 |
1.41e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 462 EAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAA------KKEIKNIKEEL 535
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEEsdlerlKEEIEKSSKQR 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 536 ATRLNSSETAD-LLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGK 614
Cdd:TIGR00606 656 AMLAGATAVYSqFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGR 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 615 EEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDL----HKANAAKDSEAQEAALSREM 690
Cdd:TIGR00606 736 QSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVtimeRFQMELKDVERKIAQQAAKL 815
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 691 KAKeELSAALEKAQEEARQQQETLAIQVGDLRLaLQRTEQAAARKEDYLRHEIGELQ-QRLQEAENRNQelSQSVSSTTR 769
Cdd:TIGR00606 816 QGS-DLDRTVQQVNQEKQEKQHELDTVVSKIEL-NRKLIQDQQEQIQHLKSKTNELKsEKLQIGTNLQR--RQQFEEQLV 891
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 770 PLLRQIENLQATLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSS----MESQNSLLRQENSRF 845
Cdd:TIGR00606 892 ELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNihgyMKDIENKIQDGKDDY 971
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110347443 846 QAQLESEKNRLCKLEDENNRYQVELENLKDEYVRTLEETRKEKTLLNSQLemERMKVEQERKK 908
Cdd:TIGR00606 972 LKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNL--TLRKRENELKE 1032
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
576-795 |
1.42e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 576 IKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRS 655
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 656 IQAALDSayKELTDLHkanaakdseAQEAALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAArk 735
Cdd:COG3883 105 LDVLLGS--ESFSDFL---------DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA-- 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 736 edylrheigELQQRLQEAENRNQELSQSVSSTTRPLLRQIENLQATLGSQTSSWEKLEKN 795
Cdd:COG3883 172 ---------ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
538-660 |
1.43e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 538 RLNSSETADLLKEKDEQIRGLMEEGEKLSKQQlhnsniikklrakDKENENMVAKLNKKVKELEEELQHLKQvldgKEEV 617
Cdd:COG0542 403 RMEIDSKPEELDELERRLEQLEIEKEALKKEQ-------------DEASFERLAELRDELAELEEELEALKA----RWEA 465
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 110347443 618 EKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAAL 660
Cdd:COG0542 466 EKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLL 508
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
394-949 |
1.89e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.73 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 394 EESGRSATPVNCEQPDILVSSTPINEGQTVLDKVAEQCEPAESQPEA-LSEKEDVCKTVEFLN--EKLEKREAQLLSLSK 470
Cdd:TIGR01612 1104 EENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAqINDLEDVADKAISNDdpEEIEKKIENIVTKID 1183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 471 EKALLEEAFDNLKDEMFRVKEESSSISSLKD-----------EFTQRIAEAEKKVQLACKERDAAKKEIKNIKE------ 533
Cdd:TIGR01612 1184 KKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGinlsygknlgkLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEkspeie 1263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 534 -----------ELATrLNSSETAD-----LLKEKDEQIRGLMEEGEKLSKQQLHNSNI--IKK-LRAKDKENENMVAKLN 594
Cdd:TIGR01612 1264 nemgiemdikaEMET-FNISHDDDkdhhiISKKHDENISDIREKSLKIIEDFSEESDIndIKKeLQKNLLDAQKHNSDIN 1342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 595 KKVKELEE-----ELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDeLEEKNRSIQAALDSayKELTD 669
Cdd:TIGR01612 1343 LYLNEIANiynilKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDIN-LEECKSKIESTLDD--KDIDE 1419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 670 LHKanaaKDSEAQEAALSREMKAKEELsaalekaqEEARQQQETLAIQVGDLRLALQRTEQAAARKEDY----LRHEIGE 745
Cdd:TIGR01612 1420 CIK----KIKELKNHILSEESNIDTYF--------KNADENNENVLLLFKNIEMADNKSQHILKIKKDNatndHDFNINE 1487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 746 LQQRLQEAENRNQELSQSVSST--TRPLLRQIENLQATLGSQTSSWE--------------------KLEKNLSDRLGES 803
Cdd:TIGR01612 1488 LKEHIDKSKGCKDEADKNAKAIekNKELFEQYKKDVTELLNKYSALAiknkfaktkkdseiiikeikDAHKKFILEAEKS 1567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 804 QTLLAAAVERERAATEELLANK--------IQMSSMESQNSLLRQENSRFQAQ-----------------LESEKNRLCK 858
Cdd:TIGR01612 1568 EQKIKEIKKEKFRIEDDAAKNDksnkaaidIQLSLENFENKFLKISDIKKKINdclketesiekkissfsIDSQDTELKE 1647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 859 LEDENNRYQVELENLKDEYvRTLEETRKEKTLLNSQLEMERMKVEQERKK-AIFTQETIKE------KERKPFSVSSTPT 931
Cdd:TIGR01612 1648 NGDNLNSLQEFLESLKDQK-KNIEDKKKELDELDSEIEKIEIDVDQHKKNyEIGIIEKIKEiaiankEEIESIKELIEPT 1726
|
650
....*....|....*....
