|
Name |
Accession |
Description |
Interval |
E-value |
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
10-183 |
2.84e-72 |
|
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: 238.58 E-value: 2.84e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 10 RGFLSGSLATWALGLAGLVGEAEESAGGTEEEEEEeeeeGALCTEKRFLRLIDGALLLRVLGIIAPSSRGGLRMvRGRDG 89
Cdd:cd22230 1 EEFMSGALVTWALGFEGLVGEEEDSLGFPEEEEEE----GTLDAEKRFLRLSNGDLLNRVMGIIDPSPRGGPRM-RGDDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 90 PAACRMWNLCHLWGRLRDFYQE-LQLLILSPPPDLQTMGCDPFSEEAVDELESILRLLLGASVQCEHRELFIRHIRGLSL 168
Cdd:cd22230 76 PAAHRVQNLHILWGRLRDFYQEeLQQLILSPPPDLQVMGRDPFTEEAVQELEKLLRLLLGAAVQCERRELFIRHIQGLDL 155
|
170
....*....|....*
gi 1907133161 169 DVQSELAGAIQEVTQ 183
Cdd:cd22230 156 DVQAELAEAIQEVTQ 170
|
|
| HkD_HkRP |
cd22223 |
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, ... |
12-183 |
5.82e-41 |
|
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: 148.12 E-value: 5.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 12 FLSGSLATWALGLAGLVGEaeesaggteeeeeeeeeegalctEKRFLRLIDGALLLRVLGIIAPSSRGgLRMVRGRDGPA 91
Cdd:cd22223 1 FLSSPLVTWAKTFADDGSA-----------------------ELSYTDLVDGVFLNNVMLQIDPRPFS-EVSNRNVDDDV 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 92 ACRMWNLCHLWGRLRDFYQE-LQLLILSPPPDLQTMGCDPFSEEAVDELESILRLLLGASVQCEHRELFIRHIRGLSLDV 170
Cdd:cd22223 57 NARIQNLDLLLRNIKSFYQEvLQQLIVMKLPDILTIGREPESEQSLEELEKLLLLLLGCAVQCERKEEFIERIKNLDLEV 136
|
170
....*....|...
gi 1907133161 171 QSELAGAIQEVTQ 183
Cdd:cd22223 137 QHALVACIQEVTD 149
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
732-1301 |
2.16e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 124.28 E-value: 2.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 732 QALRDEVAQLRREVAGLEVK-LQAQAQRLEARSAEalcLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELEA 810
Cdd:COG1196 216 RELKEELKELEAELLLLKLReLEAELEELEAELEE---LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 811 ASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGD 890
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 891 RLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALmELKARALQLEEELIQLRQypvdlATGA 970
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE-ELEEALAELEEEEEEEEE-----ALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 971 RAgprtvETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQEL 1050
Cdd:COG1196 447 AA-----EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1051 HRKLGVLEEEVRAARRAQEETRGQqqallrdhEALVQLQRRQETELEGLLVRHRDLKANmRALELAHRELQGRHEQLQAQ 1130
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALEAALA--------AALQNIVVEDDEVAAAAIEYLKAAKAG-RATFLPLDKIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1131 RANVEAQEVALLAERERLMQDGHRQRGLEEELRRLqnEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQ 1210
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL--VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1211 SQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRR 1290
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
570
....*....|.
gi 1907133161 1291 EKQKLVEKIMD 1301
Cdd:COG1196 751 EALEELPEPPD 761
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
201-959 |
1.58e-21 |
|
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: 102.44 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 201 VAEELEMQLRSLTGMMSRLARERDLGAQ------RLAELLLEREPAHLLLPEAPANASAEGVsHHLALQLTNAKAQLRRL 274
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKAERYKELKAElrelelALLVLRLEELREELEELQEELKEAEEEL-EELTAELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 275 RQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALRERAG-RLPRLQEELRRCREKLQAAEV- 352
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELEsKLDELAEELAELEEKLEELKEe 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 353 ---FKGQLEEERVLSEALEASKVLLEEQLEvarERSARLHETQRENLLLRTRLGEAHADLDSLRHQLEQLVEENVELELE 429
Cdd:TIGR02168 353 lesLEAELEELEAELEELESRLEELEEQLE---TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 430 LQR------SLEPPPGSPGEASLPGAAPSLQDEVREAEAgRLRAVERENRELRGQLQMLQAQLGSqhplLEEQRENSRQP 503
Cdd:TIGR02168 430 LEEaelkelQAELEELEEELEELQEELERLEEALEELRE-ELEEAEQALDAAERELAQLQARLDS----LERLQENLEGF 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 504 PVPNRDPATPSALHHSPQSPACQI-----GGEGSESLDLPSPASYSDITRSPKCSQAPDSHPELESPLQMVSQDPQTSDQ 578
Cdd:TIGR02168 505 SEGVKALLKNQSGLSGILGVLSELisvdeGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGT 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 579 ALQESDPTVethqcLEKSGHRVPLQSPIVWDPPQGP--------EVRI-----EVQELLGETGSREA---PQGELVHKAQ 642
Cdd:TIGR02168 585 EIQGNDREI-----LKNIEGFLGVAKDLVKFDPKLRkalsyllgGVLVvddldNALELAKKLRPGYRivtLDGDLVRPGG 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 643 VL--------------KQESPKCRPRSAELT-----LREPLKDQKALDRELELSKQQKETGRHEQRPKGLESKLGPQKPQ 703
Cdd:TIGR02168 660 VItggsaktnssilerRREIEELEEKIEELEekiaeLEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 704 QTSEGVPDAWSREEptpgETLVSAIPEEQALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEALCLSEELAQARRTEAEA 783
Cdd:TIGR02168 740 AEVEQLEERIAQLS----KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 784 HQEAEAQAREQARLREAVDTASLELEAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESqvrcHLEE 863
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE----ALAL 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 864 AEREHAEKQALREELEKAVlrgQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALM 943
Cdd:TIGR02168 892 LRSELEELSEELRELESKR---SELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
810
....*....|....*.
gi 1907133161 944 ELKARALQLEEELIQL 959
Cdd:TIGR02168 969 EARRRLKRLENKIKEL 984
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
57-183 |
1.65e-21 |
|
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: 92.55 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 57 FLRLIDGALLLRVLGIIAPSSRGGlRMVRGRDGPAACRMWNLCHLWGRLRDFYQE-LQLLILSPPPDLQTMGCDPFSEEA 135
Cdd:cd22229 30 YVALVDGVFLNEVMLQINPKSSNQ-RVNKKVNNDASLRIQNLSILVKQIKLYYQEtLQQLIMMSLPNVLVLGRNPLSEQG 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1907133161 136 VDELESILRLLLGASVQCEHRELFIRHIRGLSLDVQSELAGAIQEVTQ 183
Cdd:cd22229 109 TEEMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEVTH 156
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
730-1222 |
3.55e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.78 E-value: 3.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 730 EEQALRDEVAQLRREVAglevKLQAQAQRLEARSAEalcLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELE 809
Cdd:COG1196 282 ELEEAQAEEYELLAELA----RLEQDIARLEERRRE---LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 810 AASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELG 889
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 890 DRLEHLQEELEQAALERQKfLQEQENQHQRYRHLEQRLEAELQAASTSKEEALMELKARALQLEEELIQLRQYPVD-LAT 968
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAE-LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvKAA 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 969 GARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQ----------LQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQA 1038
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQnivveddevaAAAIEYLKAAKAGRATFLPLDKIRARAALAAALA 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1039 EKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHR 1118
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1119 ELQGRHEQLQAQRANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLA 1198
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAL 753
|
490 500
....*....|....*....|....
