|
Name |
Accession |
Description |
Interval |
E-value |
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
10-184 |
4.53e-73 |
|
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar proteins; Gipie, also called coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing.
Pssm-ID: 411801 Cd Length: 170 Bit Score: 240.89 E-value: 4.53e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 10 RGFLSGSLATWALGLAGLVGEAEESAGGTEEEEEEeeeeGALCTEKRFLRLIDGALLLRVLGIIAPSSRGGLRMvRGRDG 89
Cdd:cd22230 1 EEFMSGALVTWALGFEGLVGEEEDSLGFPEEEEEE----GTLDAEKRFLRLSNGDLLNRVMGIIDPSPRGGPRM-RGDDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 90 PAACRMWNLCHLWGRLRDFYQEELQLLILSPPPDLQTMGCDPFSEEAVDELESILRLLLGASVQCEHRELFIRHIRGLSL 169
Cdd:cd22230 76 PAAHRVQNLHILWGRLRDFYQEELQQLILSPPPDLQVMGRDPFTEEAVQELEKLLRLLLGAAVQCERRELFIRHIQGLDL 155
|
170
....*....|....*
gi 124486839 170 DVQSELAGAIQEVTQ 184
Cdd:cd22230 156 DVQAELAEAIQEVTQ 170
|
|
| HkD_HkRP |
cd22223 |
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, ... |
12-184 |
3.55e-42 |
|
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C (CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration. Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing. All family members contain a conserved globular Hook domain which folds as a variant of the helical calponin homology (CH) domain.
Pssm-ID: 411794 Cd Length: 149 Bit Score: 151.59 E-value: 3.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 12 FLSGSLATWALGLAGLVGEaeesaggteeeeeeeeeegalctEKRFLRLIDGALLLRVLGIIAPSSRGgLRMVRGRDGPA 91
Cdd:cd22223 1 FLSSPLVTWAKTFADDGSA-----------------------ELSYTDLVDGVFLNNVMLQIDPRPFS-EVSNRNVDDDV 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 92 ACRMWNLCHLWGRLRDFYQEELQLLILSPPPDLQTMGCDPFSEEAVDELESILRLLLGASVQCEHRELFIRHIRGLSLDV 171
Cdd:cd22223 57 NARIQNLDLLLRNIKSFYQEVLQQLIVMKLPDILTIGREPESEQSLEELEKLLLLLLGCAVQCERKEEFIERIKNLDLEV 136
|
170
....*....|...
gi 124486839 172 QSELAGAIQEVTQ 184
Cdd:cd22223 137 QHALVACIQEVTD 149
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
733-1302 |
7.65e-27 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 119.27 E-value: 7.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 733 QALRDEVAQLRREVAGLEVK-LQAQAQRLEARSAEalcLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELEA 811
Cdd:COG1196 216 RELKEELKELEAELLLLKLReLEAELEELEAELEE---LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 812 ASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGD 891
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 892 RLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALmELKARALQLEEELIQLRQypvdlATGA 971
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE-ELEEALAELEEEEEEEEE-----ALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 972 RAgprtvETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQEL 1051
Cdd:COG1196 447 AA-----EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1052 HRKLGVLEEEVRAARRAQEETRGQqqallrdhEALVQLQRRQETELEGLLVRHRDLKANmRALELAHRELQGRHEQLQAQ 1131
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALEAALA--------AALQNIVVEDDEVAAAAIEYLKAAKAG-RATFLPLDKIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1132 RANVEAQEVALLAERERLMQDGHRQRGLEEELRRLqnEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQ 1211
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL--VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1212 SQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRR 1291
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
570
....*....|.
gi 124486839 1292 EKQKLVEKIMD 1302
Cdd:COG1196 751 EALEELPEPPD 761
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
57-184 |
1.75e-22 |
|
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration.
Pssm-ID: 411800 Cd Length: 156 Bit Score: 95.24 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 57 FLRLIDGALLLRVLGIIAPSSRGGlRMVRGRDGPAACRMWNLCHLWGRLRDFYQEELQLLILSPPPDLQTMGCDPFSEEA 136
Cdd:cd22229 30 YVALVDGVFLNEVMLQINPKSSNQ-RVNKKVNNDASLRIQNLSILVKQIKLYYQETLQQLIMMSLPNVLVLGRNPLSEQG 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 124486839 137 VDELESILRLLLGASVQCEHRELFIRHIRGLSLDVQSELAGAIQEVTQ 184
Cdd:cd22229 109 TEEMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEVTH 156
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
731-1223 |
4.78e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 97.31 E-value: 4.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 731 EEQALRDEVAQLRREVAglevKLQAQAQRLEARSAEalcLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELE 810
Cdd:COG1196 282 ELEEAQAEEYELLAELA----RLEQDIARLEERRRE---LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 811 AASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELG 890
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 891 DRLEHLQEELEQAALERQKfLQEQENQHQRYRHLEQRLEAELQAASTSKEEALMELKARALQLEEELIQLRQYPVD-LAT 969
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAE-LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvKAA 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 970 GARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQ----------LQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQA 1039
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQnivveddevaAAAIEYLKAAKAGRATFLPLDKIRARAALAAALA 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1040 EKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHR 1119
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1120 ELQGRHEQLQAQRANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLA 1199
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAL 753
|
490 500
....*....|....*....|....
gi 124486839 1200 RLELERAQLEIQSQQLRESNQQLD 1223
Cdd:COG1196 754 EELPEPPDLEELERELERLEREIE 777
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
839-1295 |
8.23e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.54 E-value: 8.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 839 RLRAQVEAAEQ----QVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQ 914
Cdd:COG1196 204 PLERQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 915 ENQHQRYRHLEQRLEaELQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNAT 994
Cdd:COG1196 284 EEAQAEEYELLAELA-RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 995 LVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRG 1074
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1075 QQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVE-----AQEVALLAERERL 1149
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflegVKAALLLAGLRGL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1150 MQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSACRL 1229
Cdd:COG1196 523 AGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD 602
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486839 1230 TTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQK 1295
Cdd:COG1196 603 LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
202-960 |
1.53e-19 |
|
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: 95.51 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 202 VAEELEMQLRSLTGMMSRLARERDLGAQ------RLAELLLEREPAHLLLPEAPANASAEGVsHHLALQLTNAKAQLRRL 275
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKAERYKELKAElrelelALLVLRLEELREELEELQEELKEAEEEL-EELTAELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 276 RQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALRERAG-RLPRLQEELRRCREKLQAAEV- 353
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELEsKLDELAEELAELEEKLEELKEe 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 354 ---FKGQLEEERVLSEALEASKVLLEEQLEvarERSARLHETQRENLLLRTRLGEAHADLDSLRHQLEQLVEENVELELE 430
Cdd:TIGR02168 353 lesLEAELEELEAELEELESRLEELEEQLE---TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 431 LQR------SLEPPPGSPGEASLPGAAPSLQDEVREAEAgRLRAVERENRELRGQLQMLQAQLGSqhplLEEQRENSRQP 504
Cdd:TIGR02168 430 LEEaelkelQAELEELEEELEELQEELERLEEALEELRE-ELEEAEQALDAAERELAQLQARLDS----LERLQENLEGF 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 505 PVPNRDPATPSALHHSPQSPACQI-----GGEGSESLDLPSPASYSDITRSPKCSQAPDSHPELESPLQMVSQDPQTSDQ 579
Cdd:TIGR02168 505 SEGVKALLKNQSGLSGILGVLSELisvdeGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGT 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 580 ALQESDPTVethqcLEKSGHRVPLQSPIVWDPPQGPEVRI-------------EVQELLGETGSREA---PQGELVHKAQ 643
Cdd:TIGR02168 585 EIQGNDREI-----LKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvddldNALELAKKLRPGYRivtLDGDLVRPGG 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 644 VL--------------KQESPKCRPRSAELT-----LREPLKDQKALDRELELSKQQKETGRHEQRPKGLESKLGPQKPQ 704
Cdd:TIGR02168 660 VItggsaktnssilerRREIEELEEKIEELEekiaeLEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 705 QTSEGVPDAWSREEptpgETLVSAIPEEQALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEALCLSEELAQARRTEAEA 784
Cdd:TIGR02168 740 AEVEQLEERIAQLS----KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 785 HQEAEAQAREQARLREAVDTASLELEAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESqvrcHLEE 864
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE----ALAL 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 865 AEREHAEKQALREELEKAVlrgQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALM 944
Cdd:TIGR02168 892 LRSELEELSEELRELESKR---SELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
810
....*....|....*.
gi 124486839 945 ELKARALQLEEELIQL 960
Cdd:TIGR02168 969 EARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
731-1209 |
5.44e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.85 E-value: 5.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 731 EEQALRDEVAQLRREVAglevKLQAQAQRLEARSAEALclsEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELE 810
Cdd:COG1196 310 RRRELEERLEELEEELA----ELEEELEELEEELEELE---EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 811 AASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELG 890
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 891 DRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALMELKARALQLEEELIQLrQYPVDLATG 970
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV-EAAYEAALE 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 971 ARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQE 1050
Cdd:COG1196 542 AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1051 LHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQA 1130
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486839 1131 QRANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLE 1209
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
731-1300 |
2.15e-18 |
|
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: 92.04 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 731 EEQALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELE 810
Cdd:TIGR02168 282 EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 811 AASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLrgQELG 890
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL--KELQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 891 DRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLeaelqaasTSKEEALMELKARALQLEEELIQLRQYPVDLAT- 969
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQAL--------DAAERELAQLQARLDSLERLQENLEGFSEGVKAl 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 970 -GARAGPRTVETQNGRLIEVERNNATLVAekAALQGQLQHLEGQLGSLQGRAQELLLQS--------------------- 1027
Cdd:TIGR02168 512 lKNQSGLSGILGVLSELISVDEGYEAAIE--AALGGRLQAVVVENLNAAKKAIAFLKQNelgrvtflpldsikgteiqgn 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1028 ------------------------------------------QRAQEHSSRLQAEKSMMEMQG----------------- 1048
Cdd:TIGR02168 590 dreilkniegflgvakdlvkfdpklrkalsyllggvlvvddlDNALELAKKLRPGYRIVTLDGdlvrpggvitggsaktn 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1049 ---QELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRH 1125
Cdd:TIGR02168 670 ssiLERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1126 EQLQAQRANVEAQEVALLAERERLMQDGHRqrgLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELER 1205
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAE---AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1206 AQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLH---REQREY 1282
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEelsEELREL 906
|
650
....*....|....*...
gi 124486839 1283 LDQLNALRREKQKLVEKI 1300
Cdd:TIGR02168 907 ESKRSELRRELEELREKL 924
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
12-184 |
2.31e-17 |
|
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) and similar proteins; Protein Daple, also called coiled-coil domain-containing protein 88C (CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling.
Pssm-ID: 411799 Cd Length: 153 Bit Score: 80.74 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 12 FLSGSLATWALGLAGLVGEAEESAGgteeeeeeeeeegalctekRFLRLIDGALLLRVLGIIAPSSRGGlRMVRGRDGPA 91
Cdd:cd22228 1 FLQSPLVTWVKTFGPLGFGSEDKLS-------------------MYMDLVDGVFLNKIMLQIDPRPTNQ-RVNKHVNNDV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 92 ACRMWNLCHLWGRLRDFYQEELQLLILSPPPDLQTMGCDPFSEEAVDELESILRLLLGASVQCEHRELFIRHIRGLSLDV 171
Cdd:cd22228 61 NLRIQNLTILVRHIKTYYQEVLQQLIVMNLPNVLMIGKDPLSGKSMEEIKKMLLLVLGCAVQCERKEEFIERIKQLDIET 140
|
170
....*....|...
gi 124486839 172 QSELAGAIQEVTQ 184
Cdd:cd22228 141 QAAIVSHIQEVTH 153
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
885-1208 |
5.08e-16 |
|
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: 84.34 E-value: 5.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 885 RGQELgDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALMELK---ARALQLEEELIQLR 961
Cdd:TIGR02168 675 RRREI-EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLArleAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 962 QYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEK 1041
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1042 SMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHREL 1121
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1122 QGRHEQLQAQRANVEAQEVALLAERERlmqdghrqrgLEEELRrlqnehERAQMLLAEVSRERGELQGERGELRSRLARL 1201
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDN----------LQERLS------EEYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
....*..
gi 124486839 1202 ELERAQL 1208
Cdd:TIGR02168 978 ENKIKEL 984
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
60-184 |
1.98e-14 |
|
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor proteins, Hook-related proteins and nuclear mitotic apparatus protein (NuMA). They share an N-terminal conserved globular Hook domain, which folds as a variant of the helical calponin homology (CH) domain with an extended alpha-helix. The Hook domain is responsible for the binding of microtubule. The Hook family includes microtubule-binding proteins, Hook1-3. Hook1 is required for spermatid differentiation. Hook2 contributes to the establishment and maintenance of centrosome function. Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking, and is involved in Golgi and endosome transport. Hook proteins are components of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex. The Hook-related protein (HkRP) family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C(CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B(CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. NuMA, also called nuclear mitotic apparatus protein 1, or nuclear matrix protein-22 (NMP-22), or SP-H antigen, is a microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignment and the segregation of chromosomes during mitotic cell division.
Pssm-ID: 411792 Cd Length: 145 Bit Score: 71.92 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 60 LIDGALLLRVLGIIAPSS-RGGLRMVRGRDGPAACRMWNLCHLWGRLRDFYQEEL-QLLILSPPPDLQTMgcdpFSEEAV 137
Cdd:cd22211 23 LSDGVVLAEILSQIDPSYfDSEWLESRDSSDNWVLKLNNLKKLYRSLSKYYREVLgQQLSDLPLPDLSAI----ARDGDE 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 124486839 138 DELESILRLLLGASVQCEHRELFIRHIRGLSLDVQSELAGAIQEVTQ 184
Cdd:cd22211 99 EEIVKLLELVLGAAVQCENKEEYIARIQQLDESTQAELMLIIQEVLE 145
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
863-1218 |
4.09e-14 |
|
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: 77.80 E-value: 4.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 863 EEAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQAalERQKFLQEQENQHQRYRHLeqrleAELQAASTSKEEA 942
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA--ERYQALLKEKREYEGYELL-----KEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 943 LMELKAralqLEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAEK-AALQGQLQHLEGQLGSLQGRAQ 1021
Cdd:TIGR02169 243 ERQLAS----LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1022 ELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLL 1101
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1102 VRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVALLAERERlmqdghrqrgLEEELRRLQNEHERAQMLLAEVS 1181
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED----------KALEIKKQEWKLEQLAADLSKYE 468
|
330 340 350
....*....|....*....|....*....|....*..
gi 124486839 1182 RERGELQGERGELRSRLARLELERAQLEIQSQQLRES 1218
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
616-1328 |
5.57e-14 |
|
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: 77.40 E-value: 5.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 616 EVRIEVQELLGETGSREAPQGELVHKAQVLKQESPKC--RPRSAELTLREPLKDQKALDRELELSKQQKEtgRHEQRPKG 693
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeqQKQILRERLANLERQLEELEAQLEELESKLD--ELAEELAE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 694 LESKLGPQKPQQTSEGVPDAWSREEPTPGETLVSAIPEE-QALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEALCLSE 772
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQlETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 773 ELAQARRteAEAHQEAEAQAREQARLREAVDTASLELEAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQ 852
Cdd:TIGR02168 422 EIEELLK--KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 853 ALES---QVRCHLEEAEREHAEKQAL------REELEKAVLrgQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRH 923
Cdd:TIGR02168 500 NLEGfseGVKALLKNQSGLSGILGVLselisvDEGYEAAIE--AALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLP 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 924 LEQRLEAELQAASTSKEEALMELKARALQLEEELIQLRQ---------YPVD-------------------------LAT 969
Cdd:TIGR02168 578 LDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllggvLVVDdldnalelakklrpgyrivtldgdlVRP 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 970 GARAGPRTVETQNGRLiEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQ 1049
Cdd:TIGR02168 658 GGVITGGSAKTNSSIL-ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1050 ELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQ 1129
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1130 AQRANVEAQEVALLAERERLMQdghRQRGLEEELRRLQNEheraqmlLAEVSRERGELQGERGELRSRLARLELERAQLE 1209
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATER---RLEDLEEQIEELSED-------IESLAAEIEELEELIEELESELEALLNERASLE 886
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1210 IQSQQLRESNQQLDlsacrlttqcelltqlrsaqeeenrqllAEVQALSRENRELLERSLESRDHLHREQREYLDQLNAL 1289
Cdd:TIGR02168 887 EALALLRSELEELS----------------------------EELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
730 740 750
....*....|....*....|....*....|....*....
gi 124486839 1290 RREKQKLVEKIMDQYRVLEPGPLPRTKKGSWLADKVKRL 1328
Cdd:TIGR02168 939 DNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
839-1300 |
5.03e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.18 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 839 RLRAQVEAAEQQVQALEsQVRCHLEEAEREHAEKQALREELEK-----AVLRGQELGDRLEHLQEELEQAALERQKFLQE 913
Cdd:COG4913 239 RAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAAlrlwfAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 914 QENQHQRYRHLEQRL-------EAELQAASTSKEEALMELKARALQLEEELIQLRQYPV----DLATGARAGPRTVETQN 982
Cdd:COG4913 318 LDALREELDELEAQIrgnggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPasaeEFAALRAEAAALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 983 GRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEhssrlqaeksmmemqgqELHRKLGVLEEEV 1062
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD-----------------ALAEALGLDEAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1063 RAA------RRAQEETRGQQQALLRDhealvqlQRRqeteleGLLVRHRDLKANMRALElaHRELQGRHEQLQAQRANVE 1136
Cdd:COG4913 461 PFVgelievRPEEERWRGAIERVLGG-------FAL------TLLVPPEHYAAALRWVN--RLHLRGRLVYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1137 AQEVALLAER--ERLMQDGHRQRG-LEEELRRLQN-----------EHERAQMLLAEV--SRERGELQGERGELR----- 1195
Cdd:COG4913 526 PERPRLDPDSlaGKLDFKPHPFRAwLEAELGRRFDyvcvdspeelrRHPRAITRAGQVkgNGTRHEKDDRRRIRSryvlg 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1196 ----SRLARLELERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEEN--RQLLAEVQALSRENRELLE--- 1266
Cdd:COG4913 606 fdnrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDAssd 685
|
490 500 510
....*....|....*....|....*....|....*..
gi 124486839 1267 --RSLESR-DHLHREQREYLDQLNALRREKQKLVEKI 1300
Cdd:COG4913 686 dlAALEEQlEELEAELEELEEELDELKGEIGRLEKEL 722
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1009-1328 |
5.48e-13 |
|
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: 74.32 E-value: 5.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1009 LEGQLGSLQGRAQelllQSQRAQEHSSRL-QAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALV 1087
Cdd:TIGR02168 198 LERQLKSLERQAE----KAERYKELKAELrELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1088 QLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLMQDGHRqrgLEEELRRLQ 1167
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE---LEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1168 NEHE-------RAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLR 1240
Cdd:TIGR02168 351 EELEsleaeleELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1241 SAQE--------EENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALrREKQKLVEKIMDQYRVLEPGPL 1312
Cdd:TIGR02168 431 EEAElkelqaelEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL-QARLDSLERLQENLEGFSEGVK 509
|
330
....*....|....*.
gi 124486839 1313 PRTKKGSWLADKVKRL 1328
Cdd:TIGR02168 510 ALLKNQSGLSGILGVL 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
839-1100 |
5.57e-13 |
|
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: 74.32 E-value: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 839 RLRAQVEAAEQQVQALESQvrchLEEAEREHAEKQALREELEKAVlrgQELGDRLEHLQEEL-----EQAALERQK-FLQ 912
Cdd:TIGR02168 236 ELREELEELQEELKEAEEE----LEELTAELQELEEKLEELRLEV---SELEEEIEELQKELyalanEISRLEQQKqILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 913 EQENQHQR--------YRHLEQRLEaELQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGARAGPRTVETQNGR 984
Cdd:TIGR02168 309 ERLANLERqleeleaqLEELESKLD-ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 985 LIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELL--LQSQRAQEHSSRLQAEKSMMEMQGQELHR---KLGVLE 1059
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLkkLEEAELKELQAELEELEEELEELQEELERleeALEELR 467
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 124486839 1060 EEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGL 1100
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
876-1259 |
1.82e-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: 72.40 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 876 REELEKAVLRGQELGDRLEHLQEELEqaalERQKFLQEQENQHQRYRHLEQRLEaELQAASTSKEeaLMELKARALQLEE 955
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELE----RQLKSLERQAEKAERYKELKAELR-ELELALLVLR--LEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 956 ELIQLRQypvdlatgaragprtvetqngrlievernnatlvaEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSS 1035
Cdd:TIGR02168 247 ELKEAEE-----------------------------------ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1036 RLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALE 1115
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1116 LAHRELQGRHEQLQAQRANVEAQEVALLAERERLMQDGHRqrgLEEELRRLQNEHE--RAQMLLAEVSRERGELQGERGE 1193
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER---LEDRRERLQQEIEelLKKLEEAELKELQAELEELEEE 448
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486839 1194 LRSRLARLELERAQLEIQSQQLRESNQQLDL---SACRLTTQCELLTQLRSAQEEENRQLLAEVQALSR 1259
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAaerELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| HkD_Hook |
cd22222 |
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ... |
60-182 |
2.32e-12 |
|
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes Hook1-3. Hook1 is a microtubule-binding protein required for spermatid differentiation. Hook2, also a microtubule-binding protein, contributes to the establishment and maintenance of centrosome function. It may function in the positioning or formation of aggresomes, which are pericentriolar accumulations of misfolded proteins, proteasomes and chaperones. Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking. It is involved in Golgi and endosome transport. It acts as a scaffold for the opposite-polarity microtubule-based motors cytoplasmic dynein-1 and the kinesin KIF1C. It may participate in the turnover of the endocytosed scavenger receptor. Hook proteins are components of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex. Hook adaptor proteins share an N-terminal conserved globular Hook domain, which folds as a variant of the helical calponin homology (CH) domain, and contacts the helix alpha1 of dynein light intermediate chain 1 (LIC1) in a hydrophobic groove.