gi 110347443 932 MSR-SSSISGVDMAGLQTS 949
Cdd:TIGR01612 1727 IENlISSFNTNDLEGIDPN 1745
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
484-807 |
1.95e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 484 DEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEELATRLnsSETADLLKEKDEQIRGLMEEGE 563
Cdd:pfam07888 20 TDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQR--RELESRVAELKEELRQSREKHE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 564 KLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQ 643
Cdd:pfam07888 98 ELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 644 VDMDELEEKNRSIQAALDSAYKEL---------------TDLHKANAAKDSEAQEAALSREMKAKEELSAALEKAQE--- 705
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLaqrdtqvlqlqdtitTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEglg 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 706 ------------------EARQQQETLAIQVGDLRLA--------------LQRTEQAAARKEDYLRHEIGELQQRLQEA 753
Cdd:pfam07888 258 eelssmaaqrdrtqaelhQARLQAAQLTLQLADASLAlregrarwaqeretLQQSAEADKDRIEKLSAELQRLEERLQEE 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 110347443 754 ENRNQELSQSVSSTTRPLLRQIENLQATLGSQTSSWEKLEKNLSDRLGESQTLL 807
Cdd:pfam07888 338 RMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELL 391
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
455-850 |
1.96e-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: 42.41 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 455 NEKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLkdefTQRIAEAEKKVQlackerdAAKKEIKNIKEE 534
Cdd:pfam15921 457 NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDL----TASLQEKERAIE-------ATNAEITKLRSR 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 535 LATRLNSSETadlLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMV--------------AKLNKKVKEL 600
Cdd:pfam15921 526 VDLKLQELQH---LKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVgqhgrtagamqvekAQLEKEINDR 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 601 EEELQHLKQVLDGKE--------EVEKQHRENIKKLNSMVERQeKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLhK 672
Cdd:pfam15921 603 RLELQEFKILKDKKDakireleaRVSDLELEKVKLVNAGSERL-RAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVL-K 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 673 ANAAKDSEAQEAALSRemkakeeLSAALEKAQEEARQQQETLAIQVGD----LRLALQRTEQAAARkedylRHEIGELQQ 748
Cdd:pfam15921 681 RNFRNKSEEMETTTNK-------LKMQLKSAQSELEQTRNTLKSMEGSdghaMKVAMGMQKQITAK-----RGQIDALQS 748
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 749 RLQEAENrnqelSQSVSSTTRPLLRQIENLQatlgSQTSSWEKLEKNlsDRLGESQTLLAAAVERERAATE-ELLANKIQ 827
Cdd:pfam15921 749 KIQFLEE-----AMTNANKEKHFLKEEKNKL----SQELSTVATEKN--KMAGELEVLRSQERRLKEKVANmEVALDKAS 817
|
410 420
....*....|....*....|...