gi 1907133161 1199 RLELERAQLEIQSQQLRESNQQLD 1222
Cdd:COG1196 754 EELPEPPDLEELERELERLEREIE 777
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
838-1292 |
5.48e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.40 E-value: 5.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 838 RLRAQVEAAEQ----QVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQ 913
Cdd:COG1196 204 PLERQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 914 ENQHQRYRHLEQRLEaELQAASTSKEEALMELKARALQLEEELIQLRQypvdlatgaragprtvetqngRLIEVERNNAT 993
Cdd:COG1196 284 EEAQAEEYELLAELA-RLEQDIARLEERRRELEERLEELEEELAELEE---------------------ELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 994 LVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRG 1073
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1074 QQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLMQDGH 1153
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1154 RQRGLEEELRRLQNEhERAQMLLAEVSRERGELQGERGELRSRLARLeLERAQLEIQSQQLRESNQQLDLSACRLTTQCE 1233
Cdd:COG1196 502 DYEGFLEGVKAALLL-AGLRGLAGAVAVLIGVEAAYEAALEAALAAA-LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL 579
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907133161 1234 LLTQLRSAQEEENRQL--LAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREK 1292
Cdd:COG1196 580 DKIRARAALAAALARGaiGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
730-1299 |
5.84e-20 |
|
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: 97.05 E-value: 5.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 730 EEQALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELE 809
Cdd:TIGR02168 282 EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 810 AASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLrgQELG 889
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL--KELQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 890 DRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRL---EAELQAAStSKEEALMELKARALQLEEELIQLRQY---- 962
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALdaaERELAQLQ-ARLDSLERLQENLEGFSEGVKALLKNqsgl 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 963 -------------------PVDLATGARAGPRTVETQN--------------------------GRLIEVERNNAT---- 993
Cdd:TIGR02168 519 sgilgvlselisvdegyeaAIEAALGGRLQAVVVENLNaakkaiaflkqnelgrvtflpldsikGTEIQGNDREILknie 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 994 --------LVAEKAALQGQLQHLEGQL---GSLQGrAQELLLQSQ----------------------RAQEHSSRLQAEK 1040
Cdd:TIGR02168 599 gflgvakdLVKFDPKLRKALSYLLGGVlvvDDLDN-ALELAKKLRpgyrivtldgdlvrpggvitggSAKTNSSILERRR 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1041 SMmemqgQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLlvrhrdlKANMRALELAHREL 1120
Cdd:TIGR02168 678 EI-----EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL-------RKDLARLEAEVEQL 745
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1121 QGRHEQLQAQRANVEAQEVALLAERERLMQDGHRqrgLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARL 1200
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAE---AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1201 ELERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLH---RE 1277
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEelsEE 902
|
650 660
....*....|....*....|..
gi 1907133161 1278 QREYLDQLNALRREKQKLVEKI 1299
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKL 924
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
730-1208 |
6.29e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.93 E-value: 6.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 730 EEQALRDEVAQLRREVAglevKLQAQAQRLEARSAEALclsEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELE 809
Cdd:COG1196 310 RRRELEERLEELEEELA----ELEEELEELEEELEELE---EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 810 AASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELG 889
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 890 DRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALMELKARALQLEEELIQLrQYPVDLATG 969
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV-EAAYEAALE 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 970 ARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQE 1049
Cdd:COG1196 542 AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1050 LHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQA 1129
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907133161 1130 QRANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLE 1208
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1048-1307 |
2.12e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.46 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1048 QELHRKLGVLEEEVRAARRAQE-----ETRGQQQALLRDHEALVQLQRRQ------ETELEGLLVRHRDLKANMRALELA 1116
Cdd:COG1196 196 GELERQLEPLERQAEKAERYRElkeelKELEAELLLLKLRELEAELEELEaeleelEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1117 HRELQGRHEQLQAQRANVEAQ----EVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGE 1192
Cdd:COG1196 276 LEELELELEEAQAEEYELLAElarlEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1193 LRSRLA-----RLELERAQLEIQSQQLRESNQQLDLsacrLTTQCELLTQLRSA--QEEENRQLLAEVQALSRENRELLE 1265
Cdd:COG1196 356 AEAELAeaeeaLLEAEAELAEAEEELEELAEELLEA----LRAAAELAAQLEELeeAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1907133161 1266 RSLESRDHLHREQREYLDQLNALRREKQKLVEKIMDQYRVLE 1307
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
884-1207 |
3.84e-17 |
|
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: 87.80 E-value: 3.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 884 RGQELgDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALMELK---ARALQLEEELIQLR 960
Cdd:TIGR02168 675 RRREI-EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLArleAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 961 QYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEK 1040
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1041 SMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHREL 1120
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1121 QGRHEQLQAQRANVEAQEVALLAERERlmqdghrqrgLEEELRrlqnehERAQMLLAEVSRERGELQGERGELRSRLARL 1200
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDN----------LQERLS------EEYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
....*..
gi 1907133161 1201 ELERAQL 1207
Cdd:TIGR02168 978 ENKIKEL 984
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
12-183 |
3.28e-16 |
|
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: 77.27 E-value: 3.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 12 FLSGSLATWALGLAGLVGEAEESAGgteeeeeeeeeegalctekRFLRLIDGALLLRVLGIIAPSSRGGlRMVRGRDGPA 91
Cdd:cd22228 1 FLQSPLVTWVKTFGPLGFGSEDKLS-------------------MYMDLVDGVFLNKIMLQIDPRPTNQ-RVNKHVNNDV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 92 ACRMWNLCHLWGRLRDFYQE-LQLLILSPPPDLQTMGCDPFSEEAVDELESILRLLLGASVQCEHRELFIRHIRGLSLDV 170
Cdd:cd22228 61 NLRIQNLTILVRHIKTYYQEvLQQLIVMNLPNVLMIGKDPLSGKSMEEIKKMLLLVLGCAVQCERKEEFIERIKQLDIET 140
|
170
....*....|...
gi 1907133161 171 QSELAGAIQEVTQ 183
Cdd:cd22228 141 QAAIVSHIQEVTH 153
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
615-1316 |
1.55e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 82.80 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 615 EVRIEVQELLGETGSREAPQGELVHKAQVLKQESPKC--RPRSAELTLREPLKDQKALDRELELSKQQKEtgRHEQRPKG 692
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeqQKQILRERLANLERQLEELEAQLEELESKLD--ELAEELAE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 693 LESKLGPQKPQQTSEGVPDAWSREEPTPGETLVSAIPEE-QALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEALCLSE 771
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQlETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 772 ELAQARRteAEAHQEAEAQAREQARLREAVDTASLELEAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQ 851
Cdd:TIGR02168 422 EIEELLK--KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 852 ALES---QVRCHLEEAEREHAEKQAL------REELEKAVLrgQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRH 922
Cdd:TIGR02168 500 NLEGfseGVKALLKNQSGLSGILGVLselisvDEGYEAAIE--AALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLP 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 923 LEQRLEAELQAASTSKEEALMELKARALQLEEELIQLRQ---------YPVD-LATGARAGPRT---------------- 976
Cdd:TIGR02168 578 LDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllggvLVVDdLDNALELAKKLrpgyrivtldgdlvrp 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 977 --------VETQNGRLiEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQ 1048
Cdd:TIGR02168 658 ggvitggsAKTNSSIL-ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1049 ELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQ 1128
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1129 AQRANVEAQEVALLAERERLMQdghRQRGLEEELRRLQNEheraqmlLAEVSRERGELQGERGELRSRLARLELERAQLE 1208
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATER---RLEDLEEQIEELSED-------IESLAAEIEELEELIEELESELEALLNERASLE 886
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1209 IQSQQLRESNQQLDlsacrlttqcelltqlrsaqeeenrqllAEVQALSRENRELLERSLESRDHLHREQReyldQLNAL 1288
Cdd:TIGR02168 887 EALALLRSELEELS----------------------------EELRELESKRSELRRELEELREKLAQLEL----RLEGL 934
|
730 740
....*....|....*....|....*...
gi 1907133161 1289 RREKQKLVEKIMDQYRVLEPGPLPRTKK 1316
Cdd:TIGR02168 935 EVRIDNLQERLSEEYSLTLEEAEALENK 962
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
862-1217 |
3.31e-15 |
|
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: 81.65 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 862 EEAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQAalERQKFLQEQENQHQRYRHLeqrleAELQAASTSKEEA 941
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA--ERYQALLKEKREYEGYELL-----KEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 942 LMELKAralqLEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAEK-AALQGQLQHLEGQLGSLQGRAQ 1020
Cdd:TIGR02169 243 ERQLAS----LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1021 ELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLL 1100
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1101 VRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVALLAERERlmqdghrqrgLEEELRRLQNEHERAQMLLAEVS 1180
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED----------KALEIKKQEWKLEQLAADLSKYE 468
|
330 340 350
....*....|....*....|....*....|....*..