Pssm-ID: 411793 Cd Length: 147 Bit Score: 66.12 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 60 LIDGALLLRVLGIIAPSSRGGLRMVRGRDGPA---ACRMWNLCHLWGRLRDFYQEEL-QLLILSPPPDLQTMG--CDPfs 133
Cdd:cd22222 23 LSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGdnwRLKVSNLKKILKGIVDYYSEVLgQQISGFTMPDVNAIAekEDP-- 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 124486839 134 eeavDELESILRLLLGASVQCEHRELFIRHIRGLSLDVQSELAGAIQEV 182
Cdd:cd22222 101 ----KELGRLLQLVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQEL 145
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
731-1308 |
4.23e-12 |
|
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: 71.25 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 731 EEQALRDEVAQLRREVAGLE---VKLQAQAQRLEARSAEALCLSEELAqarrteaeaHQEAEAQAREQARLREAVDTASL 807
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEeelEKLTEEISELEKRLEEIEQLLEELN---------KKIKDLGEEEQLRVKEKIGELEA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 808 ELEAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQ 887
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 888 ELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLeAELQAASTSKEEALMELKARALQLEEEliqlrqypvdl 967
Cdd:TIGR02169 382 ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL-ADLNAAIAGIEAKINELEEEKEDKALE----------- 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 968 atgaragprtVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQ 1047
Cdd:TIGR02169 450 ----------IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAS 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1048 GQELH---RKLGVLEE------EVRAARRAQ------EETRGQQQALLRDHEA----LVQLQRRQETELEG--------- 1099
Cdd:TIGR02169 520 IQGVHgtvAQLGSVGEryataiEVAAGNRLNnvvvedDAVAKEAIELLKRRKAgratFLPLNKMRDERRDLsilsedgvi 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1100 ------------------------LLVRH----RDLKANMRALEL----------------AHRELQGRHEQLQAQRANV 1135
Cdd:TIGR02169 600 gfavdlvefdpkyepafkyvfgdtLVVEDieaaRRLMGKYRMVTLegelfeksgamtggsrAPRGGILFSRSEPAELQRL 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1136 EAQEVALLAERERLMQDGHRQRG------------------LEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSR 1197
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENrldelsqelsdasrkigeIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1198 LARLELERAQLEIQSQQLREsnQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQAL-SRENRELLERSL--ESRDH 1274
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEE--ALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIeQKLNRLTLEKEYleKEIQE 837
|
650 660 670
....*....|....*....|....*....|....
gi 124486839 1275 LHREQREYLDQLNALRREKQKLVEKIMDQYRVLE 1308
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
261-499 |
4.60e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.12 E-value: 4.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 261 LALQLTNAKAQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQ--AKRAELYREEAEALRERAGRLP--- 335
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEleEAQAEEYELLAELARLEQDIARlee 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 336 -------RLQEELRRCREKLQAAEVFKGQLEEERVLSEALEASKVLLEEQLEVARERSARLHETQREnlLLRTRLGEAHA 408
Cdd:COG1196 310 rrreleeRLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--AEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 409 DLDSLRHQLEQLVEENVELELELQRSLEpppgspgEASLPGAAPSLQDEVREAEAGRLRAVERENRELRGQLQMLQAQLG 488
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLER-------LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250
....*....|.
gi 124486839 489 SQHPLLEEQRE 499
Cdd:COG1196 461 LLELLAELLEE 471
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1103-1303 |
1.08e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1103 RHRDLKANMRALELAHRELqgRHEQLQAQRANVEAQEVALLAERERLMQdghRQRGLEEELRRLQNEHERAQMLLAEVSR 1182
Cdd:COG1196 214 RYRELKEELKELEAELLLL--KLRELEAELEELEAELEELEAELEELEA---ELAELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1183 ERGELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENR 1262
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 124486839 1263 ELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKIMDQ 1303
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
857-1209 |
1.24e-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: 69.71 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 857 QVRCHLEEAEREhaeKQALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEaELQAAS 936
Cdd:TIGR02169 678 RLRERLEGLKRE---LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS-SLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 937 TSKEEALMELKARALQLEEELIQLRQYPVDLAtgARAGPRTVETQNGRLIEVErnnatlvAEKAALQGQLQHLEGQLGSL 1016
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIQAELSKLE-------EEVSRIEARLREIEQKLNRL 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1017 QGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEalvqlqrRQETE 1096
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD-------ELEAQ 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1097 LEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLMQDGHRQ---RGLEEELRRLQNEHERA 1173
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQaelQRVEEEIRALEPVNMLA 977
|
330 340 350
....*....|....*....|....*....|....*.
gi 124486839 1174 QMLLAEVSRERGELQGERgelrsrlARLELERAQLE 1209
Cdd:TIGR02169 978 IQEYEEVLKRLDELKEKR-------AKLEEERKAIL 1006
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
643-1269 |
6.52e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.37 E-value: 6.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 643 QVLKQESPKCRPRSAELTLREPLKDQKALDRELELSKQQKETGRHEQRPKGLESKLgpqkpqQTSEGVPDAWSREEPTPG 722
Cdd:PRK02224 160 QLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESEL------AELDEEIERYEEQREQAR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 723 ETLVSA---IPEEQALRDEVAQLRREVAGLEVKLQAQAQRLEArsaealcLSEELAQARRTEAEAHQeaeaqarEQARLR 799
Cdd:PRK02224 234 ETRDEAdevLEEHEERREELETLEAEIEDLRETIAETEREREE-------LAEEVRDLRERLEELEE-------ERDDLL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 800 EAVDTASLELEAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREEL 879
Cdd:PRK02224 300 AEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAV 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 880 EKAVLRGQELGDRLEHLQEELEQAALERQK---FLQEQENQHQRYRHLEQRLEAELQAASTSKEEalmelkARALQLEEE 956
Cdd:PRK02224 380 EDRREEIEELEEEIEELRERFGDAPVDLGNaedFLEELREERDELREREAELEATLRTARERVEE------AEALLEAGK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 957 LIQLRQyPVDLATGAragpRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEgQLGSLQGRAQELLLQSQRAQEHSSR 1036
Cdd:PRK02224 454 CPECGQ-PVEGSPHV----ETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAE 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1037 LQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLlvrhRDLKANMRALEL 1116
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL----ERIRTLLAAIAD 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1117 AHRELQGRHEQLqAQRANVEAQevallaERERLMQDGHRQRGLEEE-----LRRLQNEHERAQMLLAEVSRERGELQGER 1191
Cdd:PRK02224 604 AEDEIERLREKR-EALAELNDE------RRERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREER 676
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124486839 1192 GELRSRLARLELERAQLEiqsqQLRESNQQLDLSACRLTTQCELLTQLrsaqEEENRQLLAEvqaLSRENRELLERSL 1269
Cdd:PRK02224 677 DDLQAEIGAVENELEELE----ELRERREALENRVEALEALYDEAEEL----ESMYGDLRAE---LRQRNVETLERML 743
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
770-1135 |
1.46e-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: 66.24 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 770 LSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELEAASrerealaealaaagRERRQWERDGPRLRAQVEAAEQ 849
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAS--------------RKIGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 850 QVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQAAL-ERQKFLQEQENQHQRYRHLEQRL 928
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 929 EAELQAASTSKEEALMELKaralQLEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQH 1008
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQ----ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1009 LEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVrAARRAQEETRGQQQALLRDHEALVQ 1088
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP-EEELSLEDVQAELQRVEEEIRALEP 972
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 124486839 1089 LQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANV 1135
Cdd:TIGR02169 973 VNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1050-1295 |
6.29e-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: 64.31 E-value: 6.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1050 ELHRKLGVLEEEVRAARRAQEetrgqQQALLRDHEALVQLQR--RQETELEGLLVRHRDLKANMRALELAHRELQGRHEQ 1127
Cdd:TIGR02168 197 ELERQLKSLERQAEKAERYKE-----LKAELRELELALLVLRleELREELEELQEELKEAEEELEELTAELQELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1128 LQAQRANVEAQEVALlaeRERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQ 1207
Cdd:TIGR02168 272 LRLEVSELEEEIEEL---QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1208 LEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALS---RENRELLERSLESRDHLHREQREYLD 1284
Cdd:TIGR02168 349 LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNneiERLEARLERLEDRRERLQQEIEELLK 428
|
250
....*....|.
gi 124486839 1285 QLNALRREKQK 1295
Cdd:TIGR02168 429 KLEEAELKELQ 439
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
828-1248 |
8.96e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 8.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 828 RERRQWERDGPRLRAQVEAAEQQVQALEsQVRCHLEEAEREHAEKQALREELEKAV------LRGQELGDRLEHLQ---E 898
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKLLqllplyQELEALEAELAELPerlE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 899 ELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALM-------ELKARALQLEEELIQLRQYPVDLAT-G 970
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQdlaeeleELQQRLAELEEELEEAQEELEELEEeL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 971 ARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQ------ELLLQSQRAQEHSSRLQAEKSMM 1044
Cdd:COG4717 230 EQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFlvlgllALLFLLLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1045 EMQGQELHRKLgvLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGL-LVRHRDLKANMRALELAHRELQG 1123
Cdd:COG4717 310 LPALEELEEEE--LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqLEELEQEIAALLAEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1124 RHEQLQAQRANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLEL 1203
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 124486839 1204 ER--AQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENR 1248
Cdd:COG4717 468 DGelAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
851-1300 |
1.26e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.14 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 851 VQALESQVRCHLEEAEREHAEKQA--LREELEKAVLRGQELGDRLEHLQEELEQAALERQK---FLQEQENQHQRYRHLE 925
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEkdLHERLNGLESELAELDEEIERYEEQREQARETRDEadeVLEEHEERREELETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 926 QRLEaELQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQ 1005
Cdd:PRK02224 258 AEIE-DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1006 LQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRA---QEETRGQQQALLRD 1082
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdAPVDLGNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1083 HEALVQLQRRQETELEGLLVRHRDLKANMRALELAHR------------------ELQGRHEQLQAQRANVEAQEVALLA 1144
Cdd:PRK02224 417 LREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvetieEDRERVEELEAELEDLEEEVEEVEE 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1145 ERERLMQdghrQRGLEEELRRLQNEHERAQMLLAEvSRERGElqgergELRSRLARLELERAQLEIQSQQLRESNQQLDL 1224
Cdd:PRK02224 497 RLERAED----LVEAEDRIERLEERREDLEELIAE-RRETIE------EKRERAEELRERAAELEAEAEEKREAAAEAEE 565
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124486839 1225 SACRLTTQCELLTQLRSAQEEENRQL--LAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKI 1300
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESLerIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEF 643
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
734-1285 |
2.25e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 734 ALRDEVAQLRREVAGLEvKLQAQAQRLEARSAEALCLSEELAQARrteaeahqeAEAQAREQARLREAVDTASLELEAAs 813
Cdd:COG4913 239 RAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALR---------LWFAQRRLELLEAELEELRAELARL- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 814 rerealaealaaaGRERRQWERDGPRLRAQVEAAEQQ--------VQALESQvrchLEEAEREHAEKQALREELEKAVLR 885
Cdd:COG4913 308 -------------EAELERLEARLDALREELDELEAQirgnggdrLEQLERE----IERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 886 -GQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEaELQAASTSKEEALMELKARALQLEEELIQLRQYP 964
Cdd:COG4913 371 lGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR-DLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 965 VDLATGARAGPRTVetqnGRLIEVERNNA---------------TLVAEKAALQGQLQ-----HLEGQLGSLQGRAQELL 1024
Cdd:COG4913 450 AEALGLDEAELPFV----GELIEVRPEEErwrgaiervlggfalTLLVPPEHYAAALRwvnrlHLRGRLVYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1025 LQSQRAQEHS--SRLQAEKSmmEMQG---QELHRKLGVL----EEEVRAARRA--------QEETRGQ---QQALLRDH- 1083
Cdd:COG4913 526 PERPRLDPDSlaGKLDFKPH--PFRAwleAELGRRFDYVcvdsPEELRRHPRAitragqvkGNGTRHEkddRRRIRSRYv 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1084 ---EALVQLQRRQEtELEGLLVRHRDLKANMRALELAHRELQGRHEQLQaQRANVEAQEVALLAERERLMQDGHRQRGLE 1160
Cdd:COG4913 604 lgfDNRAKLAALEA-ELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEIDVASAEREIAELEAELERLD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1161 E---ELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSacrlttqcELLT 1237
Cdd:COG4913 682 AssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--------LLEE 753
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 124486839 1238 QLRSAQEEENRQLLAEvqALSRENRELLERSLESRDHLHREQREYLDQ 1285
Cdd:COG4913 754 RFAAALGDAVERELRE--NLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
846-1300 |
2.37e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 846 AAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLE 925
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 926 QRLEaelqaastSKEEALMELKARALQLEEeliqlrqypvdlatgaragprtvetqngrLIEVERNNATLVAEKAALQGQ 1005
Cdd:PRK03918 266 ERIE--------ELKKEIEELEEKVKELKE-----------------------------LKEKAEEYIKLSEFYEEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1006 LQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEmqgqELHRKLGVLEEEVRAARRAQeetrgqqqallrdheA 1085
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK----ELEKRLEELEERHELYEEAK---------------A 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1086 LVQLQRRQETELEGLLVrhRDLKANMRALELAHRELQGRHEQLQAQRANVEAQEvallAERERLMQDGHRQRGLEEELRR 1165
Cdd:PRK03918 370 KKEELERLKKRLTGLTP--EKLEKELEELEKAKEEIEEEISKITARIGELKKEI----KELKKAIEELKKAKGKCPVCGR 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1166 LQNEHERAQmLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLResnqqldlsacRLTTQCELLTQLRSAQEE 1245
Cdd:PRK03918 444 ELTEEHRKE-LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES-----------ELIKLKELAEQLKELEEK 511
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 124486839 1246 ENRQLLAEVQALSRENRELLERSLESRDHLHREQREyLDQLNALRREKQKLVEKI 1300
Cdd:PRK03918 512 LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE-LEKLEELKKKLAELEKKL 565
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
793-1303 |
2.73e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 793 REQARLREAVDTASLELEAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRcHLEEAEREHAEK 872
Cdd:PRK03918 217 PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-ELKELKEKAEEY 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 873 QALREELEKAVLRGQELGDRLEHLQEELEqaalERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEAlmELKARALQ 952
Cdd:PRK03918 296 IKLSEFYEEYLDELREIEKRLSRLEEEIN----GIEERIKELEEKEERLEELKKKLKELEKRLEELEERH--ELYEEAKA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 953 LEEELIQLRqypvdlatgARAGPRTVETQNGRLIEVERnnatlvaEKAALQGQLQHLEGQLGSLQGRAQELllqsqraQE 1032
Cdd:PRK03918 370 KKEELERLK---------KRLTGLTPEKLEKELEELEK-------AKEEIEEEISKITARIGELKKEIKEL-------KK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1033 HSSRLQAEKSMMEMQGQEL--HRKLGVLEEEVRAARRAQEEtrgqqqaLLRDHEALVQLqRRQETELEGLLVRHRDLKAN 1110
Cdd:PRK03918 427 AIEELKKAKGKCPVCGRELteEHRKELLEEYTAELKRIEKE-------LKEIEEKERKL-RKELRELEKVLKKESELIKL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1111 MRALELAhRELQGRHEQLQAQRANVEAQEVALLaeRERLMQDGHRQRGLEEELRRLQ---NEHERAQMLLAEVSRERGEL 1187
Cdd:PRK03918 499 KELAEQL-KELEEKLKKYNLEELEKKAEEYEKL--KEKLIKLKGEIKSLKKELEKLEelkKKLAELEKKLDELEEELAEL 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1188 QGERG--------ELRSRLARLE-LERAQLEIQS--QQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQA 1256
Cdd:PRK03918 576 LKELEelgfesveELEERLKELEpFYNEYLELKDaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 124486839 1257 LSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKIMDQ 1303
Cdd:PRK03918 656 YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
731-1300 |
2.75e-09 |
|
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: 62.01 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 731 EEQALRDEVAQLRREVAGLEVKLQAQAQRLEArsaealcLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELE 810
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDK-------LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 811 AASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELG 890
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 891 DRLEHLQEELEQAALERqkflqeqenqhqryrhleQRLEAELQAASTSKEE---ALMELKAR---ALQLEEELIQLR--- 961
Cdd:TIGR02169 476 EEYDRVEKELSKLQREL------------------AEAEAQARASEERVRGgraVEEVLKASiqgVHGTVAQLGSVGery 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 962 QYPVDLATGARAGPRTVET--------------QNGR------------------------------LIEVERNNA---- 993
Cdd:TIGR02169 538 ATAIEVAAGNRLNNVVVEDdavakeaiellkrrKAGRatflplnkmrderrdlsilsedgvigfavdLVEFDPKYEpafk 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 994 -----TLVAEKAAL------QGQLQHLEGQL---------GSLQGRAQELLLQSQRAQEhsSRLQAEKSMMEMQGQELHR 1053
Cdd:TIGR02169 618 yvfgdTLVVEDIEAarrlmgKYRMVTLEGELfeksgamtgGSRAPRGGILFSRSEPAEL--QRLRERLEGLKRELSSLQS 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1054 KLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRA 1133
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1134 NVEAQEVALLAererlMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQsq 1213
Cdd:TIGR02169 776 KLEEALNDLEA-----RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ-- 848
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1214 qlRESNQQldlsacrltTQCELLTQLRSAQEEEnrqllaevqalsrENRELLERSLESR-DHLHREQREYLDQLNALRRE 1292
Cdd:TIGR02169 849 --IKSIEK---------EIENLNGKKEELEEEL-------------EELEAALRDLESRlGDLKKERDELEAQLRELERK 904
|
....*...