gi 110347443 828 MSSMESQNSLLRQENSRFQAQLE 850
Cdd:pfam15921 818 LQFAECQDIIQRQEQESVRLKLQ 840
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
477-784 |
2.32e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.20 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 477 EAFDNLKDEMFRVKEESSSISSLK-DEFTQRIAEAEKKVQLACKERDAAKKEIKNI---KEELATRLNSSETAdlLKEKD 552
Cdd:PLN02939 106 EAIAAIDNEQQTNSKDGEQLSDFQlEDLVGMIQNAEKNILLLNQARLQALEDLEKIlteKEALQGKINILEMR--LSETD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 553 EQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLdgkeEVEKQHRENIKKLNSMV 632
Cdd:PLN02939 184 ARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDI----QFLKAELIEVAETEERV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 633 ERQEKDLGRLQVDMDELEEKNRSIQAaldsaykeltdlhkaNAAKDSEAQEAALsreMKAKEELSAALEKAQEEARQQQE 712
Cdd:PLN02939 260 FKLEKERSLLDASLRELESKFIVAQE---------------DVSKLSPLQYDCW---WEKVENLQDLLDRATNQVEKAAL 321
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110347443 713 TLAiQVGDLRLALQRTEQ--AAARKEDYLRHEIGELQQRLQEAENRNQELSQSVSSTTRPLLRQIENLQATLGS 784
Cdd:PLN02939 322 VLD-QNQDLRDKVDKLEAslKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSK 394
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
491-784 |
2.41e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 491 EESSSISSLKDEftqRIAEAEKKVQLACKERDAAKKEIKNIK---EELATRLNSSETADLLKEKDEQIRGLMEegeklsk 567
Cdd:PRK04863 365 EEQNEVVEEADE---QQEENEARAEAAEEEVDELKSQLADYQqalDVQQTRAIQYQQAVQALERAKQLCGLPD------- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 568 qqLHNSNIikklrakdkenENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHR---ENIKKLNSMVERQE-------- 636
Cdd:PRK04863 435 --LTADNA-----------EDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEqayQLVRKIAGEVSRSEawdvarel 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 637 -----------KDLGRLQVDMDELE---EKNRSIQAALDSAYKeltdlhKANAAKDSEAQEAALSREMKAK-EELSAALE 701
Cdd:PRK04863 502 lrrlreqrhlaEQLQQLRMRLSELEqrlRQQQRAERLLAEFCK------RLGKNLDDEDELEQLQEELEARlESLSESVS 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 702 KAQE---EARQQQETLAIQVGDLR------LALQRT-----EQAAARKEDylRHEIGELQQRLQEAENRNQELSQSVSST 767
Cdd:PRK04863 576 EARErrmALRQQLEQLQARIQRLAarapawLAAQDAlarlrEQSGEEFED--SQDVTEYMQQLLERERELTVERDELAAR 653
|
330
....*....|....*..
gi 110347443 768 TRPLLRQIENLQATLGS 784
Cdd:PRK04863 654 KQALDEEIERLSQPGGS 670
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
461-754 |
2.58e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 461 REAQLLSLSKEKALLEEAFDNLKdemFRVKEESSSISSLKD-------------------EFTQRIAEAEKKVQLACKER 521
Cdd:PRK04863 784 REKRIEQLRAEREELAERYATLS---FDVQKLQRLHQAFSRfigshlavafeadpeaelrQLNRRRVELERALADHESQE 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 522 DAAKKEIKNIKEEL---------ATRLNSSETADLLKEKDEQIRGLmEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAK 592
Cdd:PRK04863 861 QQQRSQLEQAKEGLsalnrllprLNLLADETLADRVEEIREQLDEA-EEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQ 939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 593 LNKKVKELEEELQHLKQVLDGKEEVeKQHRENIK---------KLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSA 663
Cdd:PRK04863 940 LKQDYQQAQQTQRDAKQQAFALTEV-VQRRAHFSyedaaemlaKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQY 1018
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 664 YKELTDLHKANAAKDSEAQEaalsremkAKEELSA----ALEKAQEEARQQQETLAiqvGDLRLALQRTEQaAARKEDYL 739
Cdd:PRK04863 1019 NQVLASLKSSYDAKRQMLQE--------LKQELQDlgvpADSGAEERARARRDELH---ARLSANRSRRNQ-LEKQLTFC 1086
|
330
....*....|....*
gi 110347443 740 RHEIGELQQRLQEAE 754
Cdd:PRK04863 1087 EAEMDNLTKKLRKLE 1101
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
475-706 |