gi 1907133161 1181 RERGELQGERGELRSRLARLELERAQLEIQSQQLRES 1217
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
838-1143 |
2.75e-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: 78.56 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 838 RLRAQVEAAEQQVQALESQvrchLEEAEREHAEKQALREELEKAVlrgQELGDRLEHLQEEL-----EQAALERQK-FLQ 911
Cdd:TIGR02168 236 ELREELEELQEELKEAEEE----LEELTAELQELEEKLEELRLEV---SELEEEIEELQKELyalanEISRLEQQKqILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 912 EQENQHQR--------YRHLEQRLEaELQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGARAGPRTVETQNGR 983
Cdd:TIGR02168 309 ERLANLERqleeleaqLEELESKLD-ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 984 LIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELL--LQSQRAQEHSSRLQAEKsmmemqgQELHRKLGVLEEEV 1061
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLkkLEEAELKELQAELEELE-------EELEELQEELERLE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1062 RAARRAQEETRGQQQALLRDHEALVQLQRRQETeLEGLLVRHRDLKANMRALELAHRELQGRHEQLqAQRANVEAQ-EVA 1140
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDS-LERLQENLEGFSEGVKALLKNQSGLSGILGVL-SELISVDEGyEAA 538
|
...
gi 1907133161 1141 LLA 1143
Cdd:TIGR02168 539 IEA 541
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
838-1299 |
2.96e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.42 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 838 RLRAQVEAAEQQVQALEsQVRCHLEEAEREHAEKQALREELEK-----AVLRGQELGDRLEHLQEELEQAALERQKFLQE 912
Cdd:COG4913 239 RAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAAlrlwfAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 913 QENQHQRYRHLEQRL-------EAELQAASTSKEEALMELKARALQLEEELIQLRQYPV----DLATGARAGPRTVETQN 981
Cdd:COG4913 318 LDALREELDELEAQIrgnggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPasaeEFAALRAEAAALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 982 GRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEhssrlqaeksmmemqgqELHRKLGVLEEEV 1061
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD-----------------ALAEALGLDEAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1062 RAA------RRAQEETRGQQQALLRDhealvqlQRRqeteleGLLVRHRDLKANMRALElaHRELQGRHEQLQAQRANVE 1135
Cdd:COG4913 461 PFVgelievRPEEERWRGAIERVLGG-------FAL------TLLVPPEHYAAALRWVN--RLHLRGRLVYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1136 AQEVALLAER--ERLMQDGHRQRG-LEEELRRLQN-----------EHERAQMLLAEV--SRERGELQGERGELR----- 1194
Cdd:COG4913 526 PERPRLDPDSlaGKLDFKPHPFRAwLEAELGRRFDyvcvdspeelrRHPRAITRAGQVkgNGTRHEKDDRRRIRSryvlg 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1195 ----SRLARLELERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEEN--RQLLAEVQALSRENRELLE--- 1265
Cdd:COG4913 606 fdnrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDAssd 685
|
490 500 510
....*....|....*....|....*....|....*..
gi 1907133161 1266 --RSLESR-DHLHREQREYLDQLNALRREKQKLVEKI 1299
Cdd:COG4913 686 dlAALEEQlEELEAELEELEEELDELKGEIGRLEKEL 722
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1008-1326 |
4.94e-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: 77.79 E-value: 4.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1008 LEGQLGSLQGRAQelllQSQRAQEHSSRL-QAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALV 1086
Cdd:TIGR02168 198 LERQLKSLERQAE----KAERYKELKAELrELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1087 QLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLMQDGHRqrgLEEELRRLQ 1166
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE---LEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1167 NEHE-------RAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLR 1239
Cdd:TIGR02168 351 EELEsleaeleELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1240 SAQE--------EENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALrREKQKLVEKIMDQYRVLEPGPL 1311
Cdd:TIGR02168 431 EEAElkelqaelEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL-QARLDSLERLQENLEGFSEGVK 509
|
330
....*....|....*
gi 1907133161 1312 PRTKKGSWLADKGPR 1326
Cdd:TIGR02168 510 ALLKNQSGLSGILGV 524
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
730-1307 |
5.97e-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: 77.42 E-value: 5.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 730 EEQALRDEVAQLRREVAGLE---VKLQAQAQRLEARSAEALCLSEELAqarrteaeaHQEAEAQAREQARLREAVDTASL 806
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEeelEKLTEEISELEKRLEEIEQLLEELN---------KKIKDLGEEEQLRVKEKIGELEA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 807 ELEAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQ 886
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 887 ELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLeAELQAASTSKEEALMELKARALQLEEEliqlrqypvdl 966
Cdd:TIGR02169 382 ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL-ADLNAAIAGIEAKINELEEEKEDKALE----------- 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 967 atgaragprtVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQ 1046
Cdd:TIGR02169 450 ----------IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAS 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1047 GQELH---RKLGVLEE------EVRAARRAQ------EETRGQQQALLRDHEA----LVQLQRRQETELEG--------- 1098
Cdd:TIGR02169 520 IQGVHgtvAQLGSVGEryataiEVAAGNRLNnvvvedDAVAKEAIELLKRRKAgratFLPLNKMRDERRDLsilsedgvi 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1099 ------------------------LLVRH----RDLKANMRALEL----------------AHRELQGRHEQLQAQRANV 1134
Cdd:TIGR02169 600 gfavdlvefdpkyepafkyvfgdtLVVEDieaaRRLMGKYRMVTLegelfeksgamtggsrAPRGGILFSRSEPAELQRL 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1135 EAQEVALLAERERLMQDGHRQRG------------------LEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSR 1196
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENrldelsqelsdasrkigeIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1197 LARLELERAQLEIQSQQLREsnQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQAL-SRENRELLERSL--ESRDH 1273
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEE--ALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIeQKLNRLTLEKEYleKEIQE 837
|
650 660 670
....*....|....*....|....*....|....
gi 1907133161 1274 LHREQREYLDQLNALRREKQKLVEKIMDQYRVLE 1307
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
875-1258 |
1.09e-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: 76.63 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 875 REELEKAVLRGQELGDRLEHLQEELEqaalERQKFLQEQENQHQRYRHLEQRLEaELQAASTSKEeaLMELKARALQLEE 954
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELE----RQLKSLERQAEKAERYKELKAELR-ELELALLVLR--LEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 955 ELIQLRQypvdlatgaragprtvetqngrlievernnatlvaEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSS 1034
Cdd:TIGR02168 247 ELKEAEE-----------------------------------ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1035 RLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALE 1114
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1115 LAHRELQGRHEQLQAQRANVEAQEVALLAERERLMQDGHRqrgLEEELRRLQNEHE--RAQMLLAEVSRERGELQGERGE 1192
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER---LEDRRERLQQEIEelLKKLEEAELKELQAELEELEEE 448
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907133161 1193 LRSRLARLELERAQLEIQSQQLRESNQQLDL---SACRLTTQCELLTQLRSAQEEENRQLLAEVQALSR 1258
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAaerELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
60-183 |
2.50e-13 |
|
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: 68.84 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 60 LIDGALLLRVLGIIAPSS-RGGLRMVRGRDGPAACRMWNLCHLWGRLRDFYQEL--QLLILSPPPDLQTMgcdpFSEEAV 136
Cdd:cd22211 23 LSDGVVLAEILSQIDPSYfDSEWLESRDSSDNWVLKLNNLKKLYRSLSKYYREVlgQQLSDLPLPDLSAI----ARDGDE 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1907133161 137 DELESILRLLLGASVQCEHRELFIRHIRGLSLDVQSELAGAIQEVTQ 183
Cdd:cd22211 99 EEIVKLLELVLGAAVQCENKEEYIARIQQLDESTQAELMLIIQEVLE 145
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
260-498 |
5.27e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 5.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 260 LALQLTNAKAQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQ--AKRAELYREEAEALRERAGRLP--- 334
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEleEAQAEEYELLAELARLEQDIARlee 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 335 -------RLQEELRRCREKLQAAEVFKGQLEEERVLSEALEASKVLLEEQLEVARERSARLHETQREnlLLRTRLGEAHA 407
Cdd:COG1196 310 rrreleeRLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--AEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 408 DLDSLRHQLEQLVEENVELELELQRSLEpppgspgEASLPGAAPSLQDEVREAEAGRLRAVERENRELRGQLQMLQAQLG 487
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLER-------LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250
....*....|.