gi 124486839 1293 KQKLVEKI 1300
Cdd:TIGR02169 905 IEELEAQI 912
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
887-1300 |
9.23e-09 |
|
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: 60.47 E-value: 9.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 887 QELGDRLEHLQEELEQAALERqkflqeqenqhqryRHLEQRLEAELQAASTSKEEaLMELKARALQLEEELiqlrqypvd 966
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSEL--------------RRIENRLDELSQELSDASRK-IGEIEKEIEQLEQEE--------- 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 967 latgaragprtvETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELllqsqraQEHSSRLQAEKSMMEM 1046
Cdd:TIGR02169 733 ------------EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL-------EEALNDLEARLSHSRI 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1047 QgqELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALvqlqrrqETELEGLLVRHRDLKANMRALELAHRELQGRHE 1126
Cdd:TIGR02169 794 P--EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL-------EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1127 QLQAQRANVEAQEvallaererlmqdghrqRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLElerA 1206
Cdd:TIGR02169 865 ELEEELEELEAAL-----------------RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK---A 924
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1207 QLEIQSQQLREsnqqLDLSACRLTTQCELLTQLRSAQEEENRqLLAEVQALSRENRelleRSLESRDHLHREQREYLDQL 1286
Cdd:TIGR02169 925 KLEALEEELSE----IEDPKGEDEEIPEEELSLEDVQAELQR-VEEEIRALEPVNM----LAIQEYEEVLKRLDELKEKR 995
|
410
....*....|....
gi 124486839 1287 NALRREKQKLVEKI 1300
Cdd:TIGR02169 996 AKLEEERKAILERI 1009
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
728-1167 |
1.02e-08 |
|
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: 60.35 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 728 AIPEEQALRDEVAQLRRE----VAGLEVKLQAQAQRLearSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLREAVD 803
Cdd:COG3096 247 AIRVTQSDRDLFKHLITEatnyVAADYMRHANERREL---SERALELRRELFGARRQLAEEQYRLVEMARELEELSARES 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 804 TASLELEAASRERealaealaaagrerrqwerdgprlrAQVEAAEQQVQALEsQVRCHLEEAEREHAEKQALREELEKAV 883
Cdd:COG3096 324 DLEQDYQAASDHL-------------------------NLVQTALRQQEKIE-RYQEDLEELTERLEEQEEVVEEAAEQL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 884 LRGQElgdRLEHLQEELEQAA---LERQKFLQEQENQHQRYRHLEQRLE--------AELQAASTSKEEAlmELKARALQ 952
Cdd:COG3096 378 AEAEA---RLEAAEEEVDSLKsqlADYQQALDVQQTRAIQYQQAVQALEkaralcglPDLTPENAEDYLA--AFRAKEQQ 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 953 LEEELIQLRQyPVDLATGARA----GPRTVETQNGrliEVERNNATLVA--------EKAALQGQLQHLEGQLGSLQGRA 1020
Cdd:COG3096 453 ATEEVLELEQ-KLSVADAARRqfekAYELVCKIAG---EVERSQAWQTArellrryrSQQALAQRLQQLRAQLAELEQRL 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1021 QelllQSQRAQEhssrlqaeksmmemQGQELHRKLGvleeEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGL 1100
Cdd:COG3096 529 R----QQQNAER--------------LLEEFCQRIG----QQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1101 LVRHRDLKANMRALELAHRELQGRHEQLQAQ--------------RANVEAQEVALLAERERLMQdghRQRGLEEELRRL 1166
Cdd:COG3096 587 LEQLRARIKELAARAPAWLAAQDALERLREQsgealadsqevtaaMQQLLEREREATVERDELAA---RKQALESQIERL 663
|
.
gi 124486839 1167 Q 1167
Cdd:COG3096 664 S 664
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
725-1266 |
2.96e-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: 58.59 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 725 LVSAIPEEQALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQarEQARLREaVDT 804
Cdd:pfam15921 115 LQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLS--HEGVLQE-IRS 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 805 ASLELEAASREREALAEALAAA---------GRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEK--- 872
Cdd:pfam15921 192 ILVDFEEASGKKIYEHDSMSTMhfrslgsaiSKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRieq 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 873 ---------QALREELEKAVLRGQELGDRLEHLQE--------------ELEQAALERQKFLQEQENQHQ-RYRHLEQRL 928
Cdd:pfam15921 272 liseheveiTGLTEKASSARSQANSIQSQLEIIQEqarnqnsmymrqlsDLESTVSQLRSELREAKRMYEdKIEELEKQL 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 929 ---EAELQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGARAGPRTVETQNG--------------RLIEVERN 991
Cdd:pfam15921 352 vlaNSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGnsitidhlrrelddRNMEVQRL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 992 NATLVAEKAALQGQlqhLEGQLGSLQGRAQELllqsQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEE 1071
Cdd:pfam15921 432 EALLKAMKSECQGQ---MERQMAAIQGKNESL----EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTAS 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1072 TRGQQQALLRDHEALVQLQRRQETELEgllvrhrdlkanmralELAHRELQGRHeqLQAQRANVEAQEVAlLAERERLMQ 1151
Cdd:pfam15921 505 LQEKERAIEATNAEITKLRSRVDLKLQ----------------ELQHLKNEGDH--LRNVQTECEALKLQ-MAEKDKVIE 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1152 DGHRQRgleEELRRLQNEHERAQmllAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSACRLTT 1231
Cdd:pfam15921 566 ILRQQI---ENMTQLVGQHGRTA---GAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVN 639
|
570 580 590
....*....|....*....|....*....|....*.
gi 124486839 1232 Q-CELLTQLRSAQEEENrQLLAEVQALSRENRELLE 1266
Cdd:pfam15921 640 AgSERLRAVKDIKQERD-QLLNEVKTSRNELNSLSE 674
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
752-1191 |
3.97e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 752 KLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASL--ELEAASREREALAE---ALAAA 826
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPErleELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 827 GRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKqalREELEKAVlrgQELGDRLEHLQEELEQAALE 906
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE---LEELQQRL---AELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 907 RQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGARAGPRTVETQNGRLI 986
Cdd:COG4717 229 LEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 987 EVERNNATlvaEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRK-----LGVLEEE 1061
Cdd:COG4717 309 ALPALEEL---EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAallaeAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1062 VRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHrDLKANMRALELAHRELQGRHEQLQAQRANVEaQEVA 1141
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE-ELEEELEELEEELEELEEELEELREELAELE-AELE 463
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 124486839 1142 LLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGER 1191
Cdd:COG4717 464 QLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
733-1287 |
4.58e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 733 QALRDEVAQLRREVAGLEVklQAQAQRLEARSAEALCLSEELAQARrteaeaHQEAEAQAREQArLREAVDTASLELEAA 812
Cdd:COG4913 265 AAARERLAELEYLRAALRL--WFAQRRLELLEAELEELRAELARLE------AELERLEARLDA-LREELDELEAQIRGN 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 813 SREREAL-AEALAAAGRERRQWERDGPRLRAQVEAAEQQV----QALESQVRCHLEEAEREHAEKQALREELEKAVLRGQ 887
Cdd:COG4913 336 GGDRLEQlEREIERLERELEERERRRARLEALLAALGLPLpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALR 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 888 ELGDRLEHLQEELeqAALERQKFlqeqeNQHQRYRHLEQRLEAELQAastSKEEA-----LMELKAR------------- 949
Cdd:COG4913 416 DLRRELRELEAEI--ASLERRKS-----NIPARLLALRDALAEALGL---DEAELpfvgeLIEVRPEeerwrgaiervlg 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 950 --ALQL---EEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQH-LEGQLGSLQGRA--- 1020
Cdd:COG4913 486 gfALTLlvpPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAwLEAELGRRFDYVcvd 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1021 -QELLLQSQRA-----QEHSSRLQAEKSMMEMQGQ-------------ELHRKLGVLEEEVRAARRAQEETRGQQQALLR 1081
Cdd:COG4913 566 sPEELRRHPRAitragQVKGNGTRHEKDDRRRIRSryvlgfdnraklaALEAELAELEEELAEAEERLEALEAELDALQE 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1082 DHEALVQLQRRQETEL--EGLLVRHRDLKANMRALELAHRELqgrhEQLQAQRANVEAQEVALLAERERLMQdghRQRGL 1159
Cdd:COG4913 646 RREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDDL----AALEEQLEELEAELEELEEELDELKG---EIGRL 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1160 EEELRRLQNEHERAQMLLAEVsrERGELQGERGELRSRLARLELERAQLEIQsQQLRESNQQLDLSACRLTTQCE-LLTQ 1238
Cdd:COG4913 719 EKELEQAEEELDELQDRLEAA--EDLARLELRALLEERFAAALGDAVERELR-ENLEERIDALRARLNRAEEELErAMRA 795
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 124486839 1239 LRSAQEEENRQLLAEVQALsRENRELLERsLEsRDHLHREQREYLDQLN 1287
Cdd:COG4913 796 FNREWPAETADLDADLESL-PEYLALLDR-LE-EDGLPEYEERFKELLN 841
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1028-1219 |
4.86e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1028 QRAQEHSSRL-QAEKSMMEMQGQElhRKLGVLEEEVRAARRAQEETRGQQQALLR-DHEALVQLQRRQETELEGLLVRHR 1105
Cdd:COG4913 228 DALVEHFDDLeRAHEALEDAREQI--ELLEPIRELAERYAAARERLAELEYLRAAlRLWFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1106 DLKANMRALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLMQDGHRQR-----GLEEELRRL-----------QNE 1169
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERerrraRLEALLAALglplpasaeefAAL 385
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 124486839 1170 HERAQMLLAEVSRERGELQGERGELRSRLARLELERAQL--EIQSQQLRESN 1219
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELeaEIASLERRKSN 437
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
731-1308 |
5.36e-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: 57.77 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 731 EEQALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEalcLSEELAQARRTEAEAHQEAEAQAR----EQARLREAVDTAS 806
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL---LEELNKKIKDLGEEEQLRVKEKIGeleaEIASLERSIAEKE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 807 LELEAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRG 886
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 887 QELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEA------ELQAASTSKEEALMELKARALQLEEELIQL 960
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEleeekeDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 961 RQ-------------------------------YPVDLATGARAGPRTVETQNGRLIEVE-------------RNNATLV 996
Cdd:TIGR02169 475 KEeydrvekelsklqrelaeaeaqaraseervrGGRAVEEVLKASIQGVHGTVAQLGSVGeryataievaagnRLNNVVV 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 997 AEKAALQGQLQHLEGQLGslqGRAQELLLQSQRAQEHSSRLQAEKS---------------------------------- 1042
Cdd:TIGR02169 555 EDDAVAKEAIELLKRRKA---GRATFLPLNKMRDERRDLSILSEDGvigfavdlvefdpkyepafkyvfgdtlvvediea 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1043 ---------MMEMQGqELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRA 1113
Cdd:TIGR02169 632 arrlmgkyrMVTLEG-ELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1114 LELAHR---ELQGRHEQLQAQranvEAQEVALLAERERLMQDGHRQR-GLEEELRRLQNEHERAQMLLAEVSRERGELqg 1189
Cdd:TIGR02169 711 LSDASRkigEIEKEIEQLEQE----EEKLKERLEELEEDLSSLEQEIeNVKSELKELEARIEELEEDLHKLEEALNDL-- 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1190 ERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRsaQEEENRQLLAEVQALSRENR-ELLERS 1268
Cdd:TIGR02169 785 EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI--QELQEQRIDLKEQIKSIEKEiENLNGK 862
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 124486839 1269 LESRDHLHREQREYLDQLNALRREKQKLVEKIMDQYRVLE 1308
Cdd:TIGR02169 863 KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1058-1272 |
7.69e-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: 56.31 E-value: 7.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1058 LEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEA 1137
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1138 QevalLAERERLMQDGHRQRGLEEELRRLQ-NEHERAQMLLAEVSRER----GELQGERGELRSRLARLELERAQLEIQS 1212
Cdd:COG4942 105 E----LAELLRALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARreqaEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1213 QQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESR 1272
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
839-1280 |
1.36e-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: 56.34 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 839 RLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELekavlrgQELGDRLEHLQEELEQAALERQKFLQEQENQH 918
Cdd:pfam01576 226 ELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKI-------RELEAQISELQEDLESERAARNKAEKQRRDLG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 919 QRYRHLEQRLEAEL------QAASTSKEEALMELKAralQLEEELiqlRQYPVDLATGARAGPRTVETQNGRLIEVERNN 992
Cdd:pfam01576 299 EELEALKTELEDTLdttaaqQELRSKREQEVTELKK---ALEEET---RSHEAQLQEMRQKHTQALEELTEQLEQAKRNK 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 993 ATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEET 1072
Cdd:pfam01576 373 ANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1073 RGQQQALLRDHEAL-VQLQRRQETeLEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQ----EVALLAERE 1147
Cdd:pfam01576 453 EGKNIKLSKDVSSLeSQLQDTQEL-LQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQlstlQAQLSDMKK 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1148 RLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSAC 1227
Cdd:pfam01576 532 KLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLA 611
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 124486839 1228 RLTTQCELLTQLRSAQEEENRQLLAEVQALSREnrelLERSLESRDHLHREQR 1280
Cdd:pfam01576 612 EEKAISARYAEERDRAEAEAREKETRALSLARA----LEEALEAKEELERTNK 660
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
630-1317 |
1.41e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 630 SREAPQGELVHKAQVLKQESpkcRPRSAELTLREPLKDQKALDRELELSKQQKETGRHEQRPKGLESKLGPQKPQqtseg 709
Cdd:PTZ00121 1124 AEDARKAEEARKAEDARKAE---EARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRK----- 1195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 710 VPDAWSREEPTPGETLVSAipeEQALRDEVAQLRREVAGLEvklQAQAQRLEARSAEALCLSEEL-----AQARRTEAEA 784
Cdd:PTZ00121 1196 AEDARKAEAARKAEEERKA---EEARKAEDAKKAEAVKKAE---EAKKDAEEAKKAEEERNNEEIrkfeeARMAHFARRQ 1269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 785 HQEAEAQAREQARLREAVdtaslELEAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEE 864
Cdd:PTZ00121 1270 AAIKAEEARKADELKKAE-----EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 865 AEREHAEKQALREELEKAvlrgQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQ--RLEAELQAASTSKEEA 942
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAA----EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEdkKKADELKKAAAAKKKA 1420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 943 lMELKARALQLE--EELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRA 1020
Cdd:PTZ00121 1421 -DEAKKKAEEKKkaDEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1021 QEL--LLQSQRAQEHSSRLQAEKSMMEMQGQELHRKlgvlEEEVRAA--RRAQEETRGQQQALLRDHEALVQLQRRQETE 1096
Cdd:PTZ00121 1500 DEAkkAAEAKKKADEAKKAEEAKKADEAKKAEEAKK----ADEAKKAeeKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1097 LEGLLVRHRDLKANMRA-----LELAHRELQGRHEQL-QAQRANVEAQEVAllAERERLMQDGHRQRGLEEELRR---LQ 1167
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEArieevMKLYEEEKKMKAEEAkKAEEAKIKAEELK--KAEEEKKKVEQLKKKEAEEKKKaeeLK 1653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1168 NEHERAQMLLAEVSRERGELQGERGELRsrlaRLELERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAqEEEN 1247
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAEEDKKKAEEAK----KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA-EEEN 1728
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486839 1248 RQLLAEVQALSRENR---ELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKIMDQYRVLEPGPLPRTKK 1317
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKkkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
195-489 |
2.82e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 195 GPESGELVAEELEMQLRSLTGMMSRLARERDLGAQRLAELLLEREPAHLLLpeapanASAEGVSHHLALQLTNAKAQLRR 274
Cdd:TIGR02168 664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEL------EQLRKELEELSRQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 275 LRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALRERA--------GRLPRLQEELRRCRE 346
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLkeelkalrEALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 347 KLQAAEVFKGQLEEERvlsEALEASKVLLEEQLEVARERSARLHETQREnllLRTRLGEAHADLDSLRHQLEQLVEenve 426
Cdd:TIGR02168 818 EAANLRERLESLERRI---AATERRLEDLEEQIEELSEDIESLAAEIEE---LEELIEELESELEALLNERASLEE---- 887
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486839 427 lelelqrslepppgspgeaslpgAAPSLQDEVREAEAgRLRAVERENRELRGQLQMLQAQLGS 489
Cdd:TIGR02168 888 -----------------------ALALLRSELEELSE-ELRELESKRSELRRELEELREKLAQ 926
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
967-1226 |
3.02e-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: 54.38 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 967 LATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEM 1046
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1047 QGQELHRKLGVLEEEVRaarraqeetrgqqqallrdhEALVQLQRRQETELEGLLVRHRDLKANMRALELAH---RELQG 1123
Cdd:COG4942 91 EIAELRAELEAQKEELA--------------------ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKylaPARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1124 RHEQLQAQRANVEAQEVALLAERERLMQDghrQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLEL 1203
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERAELEAL---LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
250 260
....*....|....*....|...
gi 124486839 1204 ERAQLEIQSQQLRESNQQLDLSA 1226
Cdd:COG4942 228 LIARLEAEAAAAAERTPAAGFAA 250
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
828-1210 |
3.84e-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: 55.12 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 828 RERRQWERDG------PRLRAQVEAAEQQVQALESQVRCHLEEA----EREHAEKQALREELEKAVLRGQELGDRLEHLQ 897
Cdd:pfam15921 399 QNKRLWDRDTgnsitiDHLRRELDDRNMEVQRLEALLKAMKSECqgqmERQMAAIQGKNESLEKVSSLTAQLESTKEMLR 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 898 EELEQAALERQKFLQEQENQHQRYRHLEQRLEA-ELQAASTSKEEALMELKARALQ-LEEELIQLRQYPVDLAtgaraGP 975
Cdd:pfam15921 479 KVVEELTAKKMTLESSERTVSDLTASLQEKERAiEATNAEITKLRSRVDLKLQELQhLKNEGDHLRNVQTECE-----AL 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 976 RTVETQNGRLIEVER----NNATLVAEKAALQGQLQ----HLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQ 1047
Cdd:pfam15921 554 KLQMAEKDKVIEILRqqieNMTQLVGQHGRTAGAMQvekaQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELE 633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1048 GQELhrkLGVLEEEVRAARRAQEE----------TRGQQQALLRDHEALVQLQRRQETELEGLLVRHR-DLKANMRALEL 1116
Cdd:pfam15921 634 KVKL---VNAGSERLRAVKDIKQErdqllnevktSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKmQLKSAQSELEQ 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1117 AHRELQ--------------GRHEQLQAQRANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEheraqmlLAEVSR 1182
Cdd:pfam15921 711 TRNTLKsmegsdghamkvamGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQE-------LSTVAT 783
|
410 420
....*....|....*....|....*...