2.76e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.13 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 475 LEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIaEAEKKVQLACKERDAAKKEIKNIKEELATRLNSSETadlLKEKDEQ 554
Cdd:PTZ00440 455 LKKSINQLKTLISIMKSFYDLIISEKDSMDSKE-KKESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKN---IEDYYIT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 555 IRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQhrenIKKLNSMVER 634
Cdd:PTZ00440 531 IEGLKNEIEGLIELIKYYLQSIETLIKDEKLKRSMKNDIKNKIKYIEENVDHIKDIISLNDEIDNI----IQQIEELINE 606
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110347443 635 QEKDLGRLQVDMDELEEKNRSIqaaLDSAYKELTDLHKANAAKDSEAQEaALSREMKAKEELSAALEKAQEE 706
Cdd:PTZ00440 607 ALFNKEKFINEKNDLQEKVKYI---LNKFYKGDLQELLDELSHFLDDHK-YLYHEAKSKEDLQTLLNTSKNE 674
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
614-904 |
2.94e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 614 KEEVEKQHREnikkLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSEAQEaaLSREMKAK 693
Cdd:pfam07888 68 REQWERQRRE----LESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRE--LEEDIKTL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 694 EELSAALEKAQEEARQQQETLAIQVGDL---RLALQRTEQAAARKEDYLRHEIGELQQRLQEAENRNQELSQSVSSTTR- 769
Cdd:pfam07888 142 TQRVLERETELERMKERAKKAGAQRKEEeaeRKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQk 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 770 ------------PLLRQIENLQATLGSQTSSWEKLEKNLSDRLGE---SQTLLAAAVERERAATEELLANKIQMSSMESQ 834
Cdd:pfam07888 222 lttahrkeaeneALLEELRSLQERLNASERKVEGLGEELSSMAAQrdrTQAELHQARLQAAQLTLQLADASLALREGRAR 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 835 NSllrQENSRFQAQLESEKNRLCKLEDE--------------NNRYQVELENLKDEYVRTLEETRKEKTLLNSQLEMERM 900
Cdd:pfam07888 302 WA---QERETLQQSAEADKDRIEKLSAElqrleerlqeermeREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQK 378
|
....
gi 110347443 901 KVEQ 904
Cdd:pfam07888 379 EKEQ 382
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
533-908 |
3.24e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 533 EELATRLNSSETADLLKEKDEQIRGLMEEGEklskQQLHNSNIIKKLRAKDK-ENENMVAKLNKKVKELEEELQHLKQVL 611
Cdd:PRK04863 331 QAASDHLNLVQTALRQQEKIERYQADLEELE----ERLEEQNEVVEEADEQQeENEARAEAAEEEVDELKSQLADYQQAL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 612 DGKEEVEKQHRENIKKLnsmvERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDL-HK---ANAAKDSEAQEAALS 687
Cdd:PRK04863 407 DVQQTRAIQYQQAVQAL----ERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLeQKlsvAQAAHSQFEQAYQLV 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 688 REMKAKEELSAALEKAQEEARQQQEtlaiqvgdLRLALQRTEQaaarkedyLRHEIGELQQRLQEaeNRNQElsqsvsst 767
Cdd:PRK04863 483 RKIAGEVSRSEAWDVARELLRRLRE--------QRHLAEQLQQ--------LRMRLSELEQRLRQ--QQRAE-------- 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 768 trpllRQIENLQATLGSQTSSWEKLEKNLSDRlgesqtllaaavereraaTEELLANKIQMSSMESQNSLLRQEnsrfQA 847
Cdd:PRK04863 537 -----RLLAEFCKRLGKNLDDEDELEQLQEEL------------------EARLESLSESVSEARERRMALRQQ----LE 589
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110347443 848 QLESEKNRLCKLEDENNRYQVELENLK-------------DEYVRTLEETRKEKTLLNSQLEMERMKVEQERKK 908
Cdd:PRK04863 590 QLQARIQRLAARAPAWLAAQDALARLReqsgeefedsqdvTEYMQQLLERERELTVERDELAARKQALDEEIER 663
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
723-905 |
3.59e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 723 LALQRTEQAAARkedyLRHEIGELQQRLQEAENRNQELSQSVSSTTRpLLRQIENLQATLGSQTSSWEKLEKNLSDRLGE 802
Cdd:COG1579 10 LDLQELDSELDR----LEHRLKELPAELAELEDELAALEARLEAAKT-ELEDLEKEIKRLELEIEEVEARIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 803 SQTllaaavereraaTEELLANKIQMSSMESQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEYVRTLE 882
Cdd:COG1579 85 VRN------------NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
170 180
....*....|....*....|...