gi 1907133161 488 SQHPLLEEQRE 498
Cdd:COG1196 461 LLELLAELLEE 471
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
856-1208 |
9.42e-13 |
|
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: 73.56 E-value: 9.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 856 QVRCHLEEAEREhaeKQALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEaELQAAS 935
Cdd:TIGR02169 678 RLRERLEGLKRE---LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS-SLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 936 TSKEEALMELKARALQLEEELIQLRQYPVDLAtgARAGPRTVETQNGRLIEVErnnatlvAEKAALQGQLQHLEGQLGSL 1015
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIQAELSKLE-------EEVSRIEARLREIEQKLNRL 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1016 QGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDhealvqlQRRQETE 1095
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE-------RDELEAQ 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1096 LEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLMQDGHRQ---RGLEEELRRLQNEHERA 1172
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQaelQRVEEEIRALEPVNMLA 977
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907133161 1173 QMLLAEVSRERGELQGERgelrsrlARLELERAQLE 1208
Cdd:TIGR02169 978 IQEYEEVLKRLDELKEKR-------AKLEEERKAIL 1006
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
642-1268 |
2.98e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.61 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 642 QVLKQESPKCRPRSAELTLREPLKDQKALDRELELSKQQKETGRHEQRPKGLESKLgpqkpqQTSEGVPDAWSREEPTPG 721
Cdd:PRK02224 160 QLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESEL------AELDEEIERYEEQREQAR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 722 ETLVSA---IPEEQALRDEVAQLRREVAGLEVKLQAQAQRLEArsaealcLSEELAQARRTEAEAHQeaeaqarEQARLR 798
Cdd:PRK02224 234 ETRDEAdevLEEHEERREELETLEAEIEDLRETIAETEREREE-------LAEEVRDLRERLEELEE-------ERDDLL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 799 EAVDTASLELEAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREEL 878
Cdd:PRK02224 300 AEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAV 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 879 EKAVLRGQELGDRLEHLQEELEQAALERQK---FLQEQENQHQRYRHLEQRLEAELQAASTSKEEalmelkARALQLEEE 955
Cdd:PRK02224 380 EDRREEIEELEEEIEELRERFGDAPVDLGNaedFLEELREERDELREREAELEATLRTARERVEE------AEALLEAGK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 956 LIQLRQyPVDLATGAragpRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEgQLGSLQGRAQELLLQSQRAQEHSSR 1035
Cdd:PRK02224 454 CPECGQ-PVEGSPHV----ETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAE 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1036 LQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLlvrhRDLKANMRALEL 1115
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL----ERIRTLLAAIAD 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1116 AHRELQGRHEQLqAQRANVEAQevallaERERLMQDGHRQRGLEEE-----LRRLQNEHERAQMLLAEVSRERGELQGER 1190
Cdd:PRK02224 604 AEDEIERLREKR-EALAELNDE------RRERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREER 676
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907133161 1191 GELRSRLARLELERAQLEiqsqQLRESNQQLDLSACRLTTQCELLTQLrsaqEEENRQLLAEvqaLSRENRELLERSL 1268
Cdd:PRK02224 677 DDLQAEIGAVENELEELE----ELRERREALENRVEALEALYDEAEEL----ESMYGDLRAE---LRQRNVETLERML 743
|
|
| HkD_Hook |
cd22222 |
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ... |
60-181 |
9.73e-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: 64.19 E-value: 9.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 60 LIDGALLLRVLGIIAPSSRGGLRMVRGRDGPA---ACRMWNLCHLWGRLRDFYQELQLLILS--PPPDLQTMG--CDPfs 132
Cdd:cd22222 23 LSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGdnwRLKVSNLKKILKGIVDYYSEVLGQQISgfTMPDVNAIAekEDP-- 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1907133161 133 eeavDELESILRLLLGASVQCEHRELFIRHIRGLSLDVQSELAGAIQEV 181
Cdd:cd22222 101 ----KELGRLLQLVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQEL 145
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
769-1134 |
1.73e-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: 69.33 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 769 LSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELEAASrerealaealaaagRERRQWERDGPRLRAQVEAAEQ 848
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAS--------------RKIGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 849 QVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQAAL-ERQKFLQEQENQHQRYRHLEQRL 927
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 928 EAELQAASTSK---EEALMELKARALQLEEELIQLRQYPVDLATgaragprTVETQNGRLIEVERNNATLVAEKAALQGQ 1004
Cdd:TIGR02169 818 EQKLNRLTLEKeylEKEIQELQEQRIDLKEQIKSIEKEIENLNG-------KKEELEEELEELEAALRDLESRLGDLKKE 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1005 LQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVrAARRAQEETRGQQQALLRDHEA 1084
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP-EEELSLEDVQAELQRVEEEIRA 969
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1085 LVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANV 1134
Cdd:TIGR02169 970 LEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
827-1247 |
2.18e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.64 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 827 RERRQWERDGPRLRAQVEAAEQQVQALEsQVRCHLEEAEREHAEKQALREELEKAV------LRGQELGDRLEHLQ---E 897
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKLLqllplyQELEALEAELAELPerlE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 898 ELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALMELKARALQLEEELIQLRQypvdlatgaragprTV 977
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEE--------------EL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 978 ETQNGRLIEVERNNATLVAEKAALQgQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSR------LQAEKSMMEMQGQELH 1051
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAA-LEERLKEARLLLLIAAALLALLGLGGSLLSLIltiagvLFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1052 RKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQgrHEQLQAQR 1131
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1132 ANV--------EAQEVALLAERERLMQDGHRQRGLEEELR----------------RLQNEHERAQMLLAEVSRERGELQ 1187
Cdd:COG4717 373 AALlaeagvedEEELRAALEQAEEYQELKEELEELEEQLEellgeleellealdeeELEEELEELEEELEELEEELEELR 452
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907133161 1188 GERGELRSRLARLELER--AQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENR 1247
Cdd:COG4717 453 EELAELEAELEQLEEDGelAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
792-1302 |
3.46e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.17 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 792 REQARLREAVDTASLELEAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRcHLEEAEREHAEK 871
Cdd:PRK03918 217 PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-ELKELKEKAEEY 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 872 QALREELEKAVLRGQELGDRLEHLQEELEqaALERQkfLQEQENQHQRYRHLEQRLEAELQAASTSKEEAlmELKARALQ 951
Cdd:PRK03918 296 IKLSEFYEEYLDELREIEKRLSRLEEEIN--GIEER--IKELEEKEERLEELKKKLKELEKRLEELEERH--ELYEEAKA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 952 LEEELIQLRqypvdlatgARAGPRTVETQNGRLIEVERnnatlvaEKAALQGQLQHLEGQLGSLQGRAQELllqsqraQE 1031
Cdd:PRK03918 370 KKEELERLK---------KRLTGLTPEKLEKELEELEK-------AKEEIEEEISKITARIGELKKEIKEL-------KK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1032 HSSRLQAEKSMMEMQGQEL--HRKLGVLEEEVRAARRAQEEtrgqqqaLLRDHEALVQLqRRQETELEGLLVRHRDLKAN 1109
Cdd:PRK03918 427 AIEELKKAKGKCPVCGRELteEHRKELLEEYTAELKRIEKE-------LKEIEEKERKL-RKELRELEKVLKKESELIKL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1110 MRALELAhRELQGRHEQLQAQRANVEAQEVALLaeRERLMQDGHRQRGLEEELRRLQ---NEHERAQMLLAEVSRERGEL 1186
Cdd:PRK03918 499 KELAEQL-KELEEKLKKYNLEELEKKAEEYEKL--KEKLIKLKGEIKSLKKELEKLEelkKKLAELEKKLDELEEELAEL 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1187 QGERG--------ELRSRLARLE-LERAQLEIQS--QQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQA 1255
Cdd:PRK03918 576 LKELEelgfesveELEERLKELEpFYNEYLELKDaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1907133161 1256 LSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKIMDQ 1302
Cdd:PRK03918 656 YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
730-1299 |
4.17e-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: 68.17 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 730 EEQALRDEVAQLRREVAGLEVKLQAQAQRLEArsaealcLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELE 809
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDK-------LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 810 AASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELG 889
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 890 DRLEHLQEELEQAALERqkflqeqenqhqryrhleQRLEAELQAASTSKEE---ALMELKAR---ALQLEEELIQLR--- 960
Cdd:TIGR02169 476 EEYDRVEKELSKLQREL------------------AEAEAQARASEERVRGgraVEEVLKASiqgVHGTVAQLGSVGery 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 961 QYPVDLATGARAGPRTVET--------------QNGR------------------------------LIEVERNNA---- 992
Cdd:TIGR02169 538 ATAIEVAAGNRLNNVVVEDdavakeaiellkrrKAGRatflplnkmrderrdlsilsedgvigfavdLVEFDPKYEpafk 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 993 -----TLVAEKAAL------QGQLQHLEGQL---------GSLQGRAQELLLQSQRAQEhsSRLQAEKSMMEMQGQELHR 1052
Cdd:TIGR02169 618 yvfgdTLVVEDIEAarrlmgKYRMVTLEGELfeksgamtgGSRAPRGGILFSRSEPAEL--QRLRERLEGLKRELSSLQS 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1053 KLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRA 1132
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1133 NVEAQEVALLAererlMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQsq 1212
Cdd:TIGR02169 776 KLEEALNDLEA-----RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ-- 848
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1213 qlRESNQQldlsacrltTQCELLTQLRSAQEEEnrqllaevqalsrENRELLERSLESR-DHLHREQREYLDQLNALRRE 1291
Cdd:TIGR02169 849 --IKSIEK---------EIENLNGKKEELEEEL-------------EELEAALRDLESRlGDLKKERDELEAQLRELERK 904
|
....*...