gi 124486839 1183 ERGELQGERGELRSRLARLELERAQLEI 1210
Cdd:pfam15921 784 EKNKMAGELEVLRSQERRLKEKVANMEV 811
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
276-990 |
4.43e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 276 RQEVEEKAEQLLDSQAEVQGLEaEIRR---LRQETQALSAQ-AKRAELYREEAEAlreRAGRLPRLQEELRRCREKLQAA 351
Cdd:PTZ00121 1110 KAEEARKAEEAKKKAEDARKAE-EARKaedARKAEEARKAEdAKRVEIARKAEDA---RKAEEARKAEDAKKAEAARKAE 1185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 352 EVFKGqlEEERVLSEALEASKVLLEEqlEVARERSARLHETQRENLLLRtRLGEAHADLDSLRHQLEQLVEENVELELEL 431
Cdd:PTZ00121 1186 EVRKA--EELRKAEDARKAEAARKAE--EERKAEEARKAEDAKKAEAVK-KAEEAKKDAEEAKKAEEERNNEEIRKFEEA 1260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 432 QRSLEPPPGSPGEASLPGAApslqDEVREAEAGRLRAVERENRELRgqlQMLQAQLGSQHPLLEEQRENSRQPPVPNRDP 511
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKA----DELKKAEEKKKADEAKKAEEKK---KADEAKKKAEEAKKADEAKKKAEEAKKKADA 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 512 ATPSALHHSPQSPACQigGEGSESLDLPSPASYSDITRSPKCSQAPDSHPELESPLQMVSQDPQTSDQALQESDPTVETH 591
Cdd:PTZ00121 1334 AKKKAEEAKKAAEAAK--AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELK 1411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 592 QCLEKSGHRVPLQSpivwdppQGPEVRiEVQELlgETGSREAPQGELVHKAQVLKQESPKCRPRSAELTLREPLKDQKAL 671
Cdd:PTZ00121 1412 KAAAAKKKADEAKK-------KAEEKK-KADEA--KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 672 DRELELSKQQKETGRH--EQRPKGLESKLGPQKPQQTSEG--VPDAWSREEPTPGETLVSAipEEQALRDEVAQLRREVA 747
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKkaDEAKKAAEAKKKADEAKKAEEAkkADEAKKAEEAKKADEAKKA--EEKKKADELKKAEELKK 1559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 748 GLEVKLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAR----EQARLREAVDTASLELEAASRerealaeal 823
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKkmkaEEAKKAEEAKIKAEELKKAEE--------- 1630
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 824 aaagrERRQWERDGPRLRAQVEAAEQqVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQA 903
Cdd:PTZ00121 1631 -----EKKKVEQLKKKEAEEKKKAEE-LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 904 ALERQKFLQEQENQHQRYRHLEQRleaELQAASTSKEEALMELKARALQLEEE----LIQLRQYPVDLATGARAGPRTV- 978
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEEN---KIKAEEAKKEAEEDKKKAEEAKKDEEekkkIAHLKKEEEKKAEEIRKEKEAVi 1781
|
730
....*....|....*..
gi 124486839 979 -----ETQNGRLIEVER 990
Cdd:PTZ00121 1782 eeeldEEDEKRRMEVDK 1798
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1090-1299 |
5.32e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1090 QRRQETELegllvRHRDLKANMRALELAHRELQGRHEQLQAQRANVE-AQEVALLAERERLMQDGHRQRGLEEELRRLQN 1168
Cdd:COG1196 172 ERKEEAER-----KLEATEENLERLEDILGELERQLEPLERQAEKAErYRELKEELKELEAELLLLKLRELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1169 EHERAQM----LLAEVSRERGEL-----------------QGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSAC 1227
Cdd:COG1196 247 ELEELEAeleeLEAELAELEAELeelrleleeleleleeaQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124486839 1228 RLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEK 1299
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
267-436 |
8.99e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 8.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 267 NAKAQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQAL--------------SAQAKRAELyREEAEALRERAG 332
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdeidvaSAEREIAEL-EAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 333 RLPRLQEELRRCREKLQAAEVFKGQLEEERvlsEALEASKVLLEEQLEVARERSARLHETQRE--NLLLRTRLGEAHAD- 409
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEI---GRLEKELEQAEEELDELQDRLEAAEDLARLelRALLEERFAAALGDa 762
|
170 180
....*....|....*....|....*...
gi 124486839 410 -LDSLRHQLEQLVEENVELELELQRSLE 436
Cdd:COG4913 763 vERELRENLEERIDALRARLNRAEEELE 790
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1090-1308 |
9.35e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 9.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1090 QRRQETELegllvRHRDLKANMRALELAHRELQGRHEQLQAQ----------RANVEAQEVALLA--------ERERLMQ 1151
Cdd:TIGR02168 172 ERRKETER-----KLERTRENLDRLEDILNELERQLKSLERQaekaerykelKAELRELELALLVlrleelreELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1152 D----GHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSAC 1227
Cdd:TIGR02168 247 ElkeaEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1228 RLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLhREQREYLDQLNALRREKQKLVEKIMDQYRVL 1307
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL-EELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
.
gi 124486839 1308 E 1308
Cdd:TIGR02168 406 E 406
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
134-475 |
1.09e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 134 EEAVDELESILRLLLGASVQCEHRELFIRHIRGLSLDVQSELAGAIQEVTQPGAGVVLALAGPESGELVAEELEMQLRSL 213
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 214 TGMMSRLARERDLGAQRLAELLLEREpahlllpeapanasaegvshHLALQLTNAKAQLRRLRQEVEEKAEQLLDSQAEV 293
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELE--------------------EAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 294 QGLEAEIRRLRQETQALSAQAKRA--ELYREEAEALRERAgrlprlqEELRRCREKLQAAEVFKGQLEEERVLSEALEAS 371
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALleRLERLEEELEELEE-------ALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 372 KVLLEEQLEVARERSARLHETQRENLLLRTRLgeahadldSLRHQLEQLVEENVELELELQRSLEPPPGSPGEASLPGAA 451
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARL--------LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE 533
|
330 340
....*....|....*....|....
gi 124486839 452 PSLQDEVREAEAGRLRAVERENRE 475
Cdd:COG1196 534 AAYEAALEAALAAALQNIVVEDDE 557
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
733-1300 |
1.25e-06 |
|
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: 53.43 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 733 QALRDEVAQLRREVAGLEVKlQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELEAA 812
Cdd:TIGR00618 222 QVLEKELKHLREALQQTQQS-HAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIK 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 813 SREREALAEALAAAGRERRQWERDGPRLR----AQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQE 888
Cdd:TIGR00618 301 AVTQIEQQAQRIHTELQSKMRSRAKLLMKraahVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQH 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 889 LGDRLEHLQEELEQAALERQKFLQEQENQHQR-YRHLEQR-LEAELQAASTSKEEALMELKARALQLEEELIQLRQ---Y 963
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKELDILQREQATIdTRTSAFRdLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLekiH 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 964 PVDLATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQS------QRAQEHSSRL 1037
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGpltrrmQRGEQTYAQL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1038 QAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLvRHRDLKANMRALELA 1117
Cdd:TIGR00618 541 ETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS-EAEDMLACEQHALLR 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1118 HRELQGRHEQLQAQRANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSR 1197
Cdd:TIGR00618 620 KLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1198 LARLELERAQLEIQSQQLRESNQQLDLSACR---LTTQCELLTQ-LRSAQEEENRQLLAEVQALSRENRELL--ERSLES 1271
Cdd:TIGR00618 700 AQCQTLLRELETHIEEYDREFNEIENASSSLgsdLAAREDALNQsLKELMHQARTVLKARTEAHFNNNEEVTaaLQTGAE 779
|
570 580
....*....|....*....|....*....
gi 124486839 1272 RDHLHREQREYLDQLNALRREKQKLVEKI 1300
Cdd:TIGR00618 780 LSHLAAEIQFFNRLREEDTHLLKTLEAEI 808
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
840-1224 |
1.46e-06 |
|
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: 52.59 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 840 LRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVlrgQELGDRLEHLQEELEQAALERQKFLQEQENqhq 919
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQR---RELESRVAELKEELRQSREKHEELEEKYKE--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 920 ryrhlEQRLEAELQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVErnnatlvAEK 999
Cdd:pfam07888 106 -----LSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEE-------AER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1000 AALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQ-- 1077
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERkv 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1078 -ALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQ-LQAQRANVEAqevallaERERLMQDGHR 1155
Cdd:pfam07888 254 eGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQeRETLQQSAEA-------DKDRIEKLSAE 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486839 1156 QRGLEEelrRLQNEHERAQMLLAEVSRER-------GELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDL 1224
Cdd:pfam07888 327 LQRLEE---RLQEERMEREKLEVELGREKdcnrvqlSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQ 399
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
203-499 |
1.68e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 203 AEELEMQLRSLTGMMSRLARERDLGAQRLAELLLEREPAHLLLpeapanASAEGVSHHLALQLTNAKAQLRRLRQEVEEK 282
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL------EELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 283 AEQLLDSQAEVQGLEAEIRRLRQETQAL-----SAQAKRAELYREEAEALRERAGRLPRLQEELRRCREKLQAAEVFKGQ 357
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELeeeleELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 358 LEEERVLSEALEASKVLLEEQLEVARERSARLHETQRENLLLRTRLGEAHADLDSLRHQLEQLVEENVELELELQRSLEp 437
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE- 459
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486839 438 ppgspgeaslpGAAPSLQDEVREAEAGR--LRAVERENRELRGQLQMLQAQLGSQHPLLEEQRE 499
Cdd:COG1196 460 -----------ALLELLAELLEEAALLEaaLAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
733-1267 |
1.88e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.60 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 733 QALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELEAA 812
Cdd:PRK01156 193 KSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKN 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 813 ---SREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHlEEAEREHAEKQALREELEKAvlrgQEL 889
Cdd:PRK01156 273 nyyKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKY-HAIIKKLSVLQKDYNDYIKK----KSR 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 890 GDRLEHLQEELEQAALERQKFLQEQENQHQRYRhlEQRLEAELQAASTSKEEALMELKARALQLEEELIqlrqypvdlat 969
Cdd:PRK01156 348 YDDLNNQILELEGYEMDYNSYLKSIESLKKKIE--EYSKNIERMSAFISEILKIQEIDPDAIKKELNEI----------- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 970 garagprtvetqNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRL----QAEKSMME 1045
Cdd:PRK01156 415 ------------NVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIinhyNEKKSRLE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1046 MQGQELHRKLGVLEEEVRAARRAQEETRGQQ-------QALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAH 1118
Cdd:PRK01156 483 EKIREIEIEVKDIDEKIVDLKKRKEYLESEEinksineYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLED 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1119 RE--------------------LQGRHEQLQAQRANVEA--QEVALLAERERLMQDGHRQRgLEEELRRLQNEHERAQml 1176
Cdd:PRK01156 563 LDskrtswlnalavislidietNRSRSNEIKKQLNDLESrlQEIEIGFPDDKSYIDKSIRE-IENEANNLNNKYNEIQ-- 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1177 laEVSRERGELQGERGELRSRLARL-ELERAQLEIQSqQLRESNQQLDLSACRLTTQCELLTQLRSaQEEENRQLLAEVQ 1255
Cdd:PRK01156 640 --ENKILIEKLRGKIDNYKKQIAEIdSIIPDLKEITS-RINDIEDNLKKSRKALDDAKANRARLES-TIEILRTRINELS 715
|
570
....*....|..
gi 124486839 1256 ALSRENRELLER 1267
Cdd:PRK01156 716 DRINDINETLES 727
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
867-1300 |
2.09e-06 |
|
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: 52.48 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 867 REHAEKQALREELEKAvlrgQELGDRLEHLQEELEQaaleRQKFLQEQENQHQRYRHLEQRLEAElqaastsKEEALMEL 946
Cdd:pfam01576 2 RQEEEMQAKEEELQKV----KERQQKAESELKELEK----KHQQLCEEKNALQEQLQAETELCAE-------AEEMRARL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 947 KARALQLEEELIQLRqypvdlatgaragprtvetqnGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQ 1026
Cdd:pfam01576 67 AARKQELEEILHELE---------------------SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1027 SQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEE---EVRAARRAQEETRGQQQALLRDHEALV-QLQRRQETELEGllv 1102
Cdd:pfam01576 126 KVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEErisEFTSNLAEEEEKAKSLSKLKNKHEAMIsDLEERLKKEEKG--- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1103 rHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQ----EVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQmllA 1178
Cdd:pfam01576 203 -RQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQlakkEEELQAALARLEEETAQKNNALKKIRELEAQISELQ---E 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1179 EVSRERGelQGERGELRSRLARLELERAQLEIQSqQLRESNQQLDLSACRLTTqcelLTQLRSAQEEENRQLLAEVQALS 1258
Cdd:pfam01576 279 DLESERA--ARNKAEKQRRDLGEELEALKTELED-TLDTTAAQQELRSKREQE----VTELKKALEEETRSHEAQLQEMR 351
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 124486839 1259 RENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKI 1300
Cdd:pfam01576 352 QKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAEL 393
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
917-1141 |
2.14e-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: 51.69 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 917 QHQRYRHLEQRLEaELQAASTSKEEALMELKARALQLEEELIQLRQYPVDLAtgaragpRTVETQNGRLIEVERNNATLV 996
Cdd:COG4942 18 QADAAAEAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA-------RRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 997 AEKAALQGQLQHLEGQLGSLQGRAQ--------ELLLQSQRAQEHSSRLQAEKSMMEM---QGQELHRKLGVLEEEVRAA 1065
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYrlgrqpplALLLSPEDFLDAVRRLQYLKYLAPArreQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486839 1066 RRAQEETRGQQQALLRDHEALVQLQRRQETELegllvrhRDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVA 1141
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLL-------ARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
844-1273 |
3.50e-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: 51.65 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 844 VEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQ---R 920
Cdd:pfam05483 263 LEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEelnK 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 921 YRHLEQRLEAELQAASTSKEEALMELKARalqLEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNaTLVAEKA 1000
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRTEQQR---LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK-KILAEDE 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1001 ALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALL 1080
Cdd:pfam05483 419 KLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1081 RDHEALVQ--------LQRRQETELEGLLVRHRDLKA--NMRALELAHR-ELQGRHEQLQAQRANV-----EAQEVALLA 1144
Cdd:pfam05483 499 LENKELTQeasdmtleLKKHQEDIINCKKQEERMLKQieNLEEKEMNLRdELESVREEFIQKGDEVkckldKSEENARSI 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1145 ERERLMQDgHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQ----GERGELRS---RLARLELERA----------- 1206
Cdd:pfam05483 579 EYEVLKKE-KQMKILENKCNNLKKQIENKNKNIEELHQENKALKkkgsAENKQLNAyeiKVNKLELELAsakqkfeeiid 657
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486839 1207 --QLEIQSQQLRESNQQLDLSACRLTTqcELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRD 1273
Cdd:pfam05483 658 nyQKEIEDKKISEEKLLEEVEKAKAIA--DEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERD 724
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
60-182 |
3.72e-06 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 48.17 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 60 LIDGALLLRVLGIIAPSSRGGLRMVRGRDGPAA---CRMWNLCHLWGRLRDFYQEELQLLILSPP-PDLQTMG--CDPfs 133
Cdd:pfam19047 25 LTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDnwrLKVSNLKKILQSVVDYYQDVLGQQISDFLlPDVNLIGehSDP-- 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 124486839 134 eeavDELESILRLLLGASVQCEHRELFIRHIRGLSLDVQSELAGAIQEV 182
Cdd:pfam19047 103 ----AELGRLLQLILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQEL 147
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
724-1292 |
4.01e-06 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 51.80 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 724 TLVSAIPEEQALRDEVAQLRREVAGLEVKLQAQAQ--------RLEARSAEALCLSEEL---AQARRTEAEAHQEAEAQA 792
Cdd:COG3321 805 GLVRQCLAAAGDAVVLPSLRRGEDELAQLLTALAQlwvagvpvDWSALYPGRGRRRVPLptyPFQREDAAAALLAAALAA 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 793 REQARLREAVDTASLELEAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEK 872
Cdd:COG3321 885 ALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGAL 964
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 873 QALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALMELKARALQ 952
Cdd:COG3321 965 LLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAA 1044
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 953 LEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQE 1032
Cdd:COG3321 1045 AAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAAL 1124
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1033 HSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMR 1112
Cdd:COG3321 1125 LALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAAL 1204
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1113 ALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERG 1192
Cdd:COG3321 1205 LAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAA 1284
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1193 ELRSRLARLELERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESR 1272
Cdd:COG3321 1285 LALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALA 1364
|
570 580
....*....|....*....|
gi 124486839 1273 DHLHREQREYLDQLNALRRE 1292
Cdd:COG3321 1365 AAAGAAAAAAALALAALAAA 1384
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1143-1300 |
4.92e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1143 LAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLEL--ERAQLEIQSQQLRESNQ 1220
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1221 QLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKI 1300
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
262-419 |
6.18e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 262 ALQLTNAKAQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEA--EALRERAGRLPRLQE 339
Cdd:COG4913 273 ELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggDRLEQLEREIERLER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 340 ELRRCREKLQAAEVFKGQLEEERVLSEA-LEASKVLLEEQLEVARERSARLHETQRENLLLRTRLGEAHADLDSLRHQLE 418
Cdd:COG4913 353 ELEERERRRARLEALLAALGLPLPASAEeFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
.
gi 124486839 419 Q 419
Cdd:COG4913 433 R 433
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
997-1246 |
6.69e-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: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 997 AEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQ 1076
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1077 QALLRdhealvQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAqevallaererlmqdghrq 1156
Cdd:COG4942 107 AELLR------ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE------------------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1157 rgLEEELRRLQNEHERAQMLLAEvsrergeLQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSACRLTTQCELL 1236
Cdd:COG4942 162 --LAALRAELEAERAELEALLAE-------LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
250
....*....|
gi 124486839 1237 TQLRSAQEEE 1246
Cdd:COG4942 233 EAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
891-1145 |
6.90e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 891 DRLEHLQEELEQAAlERQKFLQEQENQHQRYRHLEQRLeAELQAastskeealMELKARALQLEEELIQLRQypvdlatg 970
Cdd:COG4913 235 DDLERAHEALEDAR-EQIELLEPIRELAERYAAARERL-AELEY---------LRAALRLWFAQRRLELLEA-------- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 971 aragprtvetqngrliEVERNNAtlvaEKAALQGQLQHLEGQLGSLQGRAQELllQSQRAQEHSSRLQAEKSMMEMQGQE 1050
Cdd:COG4913 296 ----------------ELEELRA----ELARLEAELERLEARLDALREELDEL--EAQIRGNGGDRLEQLEREIERLERE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1051 LHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQA 1130
Cdd:COG4913 354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
250
....*....|....*
gi 124486839 1131 QRANVEAQEVALLAE 1145
Cdd:COG4913 434 RKSNIPARLLALRDA 448
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
264-432 |
7.59e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 7.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 264 QLTNAKAQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALRERAG---RLPRLQEE 340
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAElpeRLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 341 LRRCREKLQAAEVFKGQLEE-ERVLSEALEASKVLLEEQLEVARERSARLHETQREnllLRTRLGEAHADLDSLRHQLEQ 419
Cdd:COG4717 155 LEELRELEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQRLAE---LEEELEEAQEELEELEEELEQ 231
|
170
....*....|...
gi 124486839 420 LVEENVELELELQ 432
Cdd:COG4717 232 LENELEAAALEER 244
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
845-1212 |
1.06e-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: 50.36 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 845 EAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHL 924
Cdd:pfam02463 161 EAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 925 EQRLEAELQAASTSKEEALMELKARALQLEEELIQLrqypvdlatgaragprtvETQNGRLIEVERnnATLVAEKAALQG 1004
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKE------------------EEKEKKLQEEEL--KLLAKEEEELKS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1005 QLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDH- 1083
Cdd:pfam02463 301 ELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKk 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1084 EALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLMQDGHRQRglEEEL 1163
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELE--KQEL 458
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 124486839 1164 RRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQS 1212
Cdd:pfam02463 459 KLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS 507
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
873-1305 |
1.17e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 50.18 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 873 QALREELEKavLRGQELGDRL------EHLQEELEQAALERQKFLQEQENQHQRYRHLEQR--LEAELQAASTSKEEALM 944
Cdd:PRK10246 194 KSARTELEK--LQAQASGVALltpeqvQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLdeLQQEASRRQQALQQALA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 945 ELKARA-----LQLEEELIQLR---QYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSL 1016
Cdd:PRK10246 272 AEEKAQpqlaaLSLAQPARQLRphwERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTW 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1017 QGRAQELLLQSQ-----RAQ-EHSSRLQAEKSMMEMQGQELHRKLGVL--------EEEVRAARRAQEETRGQQQALLRD 1082
Cdd:PRK10246 352 LAEHDRFRQWNNelagwRAQfSQQTSDREQLRQWQQQLTHAEQKLNALpaitltltADEVAAALAQHAEQRPLRQRLVAL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1083 HEALVQLQRRQETelegllvrhrdlkaNMRALELAHRELQGRHEQLQAQR-----ANVEAQEVALLAERERLMQDghrqr 1157
Cdd:PRK10246 432 HGQIVPQQKRLAQ--------------LQVAIQNVTQEQTQRNAALNEMRqrykeKTQQLADVKTICEQEARIKD----- 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1158 gLEEELRRLQ----------NEH---ERAQMLlaevsrergelqgERGELRSRLARLELERAQLEIQSQQLResnqqldl 1224
Cdd:PRK10246 493 -LEAQRAQLQagqpcplcgsTSHpavEAYQAL-------------EPGVNQSRLDALEKEVKKLGEEGAALR-------- 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1225 sacrltTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLER---SLESRDHLH---REQREYLDQLNALrREKQKLVE 1298
Cdd:PRK10246 551 ------GQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASlniTLQPQDDIQpwlDAQEEHERQLRLL-SQRHELQG 623
|
....*..