gi 110347443 883 ETRKEKTLLNSQLEMERMKVEQE 905
Cdd:COG1579 153 ELEAELEELEAEREELAAKIPPE 175
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
672-800 |
4.32e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 672 KANAAKDSEAQEAALSR----EMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEIGELQ 747
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRIleeaKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLE 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 110347443 748 QRLQEAENRNQELSQsvssttrpLLRQIENLQATLgsqtsswEKLEKNLSDRL 800
Cdd:PRK12704 107 KREEELEKKEKELEQ--------KQQELEKKEEEL-------EELIEEQLQEL 144
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
441-662 |
4.38e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.04 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 441 LSEKEDVCKTVEFLNEKLEKREAQLLSLSKEKA---LLEEAFDNLKDEMFR------------------VKEESSS---- 495
Cdd:PLN02939 162 LTEKEALQGKINILEMRLSETDARIKLAAQEKIhveILEEQLEKLRNELLIrgateglcvhslskeldvLKEENMLlkdd 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 496 ISSLKDEFTQrIAEAEKKVQLACKERDAAKKEIKnikeELATRLNSSETaDLLKEKDEQIRGLMEEGEKLSKQQLHNSNI 575
Cdd:PLN02939 242 IQFLKAELIE-VAETEERVFKLEKERSLLDASLR----ELESKFIVAQE-DVSKLSPLQYDCWWEKVENLQDLLDRATNQ 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 576 IKKLRAKDKENENmvakLNKKVKELEEELQHLK------QVLDGKEE----VEKQHRENIKKLNSMVERQEKDLGRLQVD 645
Cdd:PLN02939 316 VEKAALVLDQNQD----LRDKVDKLEASLKEANvskfssYKVELLQQklklLEERLQASDHEIHSYIQLYQESIKEFQDT 391
|
250
....*....|....*....
gi 110347443 646 MDEL--EEKNRSIQAALDS 662
Cdd:PLN02939 392 LSKLkeESKKRSLEHPADD 410
|
|
| PRK14473 |
PRK14473 |
F0F1 ATP synthase subunit B; Provisional |
646-752 |
4.55e-03 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 172948 [Multi-domain] Cd Length: 164 Bit Score: 39.14 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 646 MDELEEKNRSIQAALDSAYKELTDLhkANAAKDSEAQEAalsremKAKEELSAALEKAQEEARQQQETLAIQVGdlRLAL 725
Cdd:PRK14473 34 LNLLNERTRRIEESLRDAEKVREQL--ANAKRDYEAELA------KARQEAAKIVAQAQERARAQEAEIIAQAR--REAE 103
|
90 100
....*....|....*....|....*..
gi 110347443 726 QRTEQAAARKEDYLRHEIGELQQRLQE 752
Cdd:PRK14473 104 KIKEEARAQAEQERQRMLSELKSQIAD 130
|
|
| Seryl_tRNA_N |
pfam02403 |
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ... |
531-612 |
4.95e-03 |
|
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA synthetase class II domain (pfam00587) and represents the N-terminal domain of seryl-tRNA synthetase.