gi 1907133161 1292 KQKLVEKI 1299
Cdd:TIGR02169 905 IEELEAQI 912
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
845-1299 |
5.21e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.78 E-value: 5.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 845 AAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLE 924
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 925 QRLEaelqaastSKEEALMELKARALQLEEeliqlrqypvdlatgaragprtvetqngrLIEVERNNATLVAEKAALQGQ 1004
Cdd:PRK03918 266 ERIE--------ELKKEIEELEEKVKELKE-----------------------------LKEKAEEYIKLSEFYEEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1005 LQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEmqgqELHRKLGVLEEEVRAARRAQeetrgqqqallrdheA 1084
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK----ELEKRLEELEERHELYEEAK---------------A 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1085 LVQLQRRQETELEGLLVrhRDLKANMRALELAHRELQGRHEQLQAQRANVEAQEvallAERERLMQDGHRQRGLEEELRR 1164
Cdd:PRK03918 370 KKEELERLKKRLTGLTP--EKLEKELEELEKAKEEIEEEISKITARIGELKKEI----KELKKAIEELKKAKGKCPVCGR 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1165 LQNEHERAQmLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLResnqqldlsacRLTTQCELLTQLRSAQEE 1244
Cdd:PRK03918 444 ELTEEHRKE-LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES-----------ELIKLKELAEQLKELEEK 511
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1907133161 1245 ENRQLLAEVQALSRENRELLERSLESRDHLHREQREyLDQLNALRREKQKLVEKI 1299
Cdd:PRK03918 512 LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE-LEKLEELKKKLAELEKKL 565
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1018-1294 |
7.88e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 7.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1018 RAQELLLQSQRAQEHSSRLQAEKSmmemqgqELHRKLGVLEEEVRAARRAQEetrgqQQALLRDHEALVQLQR--RQETE 1095
Cdd:TIGR02168 173 RRKETERKLERTRENLDRLEDILN-------ELERQLKSLERQAEKAERYKE-----LKAELRELELALLVLRleELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1096 LEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVALlaeRERLMQDGHRQRGLEEELRRLQNEHERAQML 1175
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL---QKELYALANEISRLEQQKQILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1176 LAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLR----ESNQQLDLSACRLTTQCELLTQLRSAQEEENRQlLA 1251
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEaeleELEAELEELESRLEELEEQLETLRSKVAQLELQ-IA 396
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907133161 1252 EVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQK 1294
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
733-1304 |
9.30e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 9.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 733 ALRDEVAQLRREVAGLEvKLQAQAQRLEARSAEALCLSEELAQARrteaeahqeAEAQAREQARLREAVDTASLELEAAs 812
Cdd:COG4913 239 RAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALR---------LWFAQRRLELLEAELEELRAELARL- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 813 rerealaealaaaGRERRQWERDGPRLRAQVEAAEQQ--------VQALESQvrchLEEAEREHAEKQALREELEKAVLR 884
Cdd:COG4913 308 -------------EAELERLEARLDALREELDELEAQirgnggdrLEQLERE----IERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 885 -GQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEaELQAASTSKEEALMELKARALQLEEELIQLRQYP 963
Cdd:COG4913 371 lGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR-DLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 964 VDLATGARAGPRTVetqnGRLIEVERNNA---------------TLVAEKAALQGQLQ-----HLEGQLGSLQGRAQELL 1023
Cdd:COG4913 450 AEALGLDEAELPFV----GELIEVRPEEErwrgaiervlggfalTLLVPPEHYAAALRwvnrlHLRGRLVYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1024 LQSQRAQEHS--SRLQAEKSmmEMQG---QELHRKLGVL----EEEVRAARRA--------QEETRGQ---QQALLRDH- 1082
Cdd:COG4913 526 PERPRLDPDSlaGKLDFKPH--PFRAwleAELGRRFDYVcvdsPEELRRHPRAitragqvkGNGTRHEkddRRRIRSRYv 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1083 ---EALVQLQRRQEtELEGLLVRHRDLKANMRALELAHRELQGRHEQLQaQRANVEAQEVALLAERERLMQdghrqrgLE 1159
Cdd:COG4913 604 lgfDNRAKLAALEA-ELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEIDVASAEREIAE-------LE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1160 EELRRL---QNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLResnqqldlsacrlttqcELLT 1236
Cdd:COG4913 675 AELERLdasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ-----------------DRLE 737
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1237 QLRSAQEEENRQLLAEV--QALSRENRELLERSLESRdhlhreqreyLDQLNALRREKQKLVEKIMDQYR 1304
Cdd:COG4913 738 AAEDLARLELRALLEERfaAALGDAVERELRENLEER----------IDALRARLNRAEEELERAMRAFN 797
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
850-1299 |
1.05e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.60 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 850 VQALESQVRCHLEEAEREHAEKQA--LREELEKAVLRGQELGDRLEHLQEELEQAALERQK---FLQEQENQHQRYRHLE 924
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEkdLHERLNGLESELAELDEEIERYEEQREQARETRDEadeVLEEHEERREELETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 925 QRLEaELQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQ 1004
Cdd:PRK02224 258 AEIE-DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1005 LQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRA---QEETRGQQQALLRD 1081
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdAPVDLGNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1082 HEALVQLQRRQETELEGLLVRHRDLKANMRALELAHR------------------ELQGRHEQLQAQRANVEAQEVALLA 1143
Cdd:PRK02224 417 LREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvetieEDRERVEELEAELEDLEEEVEEVEE 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1144 ERERLMQdghrQRGLEEELRRLQNEHERAQMLLAEvSRERGElqgergELRSRLARLELERAQLEIQSQQLRESNQQLDL 1223
Cdd:PRK02224 497 RLERAED----LVEAEDRIERLEERREDLEELIAE-RRETIE------EKRERAEELRERAAELEAEAEEKREAAAEAEE 565
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907133161 1224 SACRLTTQCELLTQLRSAQEEENRQL--LAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKI 1299
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESLerIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEF 643
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
996-1222 |
2.59e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.01 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 996 AEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQ 1075
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1076 QALLRdhealvQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAqevallaererlmqdghrq 1155
Cdd:COG4942 107 AELLR------ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE------------------- 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907133161 1156 rgLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLD 1222
Cdd:COG4942 162 --LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
886-1299 |
3.36e-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: 65.09 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 886 QELGDRLEHLQEELEQAALERqkflqeqenqhqryRHLEQRLEAELQAASTSKEEaLMELKARALQLEEELiqlrqypvd 965
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSEL--------------RRIENRLDELSQELSDASRK-IGEIEKEIEQLEQEE--------- 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 966 latgaragprtvETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELllqsqraQEHSSRLQAEKSMMEM 1045
Cdd:TIGR02169 733 ------------EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL-------EEALNDLEARLSHSRI 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1046 QgqELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALvqlqrrqETELEGLLVRHRDLKANMRALELAHRELQGRHE 1125
Cdd:TIGR02169 794 P--EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL-------EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1126 QLQAQRANVEAQEvallaererlmqdghrqRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLElerA 1205
Cdd:TIGR02169 865 ELEEELEELEAAL-----------------RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK---A 924
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1206 QLEIQSQQLREsnqqLDLSACRLTTQCELLTQLRSAQEEENRqLLAEVQALSRENRelleRSLESRDHLHREQREYLDQL 1285
Cdd:TIGR02169 925 KLEALEEELSE----IEDPKGEDEEIPEEELSLEDVQAELQR-VEEEIRALEPVNM----LAIQEYEEVLKRLDELKEKR 995
|
410
....*....|....