gi 124486839 1299 KIMDQYR 1305
Cdd:PRK10246 624 QIAAHNQ 630
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
842-1073 |
1.31e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 842 AQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRY 921
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 922 RHLEQRLEAELQAASTSKEEALMELKARAlqleeeliqlrQYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAEKAA 1001
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSP-----------EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124486839 1002 LQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETR 1073
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
278-489 |
1.39e-05 |
|
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: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 278 EVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSaqakRAELYREEAEALRERAGRLPRLQEELRRCREKlQAAEVFKGQ 357
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIELLE----PIRELAERYAAARERLAELEYLRAALRLWFAQ-RRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 358 LEEERVLSEALEASKVLLEEQLEVARERSARLHETQRENLLlrTRLGEAHADLDSLRHQLEQLVEENVELELELQRSLEP 437
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG--DRLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 124486839 438 PPGSPGE-ASLPGAAPSLQDEVREAEAG---RLRAVERENRELRGQLQMLQAQLGS 489
Cdd:COG4913 375 LPASAEEfAALRAEAAALLEALEEELEAleeALAEAEAALRDLRRELRELEAEIAS 430
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
988-1188 |
1.57e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 988 VERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQ--RAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAA 1065
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1066 RRAQEETRGQQQALLRD------HEALVQLQRRQETELEGLLVRH---RDLKANMRALE-LAHRELQGRHEQLQAQRANV 1135
Cdd:COG3206 246 RAQLGSGPDALPELLQSpviqqlRAQLAELEAELAELSARYTPNHpdvIALRAQIAALRaQLQQEAQRILASLEAELEAL 325
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 124486839 1136 EAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQ 1188
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1128-1336 |
1.60e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1128 LQAQRANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQ 1207
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1208 LEIQSQQLRESNQQLDLSACRLTTQCEL---------------------LTQLRSAQEEENRQLLAEVQALsrenRELLE 1266
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLalllspedfldavrrlqylkyLAPARREQAEELRADLAELAAL----RAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1267 RSLESRDHLHREQREYLDQLNALRREKQKLVEKIMDQYRVLEPGPLPRTKKGSWLADKVKRLIRPRREGA 1336
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1037-1303 |
1.93e-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: 49.35 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1037 LQAEKSMMEMQGQELHRKLgvleeevraarrAQEETRGQQQALLRDHEALVQLQ-----RRQETELEGLLVRHRDLKANM 1111
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKM------------EQERLRQEKEEKAREVERRRKLEeaekaRQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1112 RALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLM----QDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGEL 1187
Cdd:pfam17380 346 RERELERIRQEERKRELERIRQEEIAMEISRMRELERLQmerqQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1188 QGERGELRSR-LARLELERAQlEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEvqalsrENRELLE 1266
Cdd:pfam17380 426 RAEQEEARQReVRRLEEERAR-EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEE------QRRKILE 498
|
250 260 270
....*....|....*....|....*....|....*..
gi 124486839 1267 RSLESRDHLHREQreyldqlnalrREKQKLVEKIMDQ 1303
Cdd:pfam17380 499 KELEERKQAMIEE-----------ERKRKLLEKEMEE 524
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
855-1289 |
2.40e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 855 ESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLQE---ELE---QAALERQKFLQE---QENQHQRYR--- 922
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEaesDLEqdyQAASDHLNLVQTalrQQEKIERYQadl 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 923 -HLEQRLEAELQAASTSKEEaLMELKARALQLEEELIQLRqypvdlatgaragprtvetqnGRLIEVERnnATLVAEKAA 1001
Cdd:PRK04863 358 eELEERLEEQNEVVEEADEQ-QEENEARAEAAEEEVDELK---------------------SQLADYQQ--ALDVQQTRA 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1002 LQGQ--LQHLEgqlgslqgRAQELLLQSQRAQEHSSRLQAEksmMEMQGQELHRKLGVLEEEVRAArraqeetrgqqQAL 1079
Cdd:PRK04863 414 IQYQqaVQALE--------RAKQLCGLPDLTADNAEDWLEE---FQAKEQEATEELLSLEQKLSVA-----------QAA 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1080 LRDHEALVQLQRRQETELEgllvrhrdlkaNMRALELAhRELQGRHEQLQAQRANVEAQEVALlaerERLMQDGHRQRGL 1159
Cdd:PRK04863 472 HSQFEQAYQLVRKIAGEVS-----------RSEAWDVA-RELLRRLREQRHLAEQLQQLRMRL----SELEQRLRQQQRA 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1160 EEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQL 1239
Cdd:PRK04863 536 ERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARL 615
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 124486839 1240 R--SAQEEENRQLLAE-VQALSRENRELlersLESRDHLHREQREYLDQLNAL 1289
Cdd:PRK04863 616 ReqSGEEFEDSQDVTEyMQQLLEREREL----TVERDELAARKQALDEEIERL 664
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
737-1208 |
2.65e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 737 DEVAQLRREVAGLEVKLQAQAQRLEARSAEALCLSEELA------QARRTEAEAHQEAEAQAREQARLREAVDTASLELE 810
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESdleqdyQAASDHLNLVQTALRQQEKIERYQADLEELEERLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 811 AASREREALAEALAaagrerrqwerdgpRLRAQVEAAEQQVQALESQ---VRCHLEEAERE----HAEKQALREE---LE 880
Cdd:PRK04863 366 EQNEVVEEADEQQE--------------ENEARAEAAEEEVDELKSQladYQQALDVQQTRaiqyQQAVQALERAkqlCG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 881 KAVLRGQELGDRLEHLQEELEQAALERqkflqeqenqhqryRHLEQRLEAElQAASTSKEEAlMELKARAlqleeeliql 960
Cdd:PRK04863 432 LPDLTADNAEDWLEEFQAKEQEATEEL--------------LSLEQKLSVA-QAAHSQFEQA-YQLVRKI---------- 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 961 rqypvdlatgarAGprtvetqngrliEVERNNAtlvaekaalqgqlqhlegqlgslQGRAQELLLQSQRAQEHSSRLQAe 1040
Cdd:PRK04863 486 ------------AG------------EVSRSEA-----------------------WDVARELLRRLREQRHLAEQLQQ- 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1041 ksmMEMQGQELHRKLgvleEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLlvrhRDLKANMRALELAHRE 1120
Cdd:PRK04863 518 ---LRMRLSELEQRL----RQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESL----SESVSEARERRMALRQ 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1121 LQgrhEQLQAQRANVEAQEVALLAERERLMQdghrqrgLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLAR 1200
Cdd:PRK04863 587 QL---EQLQARIQRLAARAPAWLAAQDALAR-------LREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQA 656
|
....*...
gi 124486839 1201 LELERAQL 1208
Cdd:PRK04863 657 LDEEIERL 664
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
731-1223 |
2.81e-05 |
|
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: 48.81 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 731 EEQALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEALCLSEELaQARRTEAEAHQEAEAQAREQARLREAVDTASLELE 810
Cdd:TIGR00618 373 QQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRT-SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTA 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 811 AASREREALAEALAAAGRERRQWERDGPRLRAQVE---AAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQ 887
Cdd:TIGR00618 452 QCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETrkkAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQ 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 888 ELGDRLEHLQEELEQAALErqkfLQEQENQHQRYRHLEQRLEAELQAAsTSKEEALMELKARALQLEEELIQLRQypvdl 967
Cdd:TIGR00618 532 RGEQTYAQLETSEEDVYHQ----LTSERKQRASLKEQMQEIQQSFSIL-TQCDNRSKEDIPNLQNITVRLQDLTE----- 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 968 atgARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQ-LGSLQGRAQELLLQSQRAQEHSSRLQAEKSmmem 1046
Cdd:TIGR00618 602 ---KLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALkLTALHALQLTLTQERVREHALSIRVLPKEL---- 674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1047 qGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQG-RH 1125
Cdd:TIGR00618 675 -LASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHqAR 753
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1126 EQLQAQRANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGE-----------LQGERGEL 1194
Cdd:TIGR00618 754 TVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSdedilnlqcetLVQEEEQF 833
|
490 500
....*....|....*....|....*....
gi 124486839 1195 RSRLARLELERAQLEIQSQQLRESNQQLD 1223
Cdd:TIGR00618 834 LSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1126-1294 |
5.82e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1126 EQLQAQRANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLA--EVSRERGELQGERGELRSRLARLEL 1203
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1204 ERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYL 1283
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170
....*....|.
gi 124486839 1284 DQLNALRREKQ 1294
Cdd:COG4717 234 NELEAAALEER 244
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
984-1271 |
6.09e-05 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 46.98 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 984 RLIEVERNNATLVAEKAALQGQLQHLEGQ-LGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQgQELHRKLGVLEEEV 1062
Cdd:pfam15742 70 KLLDSTKMCSSLTAEWKHCQQKIRELELEvLKQAQSIKSQNSLQEKLAQEKSRVADAEEKILELQ-QKLEHAHKVCLTDT 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1063 RAARRAQEETRGQQ----QALLRDHEALVQLQRRQ-ETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEA 1137
Cdd:pfam15742 149 CILEKKQLEERIKEasenEAKLKQQYQEEQQKRKLlDQNVNELQQQVRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLEN 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1138 qevallaerERLMQDGHR--QRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRL-ARLELERAQLEIQSQQ 1214
Cdd:pfam15742 229 ---------EKRKSDEHLksNQELSEKLSSLQQEKEALQEELQQVLKQLDVHVRKYNEKHHHHkAKLRRAKDRLVHEVEQ 299
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 124486839 1215 LRESNQQLDlsacrltTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLES 1271
Cdd:pfam15742 300 RDERIKQLE-------NEIGILQQQSEKEKAFQKQVTAQNEILLLEKRKLLEQLTEQ 349
|
|
| MAP70 |
pfam07058 |
Microtubule-associated protein 70; This family represents a family of plant ... |
854-1107 |
6.30e-05 |
|
Microtubule-associated protein 70; This family represents a family of plant microtubule-associated proteins of size 70 kDa. The proteins contain four predicted coiled-coil domains, and truncation studies identify a central domain that targets the proteins to microtubules. It has no predicted trans-membrane domains, and the region between the coils from approximately residues 240-483 is the targetting region.
Pssm-ID: 399798 [Multi-domain] Cd Length: 544 Bit Score: 47.50 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 854 LESQVRCHLEEAEREHAEKQALRE---ELEKAVLrgqELGDRLEHLQEELEQA-ALERQKFLQEQENQHQRYRHLEQRLE 929
Cdd:pfam07058 12 LENEVRDKDRELGEALAEIKALRLserLKEKAVE---ELTDELLKLDEKLKASeNLLESKNLEIKKINDEKKAALAAQFA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 930 AELQAA---STSKEEALMELKARALQLEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAeKAALQGQL 1006
Cdd:pfam07058 89 AEATLRrvhAAQKDEDMPPIEAILAPLEAELKLARQEINKLQDDNKALDRLTKSKEAALLEAERAVQIALA-KASLVDDL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1007 QHlegqlgslqgRAQELLLQSQRAQEHSSRLQAeksmMEMQgqelhrKLGVLEEEVRAARRAQEETrgqqQALLRDHEAL 1086
Cdd:pfam07058 168 QN----------KNQELMKQIEICQEENKILDK----AHRQ------KVAEVEKLSQTVRELEEAV----LAGGAAANAV 223
|
250 260
....*....|....*....|.
gi 124486839 1087 VQLQRRQETELEGLLVRHRDL 1107
Cdd:pfam07058 224 RDYQRKVKEMNEERRTLEREL 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
730-1209 |
8.42e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 730 PEEQALRDEVAQLRREVAGLE---VKLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLREavdtas 806
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEelkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE------ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 807 leLEAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRcHLEEAEREHAEKQALREELEKAVLRG 886
Cdd:PRK03918 288 --LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE-RLEELKKKLKELEKRLEELEERHELY 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 887 QELGDRLEHLQE-ELEQAALERQKFLQEQENQHQRYRHLEQRLE------AELQAASTSKEEALMELKA---------RA 950
Cdd:PRK03918 365 EEAKAKKEELERlKKRLTGLTPEKLEKELEELEKAKEEIEEEISkitariGELKKEIKELKKAIEELKKakgkcpvcgRE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 951 LQLEEELIQLRQYPVDLA----TGARAGPRTVETQNgRLIEVER---NNATLVAEKAALQgQLQHLEGQLGS-----LQG 1018
Cdd:PRK03918 445 LTEEHRKELLEEYTAELKriekELKEIEEKERKLRK-ELRELEKvlkKESELIKLKELAE-QLKELEEKLKKynleeLEK 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1019 RAQELLLQSQRAQEHSSRLQAEKSMMEmQGQELHRKLGVLEEEVRAARRAQEETRGQQQALlrDHEALVQLQRRQEtELE 1098
Cdd:PRK03918 523 KAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEEL--GFESVEELEERLK-ELE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1099 GLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLmqDGHRQRGLEEELRRLQNEHERAQMLLA 1178
Cdd:PRK03918 599 PFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL--EELEKKYSEEEYEELREEYLELSRELA 676
|
490 500 510
....*....|....*....|....*....|.
gi 124486839 1179 EVSRERGELQGERGELRSRLARLELERAQLE 1209
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
840-1229 |
9.18e-05 |
|
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: 47.25 E-value: 9.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 840 LRAQVEAAEQQVQALESQVRchLEEAEREHAEKQALREELEKAV-------------LRGQELGDRLEHLQEELEQAALE 906
Cdd:COG3096 288 LELRRELFGARRQLAEEQYR--LVEMARELEELSARESDLEQDYqaasdhlnlvqtaLRQQEKIERYQEDLEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 907 RQKFLQEQENQHQRYRHLEQRLEAELQAASTS---KEEALMELKARALQLEEELIQLRQypvdlatgARAgprtvetqng 983
Cdd:COG3096 366 QEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQladYQQALDVQQTRAIQYQQAVQALEK--------ARA---------- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 984 RLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQgraQELLLQSQRAQEHSSRLQAEKSMM-EMQGQELHRKLGVLEEEV 1062
Cdd:COG3096 428 LCGLPDLTPENAEDYLAAFRAKEQQATEEVLELE---QKLSVADAARRQFEKAYELVCKIAgEVERSQAWQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1063 RAARrAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVAL 1142
Cdd:COG3096 505 RSQQ-ALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSEL 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1143 LAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELrsrlarLELERaQLEIQSQQLRESNQQL 1222
Cdd:COG3096 584 RQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQL------LERER-EATVERDELAARKQAL 656
|
....*..
gi 124486839 1223 DLSACRL 1229
Cdd:COG3096 657 ESQIERL 663
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
864-1260 |
9.40e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.10 E-value: 9.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 864 EAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLeaelqaastSKEEAL 943
Cdd:PRK10246 413 AALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQL---------ADVKTI 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 944 MELKARALQLEEELIQLRQYPVDLATGARAGPR-------TVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSL 1016
Cdd:PRK10246 484 CEQEARIKDLEAQRAQLQAGQPCPLCGSTSHPAveayqalEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRD 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1017 QGRAQELLLQSQ----RAQEHSSRLQAEKSMME-----MQGQELHRKL-----------GVLEEEVRAARRAQEETRGQQ 1076
Cdd:PRK10246 564 ESEAQSLRQEEQaltqQWQAVCASLNITLQPQDdiqpwLDAQEEHERQlrllsqrhelqGQIAAHNQQIIQYQQQIEQRQ 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1077 QAL--------------------LRDHEALVQLQRRQETELEGLLVRHRDLKANMRAL-----------ELAHRELQGRH 1125
Cdd:PRK10246 644 QQLltalagyaltlpqedeeaswLATRQQEAQSWQQRQNELTALQNRIQQLTPLLETLpqsddlphseeTVALDNWRQVH 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1126 EQ---LQAQRANVEAQEVallAERER--------------------------LMQDGHRQRgLEEELRRLQNEHERAQML 1176
Cdd:PRK10246 724 EQclsLHSQLQTLQQQDV---LEAQRlqkaqaqfdtalqasvfddqqaflaaLLDEETLTQ-LEQLKQNLENQRQQAQTL 799
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1177 LAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNqqldlsacrlTTQCELLTQLRsaQEEENRQ----LLA 1252
Cdd:PRK10246 800 VTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENT----------TRQGEIRQQLK--QDADNRQqqqaLMQ 867
|
....*...
gi 124486839 1253 EVQALSRE 1260
Cdd:PRK10246 868 QIAQATQQ 875
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1041-1247 |
1.04e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1041 KSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEaLVQLQRRQETELEGLlvrhRDLKANMRALELAHRE 1120
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG-LVDLSEEAKLLLQQL----SELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1121 LQGRHEQLQAQRA----------------NVEAQEVALLAERERLMQ---DGHRQ-RGLEEELRRLQNE-HERAQMLLAE 1179
Cdd:COG3206 238 AEARLAALRAQLGsgpdalpellqspviqQLRAQLAELEAELAELSArytPNHPDvIALRAQIAALRAQlQQEAQRILAS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124486839 1180 VSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSACRLTTqceLLTQLRSAQEEEN 1247
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES---LLQRLEEARLAEA 382
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
94-182 |
1.09e-04 |
|
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a microtubule-binding protein required for spermatid differentiation. It is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.