Pssm-ID: 426757 [Multi-domain] Cd Length: 108 Bit Score: 37.95 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 531 IKEELATRLNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVA---KLNKKVKELEEELQHL 607
Cdd:pfam02403 14 VKESLKKRGVDVLDVDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKKEDADALIAevkELKDELKALEAELKEL 93
|
....*
gi 110347443 608 KQVLD 612
Cdd:pfam02403 94 EAELD 98
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
461-755 |
5.33e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 461 REAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKkvqlACKERDAAKKEIKNIKEELATRLN 540
Cdd:pfam01576 634 KETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELER----SKRALEQQVEEMKTQLEELEDELQ 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 541 SSETADL----------------LKEKDE-----------QIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKL 593
Cdd:pfam01576 710 ATEDAKLrlevnmqalkaqferdLQARDEqgeekrrqlvkQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAA 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 594 NK--------------KVKELEEELQHLKQvldGKEEVEKQHRENIKKLNSMverqEKDLGRLQVDMDELEEKNRSIQAA 659
Cdd:pfam01576 790 NKgreeavkqlkklqaQMKDLQRELEEARA---SRDEILAQSKESEKKLKNL----EAELLQLQEDLAASERARRQAQQE 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 660 LDSAYKELTDLHKANAA-----KDSEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAAR 734
Cdd:pfam01576 863 RDELADEIASGASGKSAlqdekRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQ 942
|
330 340
....*....|....*....|.
gi 110347443 735 kedyLRHEIGELQQRLQEAEN 755
Cdd:pfam01576 943 ----LERQNKELKAKLQEMEG 959
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
406-1090 |
5.45e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 406 EQPDILVSSTPINEGQTVLDKVAEQCEPAESQPEALSE-----KEDVCKTVEFLNEKLEKREAQLLSLSKEKALLEEAFD 480
Cdd:TIGR00618 164 EKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLrsqllTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 481 NLKDEMFRVKEESSSISSLKDEFTQ---------RIAEAEKKVQLACK-----ERDAAKKEIKNIKEELATRLNSSETaD 546
Cdd:TIGR00618 244 YLTQKREAQEEQLKKQQLLKQLRARieelraqeaVLEETQERINRARKaaplaAHIKAVTQIEQQAQRIHTELQSKMR-S 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 547 LLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDkENENMVAKLNKKVKELEEElQHLKQVLDGKEEVEKQHRENIK 626
Cdd:TIGR00618 323 RAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRD-AHEVATSIREISCQQHTLT-QHIHTLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 627 KLNSMVERQEKDLGRLQVDMDELEEKNRS-IQAALDSAYKELTDLHKANAAKDSEAQEAALSREMKAKEELSAALekAQE 705
Cdd:TIGR00618 401 ELDILQREQATIDTRTSAFRDLQGQLAHAkKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQL--QTK 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 706 EARQQQETLAIQVGDLRLALQRTEQAAARK-------EDYLRHEIGELQQRLQEAENRNQELSQSVSSTTRPLL------ 772
Cdd:TIGR00618 479 EQIHLQETRKKAVVLARLLELQEEPCPLCGscihpnpARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTserkqr 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 773 ----RQIENLQATLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSMESQnsllrQENSRFQAQ 848
Cdd:TIGR00618 559 aslkEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE-----QDLQDVRLH 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 849 LESEKNRLCKLEDENNRYQVELenLKDEYVRTLEETRKEKTLLNSQLEMERMKVEQERKKAIFTQETIKEKERKPFSV-S 927
Cdd:TIGR00618 634 LQQCSQELALKLTALHALQLTL--TQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELeT 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 928 STPTMSRSSSISGVDMAGLQTSFLSQDESHDHSFGpmpisangsnlydavrmgagsSIIENLQSQLKLREGEITHLQLEI 1007
Cdd:TIGR00618 712 HIEEYDREFNEIENASSSLGSDLAAREDALNQSLK---------------------ELMHQARTVLKARTEAHFNNNEEV 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 1008 GNLEKTRSIMAEELVKLTNQNDELEEKVKEIPKLRTQLRDLDQRYNTILQMYGEKAEEAEELRLDLEDVKNMYKTQIDEL 1087
Cdd:TIGR00618 771 TAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQ 850
|
...