gi 1907133161 1286 NALRREKQKLVEKI 1299
Cdd:TIGR02169 996 AKLEEERKAILERI 1009
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
727-1166 |
1.11e-09 |
|
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: 63.43 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 727 AIPEEQALRDEVAQLRRE----VAGLEVKLQAQAQRLearSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLREAVD 802
Cdd:COG3096 247 AIRVTQSDRDLFKHLITEatnyVAADYMRHANERREL---SERALELRRELFGARRQLAEEQYRLVEMARELEELSARES 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 803 TASLELEAASRERealaealaaagrerrqwerdgprlrAQVEAAEQQVQALEsQVRCHLEEAEREHAEKQALREELEKAV 882
Cdd:COG3096 324 DLEQDYQAASDHL-------------------------NLVQTALRQQEKIE-RYQEDLEELTERLEEQEEVVEEAAEQL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 883 LRGQElgdRLEHLQEELEQAA---LERQKFLQEQENQHQRYRHLEQRLE--------AELQAASTSKEEAlmELKARALQ 951
Cdd:COG3096 378 AEAEA---RLEAAEEEVDSLKsqlADYQQALDVQQTRAIQYQQAVQALEkaralcglPDLTPENAEDYLA--AFRAKEQQ 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 952 LEEELIQLRQyPVDLATGARA----GPRTVETQNGrliEVERNNATLVA--------EKAALQGQLQHLEGQLGSLQGRA 1019
Cdd:COG3096 453 ATEEVLELEQ-KLSVADAARRqfekAYELVCKIAG---EVERSQAWQTArellrryrSQQALAQRLQQLRAQLAELEQRL 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1020 QelllQSQRAQEhssrlqaeksmmemQGQELHRKLGvleeEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGL 1099
Cdd:COG3096 529 R----QQQNAER--------------LLEEFCQRIG----QQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1100 LVRHRDLKANMRALELAHRELQGRHEQLQAQ--------------RANVEAQEVALLAERERLMQdghRQRGLEEELRRL 1165
Cdd:COG3096 587 LEQLRARIKELAARAPAWLAAQDALERLREQsgealadsqevtaaMQQLLEREREATVERDELAA---RKQALESQIERL 663
|
.
gi 1907133161 1166 Q 1166
Cdd:COG3096 664 S 664
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
724-1265 |
1.27e-09 |
|
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: 63.21 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 724 LVSAIPEEQALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQarEQARLREaVDT 803
Cdd:pfam15921 115 LQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLS--HEGVLQE-IRS 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 804 ASLELEAASREREALAEALAAA---------GRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEK--- 871
Cdd:pfam15921 192 ILVDFEEASGKKIYEHDSMSTMhfrslgsaiSKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRieq 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 872 ---------QALREELEKAVLRGQELGDRLEHLQE--------------ELEQAALERQKFLQEQENQHQ-RYRHLEQRL 927
Cdd:pfam15921 272 liseheveiTGLTEKASSARSQANSIQSQLEIIQEqarnqnsmymrqlsDLESTVSQLRSELREAKRMYEdKIEELEKQL 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 928 ---EAELQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGARAGPRTVETQNG--------------RLIEVERN 990
Cdd:pfam15921 352 vlaNSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGnsitidhlrrelddRNMEVQRL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 991 NATLVAEKAALQGQlqhLEGQLGSLQGRAQELllqsQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEE 1070
Cdd:pfam15921 432 EALLKAMKSECQGQ---MERQMAAIQGKNESL----EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTAS 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1071 TRGQQQALLRDHEALVQLQRRQETELEgllvrhrdlkanmralELAHRELQGRHeqLQAQRANVEAQEVAlLAERERLMQ 1150
Cdd:pfam15921 505 LQEKERAIEATNAEITKLRSRVDLKLQ----------------ELQHLKNEGDH--LRNVQTECEALKLQ-MAEKDKVIE 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1151 DGHRQRgleEELRRLQNEHERAQmllAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSACRLTT 1230
Cdd:pfam15921 566 ILRQQI---ENMTQLVGQHGRTA---GAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVN 639
|
570 580 590
....*....|....*....|....*....|....*.
gi 1907133161 1231 Q-CELLTQLRSAQEEENrQLLAEVQALSRENRELLE 1265
Cdd:pfam15921 640 AgSERLRAVKDIKQERD-QLLNEVKTSRNELNSLSE 674
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
730-1307 |
1.43e-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: 63.16 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 730 EEQALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEalcLSEELAQARRTEAEAHQEAEAQAR----EQARLREAVDTAS 805
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL---LEELNKKIKDLGEEEQLRVKEKIGeleaEIASLERSIAEKE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 806 LELEAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRG 885
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 886 QELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEA------ELQAASTSKEEALMELKARALQLEEELIQL 959
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEleeekeDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 960 RQ-------------------------------YPVDLATGARAGPRTVETQNGRLIEVE-------------RNNATLV 995
Cdd:TIGR02169 475 KEeydrvekelsklqrelaeaeaqaraseervrGGRAVEEVLKASIQGVHGTVAQLGSVGeryataievaagnRLNNVVV 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 996 AEKAALQGQLQHLEGQLGslqGRAQELLLQSQRAQEHSSRLQAEKS---------------------------------- 1041
Cdd:TIGR02169 555 EDDAVAKEAIELLKRRKA---GRATFLPLNKMRDERRDLSILSEDGvigfavdlvefdpkyepafkyvfgdtlvvediea 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1042 ---------MMEMQGqELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRA 1112
Cdd:TIGR02169 632 arrlmgkyrMVTLEG-ELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1113 LELAHR---ELQGRHEQLQAQranvEAQEVALLAERERLMQDGHRQR-GLEEELRRLQNEHERAQMLLAEVSRERGELqg 1188
Cdd:TIGR02169 711 LSDASRkigEIEKEIEQLEQE----EEKLKERLEELEEDLSSLEQEIeNVKSELKELEARIEELEEDLHKLEEALNDL-- 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1189 ERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRsaQEEENRQLLAEVQALSRENR-ELLERS 1267
Cdd:TIGR02169 785 EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI--QELQEQRIDLKEQIKSIEKEiENLNGK 862
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1907133161 1268 LESrdhLHREQREYLDQLNALRREKQKLVEKIMD---QYRVLE 1307
Cdd:TIGR02169 863 KEE---LEEELEELEAALRDLESRLGDLKKERDEleaQLRELE 902
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
751-1190 |
2.20e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 751 KLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASL--ELEAASREREALAE---ALAAA 825
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPErleELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 826 GRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKqalREELEKAVlrgQELGDRLEHLQEELEQAALE 905
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE---LEELQQRL---AELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 906 RQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGARAGPRTVETQNGRLI 985
Cdd:COG4717 229 LEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 986 EVERNNATlvaEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRK-----LGVLEEE 1060
Cdd:COG4717 309 ALPALEEL---EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAallaeAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1061 VRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHrDLKANMRALELAHRELQGRHEQLQAQRANVEaQEVA 1140
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE-ELEEELEELEEELEELEEELEELREELAELE-AELE 463
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1141 LLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGER 1190
Cdd:COG4717 464 QLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
732-1286 |
2.72e-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: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 732 QALRDEVAQLRREVAGLEVklQAQAQRLEARSAEALCLSEELAQARRteaeahQEAEAQAREQArLREAVDTASLELEAA 811
Cdd:COG4913 265 AAARERLAELEYLRAALRL--WFAQRRLELLEAELEELRAELARLEA------ELERLEARLDA-LREELDELEAQIRGN 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 812 SREREAL-AEALAAAGRERRQWERDGPRLRAQVEAAEQQV----QALESQVRCHLEEAEREHAEKQALREELEKAVLRGQ 886
Cdd:COG4913 336 GGDRLEQlEREIERLERELEERERRRARLEALLAALGLPLpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALR 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 887 ELGDRLEHLQEELeqAALERQKFlqeqeNQHQRYRHLEQRLEAELQAastSKEEA-----LMELK--------------- 946
Cdd:COG4913 416 DLRRELRELEAEI--ASLERRKS-----NIPARLLALRDALAEALGL---DEAELpfvgeLIEVRpeeerwrgaiervlg 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 947 --ARALQLEEELIQ--------------LRQYPVDLATGARAGPRTVETQNGRLIEVERNNAT-----LVAEKAAL---- 1001
Cdd:COG4913 486 gfALTLLVPPEHYAaalrwvnrlhlrgrLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRawleaELGRRFDYvcvd 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1002 -QGQLQH------LEGQLgSLQGRAQELLLQSQRAQEH----SSRLQAEksmmemqgqELHRKLGVLEEEVRAARRAQEE 1070