Pssm-ID: 411796 Cd Length: 150 Bit Score: 44.07 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 94 RMWNLCHLWGRLRDFYQEELQLLILSPP-PDLQTMG--CDPFseeavdELESILRLLLGASVQCEHRELFIRHIRGLSLD 170
Cdd:cd22225 61 KMSNLKKILQGIVDYYHEFLDQQISEFLlPDLNRIAehSDPV------ELGRLLQLILGCAVNCEKKQEHIQNIMTLEES 134
|
90
....*....|..
gi 124486839 171 VQSELAGAIQEV 182
Cdd:cd22225 135 VQHVVMTAIQEL 146
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1114-1226 |
1.20e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 46.19 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1114 LELAHRELQGRHEQLQAQRANVEAQEVALLAE---RERLMQDGHRQRGLEEELRRLQNEHERAQMLLAE--VSRErgELQ 1188
Cdd:COG1566 74 ARLDPTDLQAALAQAEAQLAAAEAQLARLEAElgaEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKgaVSQQ--ELD 151
|
90 100 110
....*....|....*....|....*....|....*...
gi 124486839 1189 GERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSA 1226
Cdd:COG1566 152 EARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQA 189
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
872-1099 |
1.21e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 872 KQALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQE--NQHQRYRHLEQRLeAELQAASTSKEEALMELKAR 949
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQL-SELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 950 ALQLEEELIQLRQYPVDLAtgaragprtvetQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQ-SQ 1028
Cdd:COG3206 242 LAALRAQLGSGPDALPELL------------QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQQ 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486839 1029 RAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEEtrgqQQALLRDHEALVQ-----LQRRQETELEG 1099
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE----LRRLEREVEVARElyeslLQRLEEARLAE 381
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
871-1222 |
1.36e-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: 46.22 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 871 EKQALREELEKAVLRGQELGDRLEHLQEELEQAALERQKfLQEQENQHQ-----------RYRHLEQRLEAeLQAASTSK 939
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKK-LQERLDQLEsgddsgtpggkKYLLLQKQLEQ-LQEENFRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 940 EEALMELKARALQLEEELIQLRQYPVDLaTGARAGPRTVETQNGRLIE----VERNNATLVAEKAALQgQLQHLEGQLGS 1015
Cdd:pfam05622 79 ETARDDYRIKCEELEKEVLELQHRNEEL-TSLAEEAQALKDEMDILREssdkVKKLEATVETYKKKLE-DLGDLRRQVKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1016 LQGRAQELLLQSQRAQEHSSRLQAEKSMMEM---QGQELHRKLgvlEEEVRAARRAQEETR---GQQQALLRDHEALV-- 1087
Cdd:pfam05622 157 LEERNAEYMQRTLQLEEELKKANALRGQLETykrQVQELHGKL---SEESKKADKLEFEYKkleEKLEALQKEKERLIie 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1088 --------------QLQRRQETELEGLLVRHRDLKANMRAlELAHRELQGRHEQLQAQ----RANVEAQEVALLAERERL 1149
Cdd:pfam05622 234 rdtlretneelrcaQLQQAELSQADALLSPSSDPGDNLAA-EIMPAEIREKLIRLQHEnkmlRLGQEGSYRERLTELQQL 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486839 1150 MQDGHRQRGLEEELRRLQNEHeraqmlLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNQQL 1222
Cdd:pfam05622 313 LEDANRRKNELETQNRLANQR------ILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSEL 379
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
849-1253 |
1.66e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.32 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 849 QQVQALESQVRCHLEEAEREH----AEKQALREELE--------------KAVLRGQELGDRLEHLQEELEQAALERQKF 910
Cdd:pfam01576 15 QKVKERQQKAESELKELEKKHqqlcEEKNALQEQLQaetelcaeaeemraRLAARKQELEEILHELESRLEEEEERSQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 911 LQEQENQHQRYRHLEQRLEAElQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVER 990
Cdd:pfam01576 95 QNEKKKMQQHIQDLEEQLDEE-EAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 991 NNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAAR-RAQ 1069
Cdd:pfam01576 174 KAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALaRLE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1070 EETRGQQQALLRDHEALVQLQRRQEtelegllvrhrDLKANMRALELAHRELQGRHEQLQAQRANVE------AQEVALL 1143
Cdd:pfam01576 254 EETAQKNNALKKIRELEAQISELQE-----------DLESERAARNKAEKQRRDLGEELEALKTELEdtldttAAQQELR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1144 AERERlmQDGHRQRGLEEELRR----LQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESN 1219
Cdd:pfam01576 323 SKREQ--EVTELKKALEEETRSheaqLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430
....*....|....*....|....*....|....
gi 124486839 1220 QQLDLSACRLTTQCELLtQLRSAQEEENRQLLAE 1253
Cdd:pfam01576 401 QDSEHKRKKLEGQLQEL-QARLSESERQRAELAE 433
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1028-1300 |
1.69e-04 |
|
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: 46.27 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1028 QRAQEHSSRLQAEKSMMEMqgqELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDL 1107
Cdd:pfam05557 5 IESKARLSQLQNEKKQMEL---EHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1108 KANMRALELAHRElqgrHEQLQAqranvEAQEVallaererlmqdghrQRGLEEELRRLQNEHERAQMLLAEVSRERGEL 1187
Cdd:pfam05557 82 KKYLEALNKKLNE----KESQLA-----DAREV---------------ISCLKNELSELRRQIQRAELELQSTNSELEEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1188 QGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENR--QLLAEVQAL-------- 1257
Cdd:pfam05557 138 QERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARipELEKELERLrehnkhln 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 124486839 1258 -SRENRELLERSLES-RDHLHREQrEYLDQLNALRREKQKLVEKI 1300
Cdd:pfam05557 218 eNIENKLLLKEEVEDlKRKLEREE-KYREEAATLELEKEKLEQEL 261
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
657-1345 |
1.96e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 657 AELTLREPLKDQKALDRELELSKQQKETGRHEQRPKGLESKLGPQKPQQTSEgvpdaWSREeptpgetLVSAIPEEQALR 736
Cdd:PRK04863 445 EEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWD-----VARE-------LLRRLREQRHLA 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 737 DEVAQLRREVAGLEVKLQAQaqrleaRSAEALclseeLAQARRTEAEAHQEAEAQAREQARLREAVDTASLELEAASRER 816
Cdd:PRK04863 513 EQLQQLRMRLSELEQRLRQQ------QRAERL-----LAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERR 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 817 EALAEALAAAGRERRQWERDGP----------RLRAQVEAAEQQVQALESQVRCHLEEaERE--------HAEKQALREE 878
Cdd:PRK04863 582 MALRQQLEQLQARIQRLAARAPawlaaqdalaRLREQSGEEFEDSQDVTEYMQQLLER-EREltverdelAARKQALDEE 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 879 LEKAVLRGQELGDRLEHLQE--------------ELEQAA-----------------LERQKflqeqenqhqryRHLEQR 927
Cdd:PRK04863 661 IERLSQPGGSEDPRLNALAErfggvllseiyddvSLEDAPyfsalygparhaivvpdLSDAA------------EQLAGL 728
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 928 ---------LEAELQAASTSKEEAlmELKARALQLEEELIQLR--QYPVDLATGARAGPRTVETQNGRLIEVERNNATLV 996
Cdd:PRK04863 729 edcpedlylIEGDPDSFDDSVFSV--EELEKAVVVKIADRQWRysRFPEVPLFGRAAREKRIEQLRAEREELAERYATLS 806
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 997 AEKAALQGQLQHL----------------EGQLGSLQGRAQELL--LQSQRAQEHSSRLQAEKSMMEMQG-QELHRKLGV 1057
Cdd:PRK04863 807 FDVQKLQRLHQAFsrfigshlavafeadpEAELRQLNRRRVELEraLADHESQEQQQRSQLEQAKEGLSAlNRLLPRLNL 886
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1058 LEEEVRAARraQEETRGQQQALLRDhEALVQLQRRQETELEGLLvrhrdlkANMRALELAHRELQGRHEQLQAQRANVEA 1137
Cdd:PRK04863 887 LADETLADR--VEEIREQLDEAEEA-KRFVQQHGNALAQLEPIV-------SVLQSDPEQFEQLKQDYQQAQQTQRDAKQ 956
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1138 QEVALlaerERLMQdghrqrgleeelRRLQNEHERAQMLLAEVSrergelqgergELRSRLarleleRAQLEIQSQQLRE 1217
Cdd:PRK04863 957 QAFAL----TEVVQ------------RRAHFSYEDAAEMLAKNS-----------DLNEKL------RQRLEQAEQERTR 1003
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1218 SNQQLDLSACRLTTQCELLTQLRS---AQEEENRQLLAEVQALS-RENRELLERSLESRDHLH------REQREYLDQ-- 1285
Cdd:PRK04863 1004 AREQLRQAQAQLAQYNQVLASLKSsydAKRQMLQELKQELQDLGvPADSGAEERARARRDELHarlsanRSRRNQLEKql 1083
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486839 1286 ------LNALRREKQKLVEKIMDQYRVLEPGplprtkKGSWlaDKVKRLIRP--------RREGALHGGPRLGA 1345
Cdd:PRK04863 1084 tfceaeMDNLTKKLRKLERDYHEMREQVVNA------KAGW--CAVLRLVKDngverrlhRRELAYLSADELRS 1149
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
983-1296 |
2.08e-04 |
|
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: 45.66 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 983 GRLIEVERNNATLVAEKAALQGQL----QHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVL 1058
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQRekekERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1059 EEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQ----------- 1127
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQteeelrslske 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1128 LQAQRANVEAQEVALLAERERLMQDGHR-----QRGLE-----EELRRLQNEHERAQMLLAEVSRERGELQGERGELRSR 1197
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKlttahRKEAEneallEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1198 LARLELERAQLEIqsqQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHR 1277
Cdd:pfam07888 274 LHQARLQAAQLTL---QLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGR 350
|
330
....*....|....*....
gi 124486839 1278 EQREYLDQLNALRREKQKL 1296
Cdd:pfam07888 351 EKDCNRVQLSESRRELQEL 369
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
204-385 |
2.34e-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: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 204 EELEMQLRSLTGMMSRLARERDLGAQRLAELLLEREPAHLLLPEAPANASAEGVSHHLAlQLTNAKAQLRRLRQEVEEKA 283
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIA-ELEAELERLDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 284 EQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALRERAGRLPRLQEELRrcreklqAAEVFKGQLEEERV 363
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL-------LEERFAAALGDAVE 764
|
170 180
....*....|....*....|....
gi 124486839 364 --LSEALEASKVLLEEQLEVARER 385
Cdd:COG4913 765 reLRENLEERIDALRARLNRAEEE 788
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
261-419 |
2.47e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 261 LALQLTNAKAQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALRERAGRLPRLQEE 340
Cdd:COG3206 210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPN 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 341 ---LRRCREKLQAAEVFKGQLEEERVLS-----EALEASKVLLEEQLEVARERSARLHETQRENLLLRTRLGEAHADLDS 412
Cdd:COG3206 290 hpdVIALRAQIAALRAQLQQEAQRILASleaelEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
|
....*..
gi 124486839 413 LRHQLEQ 419
Cdd:COG3206 370 LLQRLEE 376
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
976-1296 |
2.79e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 976 RTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQG--RAQElllQSQRAQEHSSRLQAEKSMMEMQGQELHR 1053
Cdd:PRK04863 300 RQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTalRQQE---KIERYQADLEELEERLEEQNEVVEEADE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1054 KLGVLEEEVRAARRAQEETRGQqqalLRDH-EALVQLQRR--QETELEGLLVRHRDLKANMralELAHRELQGRHEQLQA 1130
Cdd:PRK04863 377 QQEENEARAEAAEEEVDELKSQ----LADYqQALDVQQTRaiQYQQAVQALERAKQLCGLP---DLTADNAEDWLEEFQA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1131 QRANVeAQEVALLAERERLMQDGHRQ--------RGLEEELRRLQnEHERAQMLLAEVSRERGELQgERGELRSRLARLE 1202
Cdd:PRK04863 450 KEQEA-TEELLSLEQKLSVAQAAHSQfeqayqlvRKIAGEVSRSE-AWDVARELLRRLREQRHLAE-QLQQLRMRLSELE 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1203 LERAQLEIQSQQLRESNQQLDLSacrlTTQCELLTQLRSAQEeenrqllAEVQALSRENRELLERSLESRDHLhreqrey 1282
Cdd:PRK04863 527 QRLRQQQRAERLLAEFCKRLGKN----LDDEDELEQLQEELE-------ARLESLSESVSEARERRMALRQQL------- 588
|
330
....*....|....
gi 124486839 1283 lDQLNALRREKQKL 1296
Cdd:PRK04863 589 -EQLQARIQRLAAR 601
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
724-950 |
2.84e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 724 TLVSAIPEEQALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLREAVD 803
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 804 TASLELEAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAV 883
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124486839 884 LRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALMELKARA 950
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1036-1285 |
3.70e-04 |
|
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: 45.34 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1036 RLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQEtELEGLLVRHRDLKANMRALE 1115
Cdd:TIGR00618 202 RSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQ-LLKQLRARIEELRAQEAVLE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1116 LAHRELqgrheqlqaqraNVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELR 1195
Cdd:TIGR00618 281 ETQERI------------NRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1196 SRLARLELERAQLEIQSQQLRESNQQLDLSAcRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHL 1275
Cdd:TIGR00618 349 TLHSQEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA 427
|
250
....*....|
gi 124486839 1276 HREQREYLDQ 1285
Cdd:TIGR00618 428 HAKKQQELQQ 437
|
|
| MASE1 |
COG3447 |
Integral membrane sensor domain MASE1 [Signal transduction mechanisms]; |
828-1163 |
3.80e-04 |
|
Integral membrane sensor domain MASE1 [Signal transduction mechanisms];
Pssm-ID: 442670 [Multi-domain] Cd Length: 637 Bit Score: 45.18 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 828 RERRQWERDgpRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQAALER 907
Cdd:COG3447 291 AERRRQRLR--ERELALRAALELLALGLLLAALDDALLLLNARGLLLLALSLAALLLLRLALLLLLLALDALLLLLADDD 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 908 QKFLQEQENQHQRYRHLEQRLEAELQ-AASTSKEEALMELKARALQLEEELIQLRQYPVDLATGARAGPRTVETQNGRLI 986
Cdd:COG3447 369 RGELRGDLLRRRGATRLGAVVARLLRrSGGRGEEVVVLLVIAQVEEALELALRERREERLLERLALALELLAITAALLAA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 987 EVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQ---RAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVR 1063
Cdd:COG3447 449 ALLLALADLLLLLLAEAAQLLARALLLGLDRLLADAALAALAalaDLLGALLSAGLRRRGGRRLGARLIRSLLSRVLAEL 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1064 AARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVALL 1143
Cdd:COG3447 529 GAVELLLALIADLTEVALGAEALERLLERLLLALLGLGLAVAALLATLGLLLALLAALALSGAAALLALGAALLLAAAIL 608
|
330 340
....*....|....*....|
gi 124486839 1144 AERERLMQDGHRQRGLEEEL 1163
Cdd:COG3447 609 GLAAALLALLRLLGERARLL 628
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
876-1248 |
3.90e-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: 45.35 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 876 REELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRlEAELQAASTSKEEALMELKARALQLEE 955
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA-KKALEYYQLKEKLELEEEYLLYLDYLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 956 ELIQLRQypvDLATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSS 1035
Cdd:pfam02463 234 LNEERID---LLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1036 RLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKanmrale 1115
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES------- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1116 lAHRELQGRHEQLQAQRANVEAQEVALLAERERlmQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELR 1195
Cdd:pfam02463 384 -ERLSSAAKLKEEELELKSEEEKEAQLLLELAR--QLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 124486839 1196 SRLaRLELERAQLEIQSQQLRESNQQLDLsACRLTTQCELLTQLRSAQEEENR 1248
Cdd:pfam02463 461 LKD-ELELKKSEDLLKETQLVKLQEQLEL-LLSRQKLEERSQKESKARSGLKV 511
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
262-487 |
4.27e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 262 ALQLTNAKAQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEA-LRERAGRLPRLQEE 340
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAeLAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 341 LRRCREKL--QAAEVFK-GQLEEERVL-----SEALEASKVLLEEQLEVARERSARLHETQRENLLLRTRLGEAHADLDS 412
Cdd:COG4942 99 LEAQKEELaeLLRALYRlGRQPPLALLlspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124486839 413 LRHQLEQLVEENVELELELQRSLEpppgspgeaslpgaapSLQDEvREAEAGRLRAVERENRELRGQLQMLQAQL 487
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLA----------------RLEKE-LAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
239-379 |
5.73e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.56 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 239 EPAHLLLPEAPANASAEgvshhlalqltnAKAQLRRLRQEVEEKAEqlldsqaEVQGLEAEIRRLRQETQALSAQAKRAE 318
Cdd:PRK11448 130 KPGPFVPPEDPENLLHA------------LQQEVLTLKQQLELQAR-------EKAQSQALAEAQQQELVALEGLAAELE 190
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124486839 319 LYREEAEA----LRERAGRLPRlQEELRRCREKLQAAEVFKgqleeervLSEALeaSKVLLEEQL 379
Cdd:PRK11448 191 EKQQELEAqleqLQEKAAETSQ-ERKQKRKEITDQAAKRLE--------LSEEE--TRILIDQQL 244
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
203-397 |
5.79e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 203 AEELEMQLRSLTGMMSRLARERDLGAQRLAELLLEREPAH----LLLPEAPANASAEGVSHHlalQLTNAKAQLRRLRQE 278
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARieevMKLYEEEKKMKAEEAKKA---EEAKIKAEELKKAEE 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 279 VEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKR--------AELYREEAEALRERAGRLPRLQEELRRCRE--KL 348
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKkaeedkkkAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkKK 1710
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 124486839 349 QAAEVFKGQ--LEEERVLSEALEASKVLLEEQLEVARErsARLHETQRENL 397
Cdd:PTZ00121 1711 EAEEKKKAEelKKAEEENKIKAEEAKKEAEEDKKKAEE--AKKDEEEKKKI 1759
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
730-1169 |
5.86e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 730 PEEQALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLEL 809
Cdd:PRK02224 307 ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 810 EAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQvrchLEEAEREHAEKQALREElEKAVLRGQEL 889
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT----LRTARERVEEAEALLEA-GKCPECGQPV 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 890 GD------------RLEHLQEELEQAALERQKfLQEQENQHQRYRHLEQRLEAELQAASTSkEEALMELKARALQLEEEL 957
Cdd:PRK02224 462 EGsphvetieedreRVEELEAELEDLEEEVEE-VEERLERAEDLVEAEDRIERLEERREDL-EELIAERRETIEEKRERA 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 958 IQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEgQLGSLQGRAQELLLQSQRAQEHSSRL 1037
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREAL 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1038 QAEKSMMEMQGQELHRKLGVLEEEVRAAR--RAQEETRGQQQALLRDHEALVQLqRRQETELEGLLVRHRDLKANMRALE 1115
Cdd:PRK02224 619 AELNDERRERLAEKRERKRELEAEFDEARieEAREDKERAEEYLEQVEEKLDEL-REERDDLQAEIGAVENELEELEELR 697
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 124486839 1116 LAHRELQGRHEQLQAQRANVEAQEVALLAERERLmqdghRQRGLeEELRRLQNE 1169
Cdd:PRK02224 698 ERREALENRVEALEALYDEAEELESMYGDLRAEL-----RQRNV-ETLERMLNE 745
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
134-476 |
5.93e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 134 EEAVDELESILRLLLGASVQCEHRELFIRHIRGLSLDVQSELAGAIQEVTQ--PGAGVVLALAGPESGELVAEELEMQLR 211
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEaaARLLLLLEAEADYEGFLEGVKAALLLA 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 212 SLTGMMSRLARERDLGAQRLAELLLEREPAHLLLPEAPANASAEGVSHHLALQLtnAKAQLRRLRQEVEEKAEQLLDSQA 291
Cdd:COG1196 518 GLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA--GRATFLPLDKIRARAALAAALARG 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 292 EVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALRERAGRLPRLQEELRRcREKLQAAEVFKGQLEEERVLSEALEAS 371
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLR-EVTLEGEGGSAGGSLTGGSRRELLAAL 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 372 KVLLEEQLEVARERSARLHETQRENLLLRTRLGEAHADLDSLRHQLEQLVEENVELELELQRSLEPPPGSPGEASLPGAA 451
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALE 754
|
330 340
....*....|....*....|....*
gi 124486839 452 PSLQDEVREAEAGRLRAVERENREL 476
Cdd:COG1196 755 ELPEPPDLEELERELERLEREIEAL 779
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
253-350 |
6.32e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 253 SAEGVSHHLALQLTNAKAQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALRERAG 332
Cdd:COG2433 396 EAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIE 475
|
90
....*....|....*...
gi 124486839 333 RLPRLQEELRRCREKLQA 350
Cdd:COG2433 476 RLERELEEERERIEELKR 493
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
905-1226 |
6.68e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 905 LERQKFLQEQENQHQRYRHLEQRLEAElqaastsKEEALMELKARALQLEEELIQL----RQYPVDLATGARAGPRTVET 980
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQE-------KEEKAREVERRRKLEEAEKARQaemdRQAAIYAEQERMAMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 981 QNGRLIEVERNNATLVAEKAALQ-GQLQHLEgqlgslqgraqELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLE 1059
Cdd:pfam17380 351 ERIRQEERKRELERIRQEEIAMEiSRMRELE-----------RLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1060 EEVRAARRAQEETRGQQ-QALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQ 1138
Cdd:pfam17380 420 VEMEQIRAEQEEARQREvRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1139 EV-----ALLAER------ERLMQDghRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERaq 1207
Cdd:pfam17380 500 ELeerkqAMIEEErkrkllEKEMEE--RQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERER-- 575
|
330
....*....|....*....