gi 110347443 1088 LRQ 1090
Cdd:TIGR00618 851 LLK 853
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
460-596 |
5.83e-03 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 40.78 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 460 KREAQLLSLSKEKALLEEAFDNLKDEM-----FRV--KEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIK 532
Cdd:PTZ00399 501 KAEMKLISLDKKKKQLLQLCDKLRDEWlpnlgIRIedKPDGPSVWKLDDKEELQREKEEKEALKEQKRLRKLKKQEEKKK 580
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110347443 533 EELAT-RLNSSETADLLKEK-------DEQIRGLM-EEGEKLSKQQLhnSNIIKKLRAKDKENENMVAKLNKK 596
Cdd:PTZ00399 581 KELEKlEKAKIPPAEFFKRQedkysafDETGLPTHdADGEEISKKER--KKLSKEYDKQAKLHEEYLAKGGKS 651
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
511-902 |
6.29e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.81 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 511 EKKVQLACKERDAAKKEIK-NIKEELATRLNSSETADLLKEKDEQIRGLMEEGEKLSKqqlhnsniikKLRAK--DKENE 587
Cdd:PRK10929 25 EKQITQELEQAKAAKTPAQaEIVEALQSALNWLEERKGSLERAKQYQQVIDNFPKLSA----------ELRQQlnNERDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 588 NMVAKLNKKVKELEEE-LQHLKQVLDgkeevekQHREnikklnsmvERQEKDLGRLQVD-MDELEEKNRSIQAALDSAYK 665
Cdd:PRK10929 95 PRSVPPNMSTDALEQEiLQVSSQLLE-------KSRQ---------AQQEQDRAREISDsLSQLPQQQTEARRQLNEIER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 666 ELTDLHKANAAKdSEAQEAALSREMKAKEELSAALEKAQ--------------EEARQQQETLAIQVGDLR--LALQR-- 727
Cdd:PRK10929 159 RLQTLGTPNTPL-AQAQLTALQAESAALKALVDELELAQlsannrqelarlrsELAKKRSQQLDAYLQALRnqLNSQRqr 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 728 -TEQAAARKEdYLRHEIGELQQRLQEAENRNQELSQS----------VSSTTRPLLRQIENLQATLGS--QTSSWeklek 794
Cdd:PRK10929 238 eAERALESTE-LLAEQSGDLPKSIVAQFKINRELSQAlnqqaqrmdlIASQQRQAASQTLQVRQALNTlrEQSQW----- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 795 nlsdrLGESQTLlaaavereraaTEELLANKIQMSSMESQNSL------LRQENSRFQAQLEseknrlcKLEDENNRYQV 868
Cdd:PRK10929 312 -----LGVSNAL-----------GEALRAQVARLPEMPKPQQLdtemaqLRVQRLRYEDLLN-------KQPQLRQIRQA 368
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 110347443 869 ELENLKDEYVRTLEE-TRKEKTLLNSQ--------LEMERMKV 902
Cdd:PRK10929 369 DGQPLTAEQNRILDAqLRTQRELLNSLlsggdtliLELTKLKV 411
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
488-781 |
7.31e-03 |
|
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: 40.71 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 488 RVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEELatrlnssetADLLKEKDEQ----------IRG 557
Cdd:COG3096 351 RYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL---------ADYQQALDVQqtraiqyqqaVQA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 558 LMEEGEKLSKQQLHNSNIikklrakdkenENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHR---ENIKKLNSMVER 634
Cdd:COG3096 422 LEKARALCGLPDLTPENA-----------EDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEkayELVCKIAGEVER 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 635 QE-----KDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKAnaakdsEAQEAALSREMKAKEELSAALEKAQEEARQ 709
Cdd:COG3096 491 SQawqtaRELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNA------ERLLEEFCQRIGQQLDAAEELEELLAELEA 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 710 QQETLAIQVGDLRLALQRTEQaaarKEDYLRHEIGELQQR------LQEAENRNQEL-------SQSVSSTTRPLLRQIE 776
Cdd:COG3096 565 QLEELEEQAAEAVEQRSELRQ----QLEQLRARIKELAARapawlaAQDALERLREQsgealadSQEVTAAMQQLLERER 640