Cdd:COG4913 566 sPEELRRhpraitRAGQV-KGNGTRHEKDDRRRIRSRYvlgfDNRAKLA---------ALEAELAELEEELAEAEERLEA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1071 TRGQQQALLRDHEALVQLQRRQETEL--EGLLVRHRDLKANMRALELAHRELqgrhEQLQAQRANVEAQEVALLAERERL 1148
Cdd:COG4913 636 LEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDDL----AALEEQLEELEAELEELEEELDEL 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1149 MQdghRQRGLEEELRRLQNEHERAQMLLAEVsrERGELQGERGELRSRLARLELERAQLEIQsQQLRESNQQLDLSACRL 1228
Cdd:COG4913 712 KG---EIGRLEKELEQAEEELDELQDRLEAA--EDLARLELRALLEERFAAALGDAVERELR-ENLEERIDALRARLNRA 785
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907133161 1229 TTQCE-LLTQLRSAQEEENRQLLAEVQALsRENRELLERsLEsRDHLHREQREYLDQLN 1286
Cdd:COG4913 786 EEELErAMRAFNREWPAETADLDADLESL-PEYLALLDR-LE-EDGLPEYEERFKELLN 841
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
838-1279 |
9.38e-09 |
|
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: 60.57 E-value: 9.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 838 RLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELekavlrgQELGDRLEHLQEELEQAALERQKFLQEQENQH 917
Cdd:pfam01576 226 ELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKI-------RELEAQISELQEDLESERAARNKAEKQRRDLG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 918 QRYRHLEQRLEAEL------QAASTSKEEALMELKAralQLEEELiqlRQYPVDLATGARAGPRTVETQNGRLIEVERNN 991
Cdd:pfam01576 299 EELEALKTELEDTLdttaaqQELRSKREQEVTELKK---ALEEET---RSHEAQLQEMRQKHTQALEELTEQLEQAKRNK 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 992 ATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEET 1071
Cdd:pfam01576 373 ANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1072 RGQQQALLRDHEAL-VQLQRRQETeLEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQ----EVALLAERE 1146
Cdd:pfam01576 453 EGKNIKLSKDVSSLeSQLQDTQEL-LQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQlstlQAQLSDMKK 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1147 RLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSAC 1226
Cdd:pfam01576 532 KLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLA 611
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1907133161 1227 RLTTQCELLTQLRSAQEEENRQLLAEVQALSREnrelLERSLESRDHLHREQR 1279
Cdd:pfam01576 612 EEKAISARYAEERDRAEAEAREKETRALSLARA----LEEALEAKEELERTNK 660
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1027-1218 |
1.18e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1027 QRAQEHSSRL-QAEKSMMEMQGQElhRKLGVLEEEVRAARRAQEETRGQQQALLR-DHEALVQLQRRQETELEGLLVRHR 1104
Cdd:COG4913 228 DALVEHFDDLeRAHEALEDAREQI--ELLEPIRELAERYAAARERLAELEYLRAAlRLWFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1105 DLKANMRALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLMQDGHRQR-----GLEEELRRL-----------QNE 1168
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERerrraRLEALLAALglplpasaeefAAL 385
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907133161 1169 HERAQMLLAEVSRERGELQGERGELRSRLARLELERAQL--EIQSQQLRESN 1218
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELeaEIASLERRKSN 437
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
629-1316 |
1.89e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 629 SREAPQGELVHKAQVLKQESpkcRPRSAELTLREPLKDQKALDRELELSKQQKETGRHEQRPKGLESKLGPQKPQqtseg 708
Cdd:PTZ00121 1124 AEDARKAEEARKAEDARKAE---EARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRK----- 1195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 709 VPDAWSREEPTPGETLVSAipeEQALRDEVAQLRREVAGLEvklQAQAQRLEARSAEALCLSEEL-----AQARRTEAEA 783
Cdd:PTZ00121 1196 AEDARKAEAARKAEEERKA---EEARKAEDAKKAEAVKKAE---EAKKDAEEAKKAEEERNNEEIrkfeeARMAHFARRQ 1269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 784 HQEAEAQAREQARLREAVdtaslELEAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEE 863
Cdd:PTZ00121 1270 AAIKAEEARKADELKKAE-----EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 864 AEREHAEKQALREELEKAvlrgQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQ--RLEAELQAASTSKEEA 941
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAA----EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEdkKKADELKKAAAAKKKA 1420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 942 lMELKARALQLE--EELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRA 1019
Cdd:PTZ00121 1421 -DEAKKKAEEKKkaDEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1020 QEL--LLQSQRAQEHSSRLQAEKSMMEMQGQELHRKlgvlEEEVRAA--RRAQEETRGQQQALLRDHEALVQLQRRQETE 1095
Cdd:PTZ00121 1500 DEAkkAAEAKKKADEAKKAEEAKKADEAKKAEEAKK----ADEAKKAeeKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1096 LEGLLVRHRDLKANMRA-----LELAHRELQGRHEQL-QAQRANVEAQEVAllAERERLMQDGHRQRGLEEELRR---LQ 1166
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEArieevMKLYEEEKKMKAEEAkKAEEAKIKAEELK--KAEEEKKKVEQLKKKEAEEKKKaeeLK 1653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1167 NEHERAQMLLAEVSRERGELQGERGELRsrlaRLELERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAqEEEN 1246
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAEEDKKKAEEAK----KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA-EEEN 1728
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907133161 1247 RQLLAEVQALSRENR---ELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKIMDQYRVLEPGPLPRTKK 1316
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKkkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1057-1271 |
2.09e-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: 58.24 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1057 LEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEA 1136
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1137 QevalLAERERLMQDGHRQRGLEEELRRLQ-NEHERAQMLLAEVSRER----GELQGERGELRSRLARLELERAQLEIQS 1211
Cdd:COG4942 105 E----LAELLRALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARreqaEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1212 QQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESR 1271
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
194-488 |
2.85e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 194 GPESGELVAEELEMQLRSLTGMMSRLARERDLGAQRLAELLLEREPAHLLLpeapanASAEGVSHHLALQLTNAKAQLRR 273
Cdd:TIGR02168 664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEL------EQLRKELEELSRQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 274 LRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALRERA--------GRLPRLQEELRRCRE 345
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLkeelkalrEALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 346 KLQAAEVFKGQLEEERvlsEALEASKVLLEEQLEVARERSARLHETQREnllLRTRLGEAHADLDSLRHQLEQLVEenve 425
Cdd:TIGR02168 818 EAANLRERLESLERRI---AATERRLEDLEEQIEELSEDIESLAAEIEE---LEELIEELESELEALLNERASLEE---- 887
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907133161 426 lelelqrslepppgspgeaslpgAAPSLQDEVREAEAgRLRAVERENRELRGQLQMLQAQLGS 488
Cdd:TIGR02168 888 -----------------------ALALLRSELEELSE-ELRELESKRSELRRELEELREKLAQ 926
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
827-1209 |
3.25e-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: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 827 RERRQWERDG------PRLRAQVEAAEQQVQALESQVRCHLEEA----EREHAEKQALREELEKAVLRGQELGDRLEHLQ 896
Cdd:pfam15921 399 QNKRLWDRDTgnsitiDHLRRELDDRNMEVQRLEALLKAMKSECqgqmERQMAAIQGKNESLEKVSSLTAQLESTKEMLR 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 897 EELEQAALERQKFLQEQENQHQRYRHLEQRLEA-ELQAASTSKEEALMELKARALQ-LEEELIQLRQYPVDLAtgaraGP 974
Cdd:pfam15921 479 KVVEELTAKKMTLESSERTVSDLTASLQEKERAiEATNAEITKLRSRVDLKLQELQhLKNEGDHLRNVQTECE-----AL 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 975 RTVETQNGRLIEVER----NNATLVAEKAALQGQLQ----HLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQ 1046
Cdd:pfam15921 554 KLQMAEKDKVIEILRqqieNMTQLVGQHGRTAGAMQvekaQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELE 633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1047 GQELhrkLGVLEEEVRAARRAQEE----------TRGQQQALLRDHEALVQLQRRQETELEGLLVRHR-DLKANMRALEL 1115
Cdd:pfam15921 634 KVKL---VNAGSERLRAVKDIKQErdqllnevktSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKmQLKSAQSELEQ 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1116 AHRELQ--------------GRHEQLQAQRANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEheraqmlLAEVSR 1181
Cdd:pfam15921 711 TRNTLKsmegsdghamkvamGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQE-------LSTVAT 783
|
410 420
....*....|....*....|....*...