gi 124486839 1208 lEIQSQQLRESNQQLDLSA 1226
Cdd:pfam17380 576 -EMMRQIVESEKARAEYEA 593
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
726-1281 |
6.86e-04 |
|
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: 44.33 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 726 VSAIPEEQALRDE-VAQLRREVAGLEVKLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLREAVDT 804
Cdd:pfam05483 270 ANQLEEKTKLQDEnLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSF 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 805 ASLELEAASREREALAEAlaaagrERRQWERDGPRLRaqVEAAEQQVQALEsqvrchLEEAEREHAEKQALREELEKAVL 884
Cdd:pfam05483 350 VVTEFEATTCSLEELLRT------EQQRLEKNEDQLK--IITMELQKKSSE------LEEMTKFKNNKEVELEELKKILA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 885 RGQELGD---RLEHLQEELEQAALERQKFLQEQENQhqryrhlEQRLEAELQAASTSKEEALMELKARALQLEEELIQlr 961
Cdd:pfam05483 416 EDEKLLDekkQFEKIAEELKGKEQELIFLLQAREKE-------IHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLK-- 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 962 qypvdlatgaragpRTVETQNGRLIEVErnNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAE- 1040
Cdd:pfam05483 487 --------------NIELTAHCDKLLLE--NKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDEl 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1041 ---KSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRAlela 1117
Cdd:pfam05483 551 esvREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSA---- 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1118 hrelqgRHEQLQAQRANVEAQEVALLAERERL--MQDGHRQ----RGLEEElrRLQNEHERAQMLLAEVSRERGELQGE- 1190
Cdd:pfam05483 627 ------ENKQLNAYEIKVNKLELELASAKQKFeeIIDNYQKeiedKKISEE--KLLEEVEKAKAIADEAVKLQKEIDKRc 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1191 RGELRSRLARLELERAQLEiqsQQLRESNQQLDLSACRLTTQcellTQLRSAQEEENRQLLAEVQALSREnrelLERSLE 1270
Cdd:pfam05483 699 QHKIAEMVALMEKHKHQYD---KIIEERDSELGLYKNKEQEQ----SSAKAALEIELSNIKAELLSLKKQ----LEIEKE 767
|
570
....*....|.
gi 124486839 1271 SRDHLHREQRE 1281
Cdd:pfam05483 768 EKEKLKMEAKE 778
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
731-1100 |
8.16e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 731 EEQALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEALCLSE---ELAQARRTEAEAHQEAEAQAREQ---ARLREAVDT 804
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSAresDLEQDYQAASDHLNLVQTALRQQekiERYQEDLEE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 805 ASLELEAASREREALAEALAAAGRERRQWERDGPRLRAQVE--------------AAEQQVQALE-SQVRCHLEEAEREH 869
Cdd:COG3096 359 LTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqqaldvqqtraiQYQQAVQALEkARALCGLPDLTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 870 AEkqalrEELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQ----------------------EQENQHQRYRHLEQR 927
Cdd:COG3096 439 AE-----DYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKayelvckiageversqawqtarELLRRYRSQQALAQR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 928 LEAelQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGAragPRTVETQNGRLIEVERNNATLVAEKAALQGQLQ 1007
Cdd:COG3096 514 LQQ--LRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEEL---EELLAELEAQLEELEEQAAEAVEQRSELRQQLE 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1008 HLEGQLGSLQGRAQELLlqsqRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALV 1087
Cdd:COG3096 589 QLRARIKELAARAPAWL----AAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLS 664
|
410
....*....|...
gi 124486839 1088 QLQRRQETELEGL 1100
Cdd:COG3096 665 QPGGAEDPRLLAL 677
|
|
| Mating_C |
pfam12737 |
C-terminal domain of homeodomain 1; Mating in fungi is controlled by the loci that determine ... |
468-589 |
9.42e-04 |
|
C-terminal domain of homeodomain 1; Mating in fungi is controlled by the loci that determine the mating type of an individual, and only individuals with differing mating types can mate. Basidiomycete fungi have evolved a unique mating system, termed tetrapolar or bifactorial incompatibility, in which mating type is determined by two unlinked loci; compatibility at both loci is required for mating to occur. The multi-allelic tetrapolar mating system is considered to be a novel innovation that could have only evolved once, and is thus unique to the mushroom fungi. This domain is C-terminal to the homeodomain transcription factor region.
Pssm-ID: 372279 [Multi-domain] Cd Length: 412 Bit Score: 43.44 E-value: 9.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 468 AVERENRELRGQLQMLQAQLgsqhpLLEEQRENSRQP-PVPNRDPATPSALHHSPQSPACQIGGEGsESLDLP---SPAS 543
Cdd:pfam12737 34 AVKDMTPDLKEQLKDEKKRK-----RQAERSMRDALAyPSPERSPASSPERNLSPQVDVCQLTIRQ-NNLNLKrrsSSSS 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 124486839 544 YSDITRSPKCSQAPDSHPELESPLQMVS-QDPQTSDQA-LQESDPTVE 589
Cdd:pfam12737 108 DVDSSNAERCHKRPRLDSPSSSSSPEKClPSPAPSEQEaLSEISAACG 155
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
264-468 |
9.58e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 9.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 264 QLTNAKAQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQ-AKRAELYREEAEALRERAGRLPRL----- 337
Cdd:COG3883 31 ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEiEERREELGERARALYRSGGSVSYLdvllg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 338 ----QEELRRCREKLQAAEVFKGQLEEERVLSEALEASKVLLEEQLEVARERSARLHETQREnllLRTRLGEAHADLDSL 413
Cdd:COG3883 111 sesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE---LEAQQAEQEALLAQL 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 124486839 414 RHQLEQLVEENVELELELQRSLEPPPGSPGEASLPGAAPSLQDEVREAEAGRLRA 468
Cdd:COG3883 188 SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
734-1229 |
9.71e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 44.08 E-value: 9.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 734 ALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEAL-CLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELEAA 812
Cdd:COG3899 746 ALLLELAEALYLAGRFEEAEALLERALAARALAALaALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGD 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 813 SREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDR 892
Cdd:COG3899 826 RRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALA 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 893 LEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGAR 972
Cdd:COG3899 906 AAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAA 985
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 973 AGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELH 1052
Cdd:COG3899 986 AAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAA 1065
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1053 RKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQR 1132
Cdd:COG3899 1066 AALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALA 1145
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1133 ANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQS 1212
Cdd:COG3899 1146 LAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLL 1225
|
490
....*....|....*..
gi 124486839 1213 QQLRESNQQLDLSACRL 1229
Cdd:COG3899 1226 LLLAALALAAALLALRL 1242
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
732-1231 |
9.91e-04 |
|
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: 44.06 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 732 EQALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEALCLSEELAQARRTEAEAHqeaeaqareqaRLREAVDTASLELEA 811
Cdd:pfam12128 421 ESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIE-----------RAREEQEAANAEVER 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 812 ASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQA--------LESQVRCHLEEAEREHAEKQALREELEKAV 883
Cdd:pfam12128 490 LQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPqagtllhfLRKEAPDWEQSIGKVISPELLHRTDLDPEV 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 884 LRGQELGDR-LEHLQEELEQAalerqkflqeqenQHQRYRHLEQRLEAELQAAstskEEALMELKARALQLEEELIQLRQ 962
Cdd:pfam12128 570 WDGSVGGELnLYGVKLDLKRI-------------DVPEWAASEEELRERLDKA----EEALQSAREKQAAAEEQLVQANG 632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 963 yPVDLA----TGARAGPRTVETQNGRLIEVERN-----NATLVAEKAALQGQLQHLEGQLGSLqGRAQELLLQSQRAQEH 1033
Cdd:pfam12128 633 -ELEKAsreeTFARTALKNARLDLRRLFDEKQSekdkkNKALAERKDSANERLNSLEAQLKQL-DKKHQAWLEEQKEQKR 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1034 SSRLQAEKSMMEMQGqELHRKLGVLEEEVrAARRAQEETRgqqqallrdheaLVQLQRRQETELEGLLVRhrdlKANMRA 1113
Cdd:pfam12128 711 EARTEKQAYWQVVEG-ALDAQLALLKAAI-AARRSGAKAE------------LKALETWYKRDLASLGVD----PDVIAK 772
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1114 LELAHRELQGRHEQLQAQRANVeaqevallAERERLMQdghrqrglEEELRRLQNEHERAQMLLAEVSRERGELQGERGE 1193
Cdd:pfam12128 773 LKREIRTLERKIERIAVRRQEV--------LRYFDWYQ--------ETWLQRRPRLATQLSNIERAISELQQQLARLIAD 836
|
490 500 510
....*....|....*....|....*....|....*...
gi 124486839 1194 LRSRLARLELERAQLEIQSQQLRESNQQLDLSACRLTT 1231
Cdd:pfam12128 837 TKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLAT 874
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
732-1167 |
1.00e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 43.74 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 732 EQALRDEVAQLRREVAGlEVKLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELEA 811
Cdd:COG5278 85 RAEIDELLAELRSLTAD-NPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 812 ASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGD 891
Cdd:COG5278 164 ALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 892 RLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGA 971
Cdd:COG5278 244 LLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 972 RAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQEL 1051
Cdd:COG5278 324 ALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1052 HRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQ 1131
Cdd:COG5278 404 AEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAA 483
|
410 420 430
....*....|....*....|....*....|....*.
gi 124486839 1132 RANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQ 1167
Cdd:COG5278 484 LAEAEAAAALAAAAALSLALALAALLLAAAEAALAA 519
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
871-1078 |
1.07e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 871 EKQALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLeAELQAASTSKEEALMELkARA 950
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI-AEAEAEIEERREELGER-ARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 951 LQLEE------ELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELL 1024
Cdd:COG3883 95 LYRSGgsvsylDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 124486839 1025 LQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQA 1078
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
265-500 |
1.13e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 265 LTNAKAQLRRLRQEVEEKaeqlldsqaEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALRERAgrlprlQEELRRC 344
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEK---------EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA------DEVLEEH 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 345 REKLQAAEVFKGQLEEERVLSEALEASKVLLEEQLEVARERSARLhETQRENLLLRTRLGEAHA------------DLDS 412
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEEL-EEERDDLLAEAGLDDADAeavearreeledRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 413 LRHQLEQLVEENVELELELQRSLEPPPGSPGEAS-LPGAAPSLQDEVREAEA------GRLRAVERENRELRGQLQMLQA 485
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEeLREEAAELESELEEAREavedrrEEIEELEEEIEELRERFGDAPV 405
|
250
....*....|....*
gi 124486839 486 QLGSQHPLLEEQREN 500
Cdd:PRK02224 406 DLGNAEDFLEELREE 420
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
264-446 |
1.25e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 264 QLTNAKAQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALsaQAKRAELYREEAEALRE--RAGRLPRLQ--- 338
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL--RAELEAQKEELAELLRAlyRLGRQPPLAlll 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 339 ------EELRR-------CREKLQAAEVFKGQLEEERVLSEALEASKVLLEEQLEVARERSARL--HETQRENLL--LRT 401
Cdd:COG4942 127 spedflDAVRRlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALeaLKAERQKLLarLEK 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 124486839 402 RLGEAHADLDSLRHQLEQLVEENVELELELQRSLEPPPGSPGEAS 446
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
984-1292 |
1.33e-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: 43.40 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 984 RLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEksmmeMQGQElhrKLGVLEEEVR 1063
Cdd:COG3096 286 RALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTA-----LRQQE---KIERYQEDLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1064 AARRAQEEtrgQQQALLRDHEALVQLQ-RRQETELEgllvrHRDLKANMRALELAHRELQGRHEQL-QAQRANVEAQEVA 1141
Cdd:COG3096 358 ELTERLEE---QEEVVEEAAEQLAEAEaRLEAAEEE-----VDSLKSQLADYQQALDVQQTRAIQYqQAVQALEKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1142 LLAE-------------RERLMQDGHRQRGLEEELRRLQ---NEHERAQMLL----AEVSRERG-----ELQGERGELRS 1196
Cdd:COG3096 430 GLPDltpenaedylaafRAKEQQATEEVLELEQKLSVADaarRQFEKAYELVckiaGEVERSQAwqtarELLRRYRSQQA 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1197 RLARLELERAQLEIQSQQLRESNQqldlsACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLH 1276
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLRQQQN-----AERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELR 584
|
330
....*....|....*.
gi 124486839 1277 REqreyLDQLNALRRE 1292
Cdd:COG3096 585 QQ----LEQLRARIKE 596
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
864-1308 |
1.40e-03 |
|
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: 43.17 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 864 EAEREHAEK--QALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEE 941
Cdd:pfam05483 175 EYEREETRQvyMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKEN 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 942 ALMELkarALQLEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNATL---VAEKAALQGQLQHLEGQLGSLQG 1018
Cdd:pfam05483 255 KMKDL---TFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLqrsMSTQKALEEDLQIATKTICQLTE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1019 RAQELLLQSQRAQEHSSRLQAeksmmemqgqELHRKLGVLEEEVRAARRAQEETRGQQQALL-------RDHEALVQLQR 1091
Cdd:pfam05483 332 EKEAQMEELNKAKAAHSFVVT----------EFEATTCSLEELLRTEQQRLEKNEDQLKIITmelqkksSELEEMTKFKN 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1092 RQETELEGL---LVRHRDLKANMRALELAHRELQGRHEQLqaqranveaqeVALLAERERLMQDghrqrgLEEELRRLQN 1168
Cdd:pfam05483 402 NKEVELEELkkiLAEDEKLLDEKKQFEKIAEELKGKEQEL-----------IFLLQAREKEIHD------LEIQLTAIKT 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1169 EHeraQMLLAEVSRERGELQGER---GELRSRLARLELERAQL--EIQSQQLRESNQQLDLSACRLTTQcELLTQLRSAQ 1243
Cdd:pfam05483 465 SE---EHYLKEVEDLKTELEKEKlknIELTAHCDKLLLENKELtqEASDMTLELKKHQEDIINCKKQEE-RMLKQIENLE 540
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124486839 1244 EEENrQLLAEVQALSRENREL-------LERSLESRDHLHREQREYLDQLNALRREKQKLVEKIMDQYRVLE 1308
Cdd:pfam05483 541 EKEM-NLRDELESVREEFIQKgdevkckLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIE 611
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
867-1284 |
1.48e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 867 REHAEKQALREELEKAVLrGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEA-LME 945
Cdd:COG4913 587 GTRHEKDDRRRIRSRYVL-GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdVAS 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 946 LKARALQLEEELIQLRQYPVDLATgaragprtvetqngrlievernnatlvaekaalqgqlqhLEGQLGSLQGRAQELLL 1025
Cdd:COG4913 666 AEREIAELEAELERLDASSDDLAA---------------------------------------LEEQLEELEAELEELEE 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1026 QSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRgQQQALLRDHEAlvQLQRRQETELEGLlvrHR 1105
Cdd:COG4913 707 ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER-FAAALGDAVER--ELRENLEERIDAL---RA 780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1106 DLKANMRALELAHRELQGR-HEQLQAQRANVEAQEvALLAERERLMQDG-HRqrgLEEELRRLQNEHERAQM--LLAEVS 1181
Cdd:COG4913 781 RLNRAEEELERAMRAFNREwPAETADLDADLESLP-EYLALLDRLEEDGlPE---YEERFKELLNENSIEFVadLLSKLR 856
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1182 RERGELQGERGELRSRLARLEL---ERAQLEIQSQQLRESNqqldlsacrlttqcELLTQLRSAQeeENRQLLAEVQALS 1258
Cdd:COG4913 857 RAIREIKERIDPLNDSLKRIPFgpgRYLRLEARPRPDPEVR--------------EFRQELRAVT--SGASLFDEELSEA 920
|
410 420 430
....*....|....*....|....*....|
gi 124486839 1259 RENR--ELLERsLESRDHLH--REQREYLD 1284
Cdd:COG4913 921 RFAAlkRLIER-LRSEEEESdrRWRARVLD 949
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
829-960 |
1.50e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.77 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 829 ERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLqEELEQAALERQ 908
Cdd:PRK12705 33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKL-DNLENQLEERE 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 124486839 909 KFLQEQENQhqrYRHLEQRLEAELQAASTSKEEALMELKARALQ--LEEELIQL 960
Cdd:PRK12705 112 KALSARELE---LEELEKQLDNELYRVAGLTPEQARKLLLKLLDaeLEEEKAQR 162
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
274-380 |
1.64e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 274 RLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSaqAKRAELYREEAEALREragRLPRLQEELRRCREKLQAAEV 353
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEAS--FERLAELRDELAELEE---ELEALKARWEAEKELIEEIQE 475
|
90 100
....*....|....*....|....*..
gi 124486839 354 FKGQLEEERVLSEALEASKVLLEEQLE 380
Cdd:COG0542 476 LKEELEQRYGKIPELEKELAELEEELA 502
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
269-419 |
1.70e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 269 KAQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALRERAGRLPRLQEELRRCREKL 348
Cdd:PRK03918 230 VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDEL 309
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486839 349 QAAEVFKGQLEEERvlsEALEASKVLLEEQLEVARERSARLHETQRENLLLRTRLgEAHADLDSLRHQLEQ 419
Cdd:PRK03918 310 REIEKRLSRLEEEI---NGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELER 376
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
188-499 |
1.90e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 188 GVVLALAGPESGELVAEELEMQLRSLTGMMSRLARERDLGAQRLAEL--------LLEREPAHLLLPEAPANASAEGVSH 259
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELsdasrkigEIEKEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 260 HLAL---QLTNAKAQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAeALRERAGRLPR 336
Cdd:TIGR02169 745 DLSSleqEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEA-RLREIEQKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 337 LQEELRRCREKLQAAEVFKGQLEEERV-LSEALEASKVLLEEQLEVARERSARLHE---------TQRENLL-----LRT 401
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRIDLKEQIKsIEKEIENLNGKKEELEEELEELEAALRDlesrlgdlkKERDELEaqlreLER 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 402 RLGEAHADLDSLRHQLEQ-------LVEENVELELELQRSLEPPPGSPGEASLPGAAPSLQDEVREAEAGRLRAVERENR 474
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSElkakleaLEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEE 983
|
330 340
....*....|....*....|....*
gi 124486839 475 ELRGQLqmlqaQLGSQHPLLEEQRE 499
Cdd:TIGR02169 984 VLKRLD-----ELKEKRAKLEEERK 1003
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1005-1149 |
2.04e-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: 41.45 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1005 QLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQ-------- 1076
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnke 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124486839 1077 -QALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQR----ANVEAQEVALLAERERL 1149
Cdd:COG1579 91 yEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELdeelAELEAELEELEAEREEL 168
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1148-1309 |
2.11e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1148 RLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLReSNQQLDlsac 1227
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-NNKEYE---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1228 RLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKIMDQYRVL 1307
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
..