|
....*
gi 110347443 777 NLQAT 781
Cdd:COG3096 641 EATVE 645
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
449-736 |
7.69e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 449 KTVEFLNEKLEKREAQLlslskekallEEAFDNLKDemFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEI 528
Cdd:COG3206 175 KALEFLEEQLPELRKEL----------EEAEAALEE--FRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 529 KNIKEELAtrLNSSETADLLKekDEQIRGLMEEGEKLSKQqlhnsniIKKLRAKDKENenmvaklNKKVKELEEELQHLK 608
Cdd:COG3206 243 AALRAQLG--SGPDALPELLQ--SPVIQQLRAQLAELEAE-------LAELSARYTPN-------HPDVIALRAQIAALR 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 609 QvldgkeevekqhrenikklnsmverqekdlgrlqvdmdELEEKNRSIQAALDSAYKELtdlhkanaakdsEAQEAALSR 688
Cdd:COG3206 305 A--------------------------------------QLQQEAQRILASLEAELEAL------------QAREASLQA 334
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 110347443 689 EMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKE 736
Cdd:COG3206 335 QLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
986-1072 |
7.82e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 986 IENLQSQLKLREGEIthlqleIGNLEKTRSIMAEELVKLTNQNDELEEKVKEIPKLRTQLRDLDQRYNTILQMYGEKAEE 1065
Cdd:COG3206 300 IAALRAQLQQEAQRI------LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQR 373
|
....*..
gi 110347443 1066 AEELRLD 1072
Cdd:COG3206 374 LEEARLA 380
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
435-567 |
8.00e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 435 ESQPEALSEKEDVCKTVEFLNEKLEKREAQLLslsKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKV 514
Cdd:PRK12704 61 EAKEEIHKLRNEFEKELRERRNELQKLEKRLL---QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110347443 515 QLACKE--------RDAAKKEI-KNIKEELATrlnssETADLLKEKDEQIRglmEEGEKLSK 567
Cdd:PRK12704 138 EEQLQElerisgltAEEAKEILlEKVEEEARH-----EAAVLIKEIEEEAK---EEADKKAK 191
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
698-984 |
8.82e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 698 AALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDylrhEIGELQQRLQEAENRNQELSQSVSSTTRPLLRQIEN 777
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA----ELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 778 LQATlGSQTSSWEKL--EKNLSDRLGESQTLlaaavereraateellaNKIqmssMESQNSLLRQENSRfQAQLESEKNR 855
Cdd:COG3883 95 LYRS-GGSVSYLDVLlgSESFSDFLDRLSAL-----------------SKI----ADADADLLEELKAD-KAELEAKKAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 856 LCKLEDENNRYQVELENLKDEYVRTLEETRKEKTLLNSQLEMERMKVEQERKKAIFTQETIKEKERKPFSVSSTPTMSRS 935
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 110347443 936 SSISGVDMAGLQTSFLSQDESHDHSFGPMPISANGSNLYDAVRMGAGSS 984
Cdd:COG3883 232 AAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAAS 280
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
488-621 |
9.52e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.06 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347443 488 RVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKE-IKNIKEELatrlnssetADLLKEKDEqirglMEEGEKLS 566
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFErLAELRDEL---------AELEEELEA-----LKARWEAE 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 110347443 567 KQQLHNsniIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLdgKEEVEKQH 621
Cdd:COG0542 467 KELIEE---IQELKEELEQRYGKIPELEKELAELEEELAELAPLL--REEVTEED 516
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