gi 124486839 1308 EP 1309
Cdd:COG1579 173 PP 174
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
997-1301 |
2.13e-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: 42.63 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 997 AEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAeksmmeMQGQelhrkLGVLEEEVRAARRaqEETRGQQ 1076
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNK------LLPQ-----ANLLADETLADRL--EELREEL 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1077 QALLRDhEALVQLQRRQETELEGLLvrhrdlkANMRALELAHRELQGRHEQLQAQRANVEAQEVALlaerERLMQdghrq 1156
Cdd:COG3096 903 DAAQEA-QAFIQQHGKALAQLEPLV-------AVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFAL----SEVVQ----- 965
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1157 rgleeelRRLQNEHERAQMLLAEVSrergelqgergELRSRLarleleRAQLEIQSQQLRESNQQLDLSACRLTTQCELL 1236
Cdd:COG3096 966 -------RRPHFSYEDAVGLLGENS-----------DLNEKL------RARLEQAEEARREAREQLRQAQAQYSQYNQVL 1021
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486839 1237 TQLRSAQEEENRQLLA---EVQALS-RENRELLERSLESRDHLH------REQREYLD-QLNALRREKQKLVEKIM 1301
Cdd:COG3096 1022 ASLKSSRDAKQQTLQEleqELEELGvQADAEAEERARIRRDELHeelsqnRSRRSQLEkQLTRCEAEMDSLQKRLR 1097
|
|
| FtsB |
COG2919 |
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning]; |
271-320 |
2.16e-03 |
|
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442163 [Multi-domain] Cd Length: 96 Bit Score: 38.71 E-value: 2.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 124486839 271 QLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAkRAELY 320
Cdd:COG2919 30 AYRELRQEIAELEAENAKLKARNAELEAEVADLKDGPDYIEERA-REELG 78
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
203-352 |
2.21e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 203 AEELEMQLRSLTGMMSRLARERDLGAQRLAELLLEREPAHLLLPEAPANAsaegvshhlalQLTNAKAQLRRLRQEVEEK 282
Cdd:COG3206 214 AKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP-----------VIQQLRAQLAELEAELAEL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 283 AEQLLDSQAEVQGLEAEIRRLRQ-------------ETQALSAQAKRAELyREEAEALRERAGRLPRLQEELRRCREKLQ 349
Cdd:COG3206 283 SARYTPNHPDVIALRAQIAALRAqlqqeaqrilaslEAELEALQAREASL-QAQLAQLEARLAELPELEAELRRLEREVE 361
|
...
gi 124486839 350 AAE 352
Cdd:COG3206 362 VAR 364
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1079-1177 |
2.23e-03 |
|
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439942 [Multi-domain] Cd Length: 421 Bit Score: 42.30 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1079 LLRDHEALVQlqrrqetelEGLLVRHRDLKAN-MRALELAHRELQGRHEQLQAQRaNVEAQEVALL----AERERLMQD- 1152
Cdd:COG0172 6 LIRENPEAVK---------EALAKRGFDLDVDeLLELDEERRELQTEVEELRAER-NALSKEIGKAkkkgEEAEALIAEv 75
|
90 100
....*....|....*....|....*...
gi 124486839 1153 ---GHRQRGLEEELRRLQNEHERAQMLL 1177
Cdd:COG0172 76 kelKEEIKELEEELKELEEELDELLLSI 103
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
897-1156 |
2.50e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.32 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 897 QEELEQAALERQkfLQEQENQHQRYRHLEQRLEAELQAASTSKEEALMELKARALQLEEELIQLRQyPVDLATGARAGPR 976
Cdd:pfam05667 223 EEEWNSQGLASR--LTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSG-SSTTDTGLTKGSR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 977 TVETQNGRLIEVERNNATLVAEKAALQGQLQ-HLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKL 1055
Cdd:pfam05667 300 FTHTEKLQFTNEAPAATSSPPTKVETEEELQqQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQN 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1056 GVLEEEVRAARRAQE---ETRGQQQALLRDHEA----LVQLQRRQETELEGLLVRHRDLK--ANMRALELAHR--ELQGR 1124
Cdd:pfam05667 380 EELEKQYKVKKKTLDllpDAEENIAKLQALVDAsaqrLVELAGQWEKHRVPLIEEYRALKeaKSNKEDESQRKleEIKEL 459
|
250 260 270
....*....|....*....|....*....|....*..
gi 124486839 1125 HEQLQ-----AQRAnvEAQEVALLAERERLMQDGHRQ 1156
Cdd:pfam05667 460 REKIKevaeeAKQK--EELYKQLVAEYERLPKDVSRS 494
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
908-1330 |
2.79e-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: 42.34 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 908 QKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALMELKaralQLEEELIQLRQYPVDlATGARAGPRTVETQNGRLIE 987
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELE----SKEEQLSSYEDKLFD-VCGSQDEESDLERLKEEIEK 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 988 VERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEE-----V 1062
Cdd:TIGR00606 651 SSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRrdemlG 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1063 RAARRAQE---------ETRGQQQALLRDHEALVQLQRRQETELEGLLVRH---RDLKANMRALELAHRELQGRHEQLQA 1130
Cdd:TIGR00606 731 LAPGRQSIidlkekeipELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEesaKVCLTDVTIMERFQMELKDVERKIAQ 810
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1131 QRANVEAQEVALLAE--RERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQL 1208
Cdd:TIGR00606 811 QAAKLQGSDLDRTVQqvNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQL 890
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1209 EIQSQQLRESNQQLDLSACRL----TTQCELLTQ---LRSAQEEENRQLLAEVQALSRE-------NRELLERSLESRDH 1274
Cdd:TIGR00606 891 VELSTEVQSLIREIKDAKEQDspleTFLEKDQQEkeeLISSKETSNKKAQDKVNDIKEKvknihgyMKDIENKIQDGKDD 970
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 124486839 1275 LHREQREYLDQLNALRREKQKLVEKIMDQYRVLEPGPLPRTKKGSWLADKVKRLIR 1330
Cdd:TIGR00606 971 YLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKR 1026
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
835-1226 |
2.92e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.20 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 835 RDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQ 914
Cdd:COG5278 131 RAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 915 ENQHQRYRHLEQRLEAELQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNAT 994
Cdd:COG5278 211 AELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALE 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 995 LVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRG 1074
Cdd:COG5278 291 LAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1075 QQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLMQDGH 1154
Cdd:COG5278 371 AALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELA 450
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124486839 1155 RQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSA 1226
Cdd:COG5278 451 EAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALA 522
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
976-1299 |
3.05e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 976 RTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQ--ELHR 1053
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERleELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1054 KLGVLEEEVRAARRAQEETRGQQQALlrdHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRA 1133
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEEL---EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1134 NVEAQEVALlAERERLMQDGHRQRGL----------EEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLEL 1203
Cdd:COG4717 231 QLENELEAA-ALEERLKEARLLLLIAaallallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1204 ERAQLEIQSQQLRESNQQLDLSAC-----------RLTTQCELLTQLRSAQEE--------ENRQLLAEVQALSRENREL 1264
Cdd:COG4717 310 LPALEELEEEELEELLAALGLPPDlspeellelldRIEELQELLREAEELEEElqleeleqEIAALLAEAGVEDEEELRA 389
|
330 340 350
....*....|....*....|....*....|....*
gi 124486839 1265 LERSLESRDHLHREQREYLDQLNALRREKQKLVEK 1299
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1126-1298 |
3.19e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1126 EQLQAQRANVEAQEVALLA--ERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLeL 1203
Cdd:COG3206 182 EQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL-L 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1204 ERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYL 1283
Cdd:COG3206 261 QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLE 340
|
170
....*....|....*
gi 124486839 1284 DQLNALRREKQKLVE 1298
Cdd:COG3206 341 ARLAELPELEAELRR 355
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
437-615 |
3.78e-03 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 42.06 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 437 PPPGSPGEASLPGAAPSLQDEVREAEAGRLRAVERenrelrgQLQMLQAQLGSQHPLLEEqrenSRQPPVPNRDP--ATP 514
Cdd:pfam03154 199 PTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQ-------TPTLHPQRLPSPHPPLQP----MTQPPPPSQVSpqPLP 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 515 SALHHSPQSPACQIGGEGSESLDLP-SPASYSDITRSPKCSQAPDSHPELESPLQMVSQDPQTSDQALQESDPTvethqc 593
Cdd:pfam03154 268 QPSLHGQMPPMPHSLQTGPSHMQHPvPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPR------ 341
|
170 180
....*....|....*....|..
gi 124486839 594 lEKSGHRVPLQSPIVWDPPQGP 615
Cdd:pfam03154 342 -EQPLPPAPLSMPHIKPPPTTP 362
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
273-419 |
4.16e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 41.25 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 273 RRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALREragRLPRLQEELRRCREKLQAAE 352
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQA---AVKAAQAQLAQAQIDLARRR 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486839 353 VF-------KGQLEEERVLSEALEASKVLLEEQLEVARERSARLHETQREnlLLRTRLGEAHADLDSLRHQLEQ 419
Cdd:pfam00529 131 VLapiggisRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQA--EVRSELSGAQLQIAEAEAELKL 202
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
269-419 |
4.40e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.65 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 269 KAQLRRLRQEVEEKAEQL----------------LDSQAEVQG--------LEAEIRRLRQETQALSAQAKRAELYREEA 324
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVerrrkleeaekarqaeMDRQAAIYAeqermameRERELERIRQEERKRELERIRQEEIAMEI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 325 EALRERAGRLPRLQEELRRCREKLQAAEVFKGQLEEERVLSEALEASKVLLEEQLEVARERSARLHETQRENLLLRTRLG 404
Cdd:pfam17380 375 SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE 454
|
170
....*....|....*..
gi 124486839 405 EA--HADLDSLRHQLEQ 419
Cdd:pfam17380 455 EQerQQQVERLRQQEEE 471
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
264-352 |
4.66e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 264 QLTNAKAQLRRLRQEVEE-KAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAK----RAELYREEAEALRERAGRLPRLQ 338
Cdd:COG0542 412 ELDELERRLEQLEIEKEAlKKEQDEASFERLAELRDELAELEEELEALKARWEaekeLIEEIQELKEELEQRYGKIPELE 491
|
90
....*....|....
gi 124486839 339 EELRRCREKLQAAE 352
Cdd:COG0542 492 KELAELEEELAELA 505
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
264-342 |
4.74e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 264 QLTNAKAQLRRL---RQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALR-ERAGRLPRLQE 339
Cdd:PHA02562 307 KLKELQHSLEKLdtaIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFvDNAEELAKLQD 386
|
...
gi 124486839 340 ELR 342
Cdd:PHA02562 387 ELD 389
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
743-1292 |
5.18e-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: 41.26 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 743 RREVAGLEVKLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELEAASREREALAEA 822
Cdd:pfam05557 26 KRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 823 LAAAGRERRqwerdgpRLRAQVEAAEQQVQALESqvrchleeaerehaEKQALREELEKAVLRGQELGDRLEHLqeeleq 902
Cdd:pfam05557 106 ISCLKNELS-------ELRRQIQRAELELQSTNS--------------ELEELQERLDLLKAKASEAEQLRQNL------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 903 aalerQKFLQEQENQHQRYRHLEQRLeaELQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGARAGPRTVETQN 982
Cdd:pfam05557 159 -----EKQQSSLAEAEQRIKELEFEI--QSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 983 GRLIEVERNNATLvAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSR----------LQAEKSMMEMQGQELH 1052
Cdd:pfam05557 232 DLKRKLEREEKYR-EEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRieqlqqreivLKEENSSLTSSARQLE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1053 RKLGVLEEEVRAARRAQEEtrgqQQALLRDHEALVQ-LQRR-----QETELEGLLVRHRDLKANM----RALELAHRELQ 1122
Cdd:pfam05557 311 KARRELEQELAQYLKKIED----LNKKLKRHKALVRrLQRRvllltKERDGYRAILESYDKELTMsnysPQLLERIEEAE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1123 GRHEQLQAQRANVEAQeVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVS---RERGELQGERGELRSRLA 1199
Cdd:pfam05557 387 DMTQKMQAHNEEMEAQ-LSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDslrRKLETLELERQRLREQKN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1200 RLELERAQLEIQsqqlresnQQLDLSACR-LTTQCELLTQLRSAQEEENRQLLAEVQALSRENReLLERSLESRDHLHRE 1278
Cdd:pfam05557 466 ELEMELERRCLQ--------GDYDPKKTKvLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLK-KLEDDLEQVLRLPET 536
|
570
....*....|....*
gi 124486839 1279 QREYLDQ-LNALRRE 1292
Cdd:pfam05557 537 TSTMNFKeVLDLRKE 551
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
866-1157 |
5.55e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 40.82 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 866 EREHAEKQALREELEKAVLRGQELGDRLEHLQ---EELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEA 942
Cdd:pfam19220 58 AQERAAYGKLRRELAGLTRRLSAAEGELEELVarlAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 943 LMELKA----------RALQLEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQ 1012
Cdd:pfam19220 138 EEENKAlreeaqaaekALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQ 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1013 LGSLQGRAQELLLQSQRAQEhssRLQAEKSMMEMQGQELHRKLGVLE--------------EEVRAARRAQEETRGQQQA 1078
Cdd:pfam19220 218 LAAEQAERERAEAQLEEAVE---AHRAERASLRMKLEALTARAAATEqllaearnqlrdrdEAIRAAERRLKEASIERDT 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1079 LLRDHEALVQLQRRQETELEGLLVRH-----------RDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVALLAERE 1147
Cdd:pfam19220 295 LERRLAGLEADLERRTQQFQEMQRARaeleeraemltKALAAKDAALERAEERIASLSDRIAELTKRFEVERAALEQANR 374
|
330
....*....|
gi 124486839 1148 RLMQDGHRQR 1157
Cdd:pfam19220 375 RLKEELQRER 384
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
830-1198 |
6.42e-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: 41.31 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 830 RRQWERDgprLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQAaLERQK 909
Cdd:pfam01576 726 KAQFERD---LQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEA-VKQLK 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 910 FLQEQENQHQRyrhleqrleaELQAASTSKEEALM---ELKARALQLEEELIQLRQypvDLATGARAgPRTVETQNGRLI 986
Cdd:pfam01576 802 KLQAQMKDLQR----------ELEEARASRDEILAqskESEKKLKNLEAELLQLQE---DLAASERA-RRQAQQERDELA 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 987 EVERNNAT----LVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAE--------------KSMMEMQG 1048
Cdd:pfam01576 868 DEIASGASgksaLQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTElaaerstsqksesaRQQLERQN 947
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1049 QELHRKLGVLEEEVRAARRAQEETRGQQQALLRDhealvQL-QRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQ 1127
Cdd:pfam01576 948 KELKAKLQEMEGTVKSKFKSSIAALEAKIAQLEE-----QLeQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYK 1022
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486839 1128 LQAQRANVeaqevallaereRLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRL 1198
Cdd:pfam01576 1023 DQAEKGNS------------RMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
270-419 |
6.58e-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: 39.91 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 270 AQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALRERA-GRLPRL--QEELRRCRE 346
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeEQLGNVrnNKEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486839 347 KLQAAEVFKGQLEEE-RVLSEALEASKVLLEEQLEVARERSARLHETQREnllLRTRLGEAHADLDSLRHQLEQ 419
Cdd:COG1579 97 EIESLKRRISDLEDEiLELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREE 167
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
998-1226 |
7.44e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 998 EKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKsmmemqgQELHRKLGVLEEEVRAARRAQEetrgQQQ 1077
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL-------EALQAEIDKLQAEIAEAEAEIE----ERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1078 ALLRDHEALVQLQRRQETELEGLLVRH--RDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLMQdghR 1155
Cdd:COG3883 86 EELGERARALYRSGGSVSYLDVLLGSEsfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA---L 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486839 1156 QRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSA 1226
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
793-1292 |
7.94e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 41.00 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 793 REQARLREAVDTASLELEAASREREALAEALAAAGRERRQWERDG-PRLRAQVEAAEQQVQALESQVRCHLEEAEREHAE 871
Cdd:COG3899 742 EYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGnPPASARAYANLGLLLLGDYEEAYEFGELALALAE 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 872 KQALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALMELKARAL 951
Cdd:COG3899 822 RLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAA 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 952 QLEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQ 1031
Cdd:COG3899 902 AALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAA 981
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1032 EHSSRLQAeksmmemQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANM 1111
Cdd:COG3899 982 AAAAAAAA-------ALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAA 1054
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1112 RALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGER 1191
Cdd:COG3899 1055 AAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAA 1134
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1192 GELRSRLARLELERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLES 1271
Cdd:COG3899 1135 LLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALAL 1214
|
490 500
....*....|....*....|.
gi 124486839 1272 RDHLHREQREYLDQLNALRRE 1292
Cdd:COG3899 1215 LALEAAALLLLLLLAALALAA 1235
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
828-1180 |
8.37e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.94 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 828 RERRQWERDGPRLRAQVEAAEQQVQALESqvrchleEAEREHAEKQALREELekavlrgQELGDRLE---HLQEELeqaa 904
Cdd:PRK10246 537 KEVKKLGEEGAALRGQLDALTKQLQRDES-------EAQSLRQEEQALTQQW-------QAVCASLNitlQPQDDI---- 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 905 lerQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALME--LKARALQLEEeliQLRQYPVDL-ATGARAGPRTVETQ 981
Cdd:PRK10246 599 ---QPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQqqIEQRQQQLLT---ALAGYALTLpQEDEEASWLATRQQ 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 982 NGRLIEVERNnatlvaEKAALQGQLQHLEG------QLGSLQGRAQELLLQSQRaQEHSSRLQAEKSMMEMQGQELHRKL 1055
Cdd:PRK10246 673 EAQSWQQRQN------ELTALQNRIQQLTPlletlpQSDDLPHSEETVALDNWR-QVHEQCLSLHSQLQTLQQQDVLEAQ 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1056 GVLEEEVRAARRAQEETRGQQQALLR---DHEALVQLQRRQETeLEGLLVRHRDLKAnmRALELAHRELQGRHEQLQAQr 1132
Cdd:PRK10246 746 RLQKAQAQFDTALQASVFDDQQAFLAallDEETLTQLEQLKQN-LENQRQQAQTLVT--QTAQALAQHQQHRPDGLDLT- 821
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 124486839 1133 ANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEV 1180
Cdd:PRK10246 822 VTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQALMQQI 869
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1103-1303 |
8.67e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.44 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1103 RHRDLKANMRALELAHRELQGRHEQLQAQ-----RANVEAQE-VALLAERERLMQDGHRQRGLEEELRRLQNEHERAQML 1176
Cdd:COG0497 166 AWRALKKELEELRADEAERARELDLLRFQleeleAAALQPGEeEELEEERRRLSNAEKLREALQEALEALSGGEGGALDL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1177 LAEVSRERGELQGERGELRSRLARleLERAQLEIQ--SQQLRESNQQLDLSACRLTTQCELLTQLRSAQ-------EEen 1247
Cdd:COG0497 246 LGQALRALERLAEYDPSLAELAER--LESALIELEeaASELRRYLDSLEFDPERLEEVEERLALLRRLArkygvtvEE-- 321
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486839 1248 rqlLAEVQALSRENRELLERSLESRDHLHRE----QREYLD---QLNALRREK-QKLVEKIMDQ 1303
Cdd:COG0497 322 ---LLAYAEELRAELAELENSDERLEELEAElaeaEAELLEaaeKLSAARKKAaKKLEKAVTAE 382
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
741-1264 |
8.92e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 741 QLRREVAGLEVKLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELEAASREREALA 820
Cdd:pfam01576 458 KLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 821 EALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQvrchleeaerehaeKQALREELEKAVLRgqelGDRLEHLQEEL 900
Cdd:pfam01576 538 GTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKT--------------KNRLQQELDDLLVD----LDHQRQLVSNL 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 901 EQAALERQKFLQEQENQHQRYRHLEQRLEAELQAAST---SKEEALMELKARALQLEEELIQLRQYPVDLATGARAGPRT 977
Cdd:pfam01576 600 EKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETralSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKN 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 978 VEtqngrliEVERNNATLVAEKAALQGQLQHLEGQLGSLQgraqelllqsqraqehSSRLQAEKSMMEMQGQelhrklgv 1057
Cdd:pfam01576 680 VH-------ELERSKRALEQQVEEMKTQLEELEDELQATE----------------DAKLRLEVNMQALKAQ-------- 728
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1058 LEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEG----LLVRHRDLKANMRALELAHRELQGRHEQLQAQRA 1133
Cdd:pfam01576 729 FERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAakkkLELDLKELEAQIDAANKGREEAVKQLKKLQAQMK 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486839 1134 NVEAQEVALLAERERLM----QDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLE 1209
Cdd:pfam01576 809 DLQRELEEARASRDEILaqskESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLE 888
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124486839 1210 IQSQQLRESNQQLDLSA-------CRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENREL 1264
Cdd:pfam01576 889 ARIAQLEEELEEEQSNTellndrlRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKEL 950
|
|
| |