gi 1907133161 1182 ERGELQGERGELRSRLARLELERAQLEI 1209
Cdd:pfam15921 784 EKNKMAGELEVLRSQERRLKEKVANMEV 811
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
275-989 |
4.34e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 275 RQEVEEKAEQLLDSQAEVQGLEaEIRR---LRQETQALSAQ-AKRAELYREEAEAlreRAGRLPRLQEELRRCREKLQAA 350
Cdd:PTZ00121 1110 KAEEARKAEEAKKKAEDARKAE-EARKaedARKAEEARKAEdAKRVEIARKAEDA---RKAEEARKAEDAKKAEAARKAE 1185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 351 EVFKGqlEEERVLSEALEASKVLLEEqlEVARERSARLHETQRENLLLRtRLGEAHADLDSLRHQLEQLVEENVELELEL 430
Cdd:PTZ00121 1186 EVRKA--EELRKAEDARKAEAARKAE--EERKAEEARKAEDAKKAEAVK-KAEEAKKDAEEAKKAEEERNNEEIRKFEEA 1260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 431 QRSLEPPPGSPGEASLPGAApslqDEVREAEAGRLRAVERENRELRgqlQMLQAQLGSQHPLLEEQRENSRQPPVPNRDP 510
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKA----DELKKAEEKKKADEAKKAEEKK---KADEAKKKAEEAKKADEAKKKAEEAKKKADA 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 511 ATPSALHHSPQSPACQigGEGSESLDLPSPASYSDITRSPKCSQAPDSHPELESPLQMVSQDPQTSDQALQESDPTVETH 590
Cdd:PTZ00121 1334 AKKKAEEAKKAAEAAK--AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELK 1411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 591 QCLEKSGHRVPLQSpivwdppQGPEVRiEVQELlgETGSREAPQGELVHKAQVLKQESPKCRPRSAELTLREPLKDQKAL 670
Cdd:PTZ00121 1412 KAAAAKKKADEAKK-------KAEEKK-KADEA--KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 671 DRELELSKQQKETGRH--EQRPKGLESKLGPQKPQQTSEG--VPDAWSREEPTPGETLVSAipEEQALRDEVAQLRREVA 746
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKkaDEAKKAAEAKKKADEAKKAEEAkkADEAKKAEEAKKADEAKKA--EEKKKADELKKAEELKK 1559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 747 GLEVKLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAR----EQARLREAVDTASLELEAASRerealaeal 822
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKkmkaEEAKKAEEAKIKAEELKKAEE--------- 1630
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 823 aaagrERRQWERDGPRLRAQVEAAEQqVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQA 902
Cdd:PTZ00121 1631 -----EKKKVEQLKKKEAEEKKKAEE-LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 903 ALERQKFLQEQENQHQRYRHLEQRleaELQAASTSKEEALMELKARALQLEEE----LIQLRQYPVDLATGARAGPRTV- 977
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEEN---KIKAEEAKKEAEEDKKKAEEAKKDEEekkkIAHLKKEEEKKAEEIRKEKEAVi 1781
|
730
....*....|....*..
gi 1907133161 978 -----ETQNGRLIEVER 989
Cdd:PTZ00121 1782 eeeldEEDEKRRMEVDK 1798
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
654-1299 |
5.46e-08 |
|
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: 58.06 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 654 RSAELTLREPLKDQKALDRELELSKQQKETGRHEQRPKGLESKLgpQKPQQTSEGVPDAWSREEPTPGETLVSAIPEEQA 733
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKA--ELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKH 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 734 LRDEVAQLRREVAGLEVKLQAQAQRLEarsaealcLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELEAASR 813
Cdd:TIGR00618 231 LREALQQTQQSHAYLTQKREAQEEQLK--------KQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAV 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 814 EREALAEALAAAGRERRQWERDGPRLR----AQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELG 889
Cdd:TIGR00618 303 TQIEQQAQRIHTELQSKMRSRAKLLMKraahVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIH 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 890 DRLEHLQEELEQAALERQKFLQEQENQHQR-YRHLEQR-LEAELQAASTSKEEALMELKARALQLEEELIQLRQ---YPV 964
Cdd:TIGR00618 383 TLQQQKTTLTQKLQSLCKELDILQREQATIdTRTSAFRdLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLekiHLQ 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 965 DLATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQS------QRAQEHSSRLQA 1038
Cdd:TIGR00618 463 ESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGpltrrmQRGEQTYAQLET 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1039 EKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLvRHRDLKANMRALELAHR 1118
Cdd:TIGR00618 543 SEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS-EAEDMLACEQHALLRKL 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1119 ELQGRHEQLQAQRANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLA 1198
Cdd:TIGR00618 622 QPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1199 RLELERAQLEIQSQQLRESNQQLDLSACR---LTTQCELLTQ-LRSAQEEENRQLLAEVQALSRENRELL--ERSLESRD 1272
Cdd:TIGR00618 702 CQTLLRELETHIEEYDREFNEIENASSSLgsdLAAREDALNQsLKELMHQARTVLKARTEAHFNNNEEVTaaLQTGAELS 781
|
650 660
....*....|....*....|....*..
gi 1907133161 1273 HLHREQREYLDQLNALRREKQKLVEKI 1299
Cdd:TIGR00618 782 HLAAEIQFFNRLREEDTHLLKTLEAEI 808
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
866-1299 |
7.39e-08 |
|
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: 57.49 E-value: 7.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 866 REHAEKQALREELEKAvlrgQELGDRLEHLQEELEQaaleRQKFLQEQENQHQRYRHLEQRLEAElqaastsKEEALMEL 945
Cdd:pfam01576 2 RQEEEMQAKEEELQKV----KERQQKAESELKELEK----KHQQLCEEKNALQEQLQAETELCAE-------AEEMRARL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 946 KARALQLEEELIQLRqypvdlatgaragprtvetqnGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQ 1025
Cdd:pfam01576 67 AARKQELEEILHELE---------------------SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1026 SQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEE---EVRAARRAQEETRGQQQALLRDHEALV-QLQRRQETELEGllv 1101
Cdd:pfam01576 126 KVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEErisEFTSNLAEEEEKAKSLSKLKNKHEAMIsDLEERLKKEEKG--- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1102 rHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQ----EVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQmllA 1177
Cdd:pfam01576 203 -RQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQlakkEEELQAALARLEEETAQKNNALKKIRELEAQISELQ---E 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1178 EVSRERGelQGERGELRSRLARLELERAQLEIQSqQLRESNQQLDLSACRLTTqcelLTQLRSAQEEENRQLLAEVQALS 1257
Cdd:pfam01576 279 DLESERA--ARNKAEKQRRDLGEELEALKTELED-TLDTTAAQQELRSKREQE----VTELKKALEEETRSHEAQLQEMR 351
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1907133161 1258 RENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKI 1299
Cdd:pfam01576 352 QKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAEL 393
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
843-1272 |
7.73e-08 |
|
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: 57.42 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 843 VEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQ---R 919
Cdd:pfam05483 263 LEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEelnK 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 920 YRHLEQRLEAELQAASTSKEEALMELKARalqLEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNaTLVAEKA 999
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRTEQQR---LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK-KILAEDE 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1000 ALQGQLQHLEGQLGSLQGRAQEL--LLQSQRAQEHSsrLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQA 1077
Cdd:pfam05483 419 KLLDEKKQFEKIAEELKGKEQELifLLQAREKEIHD--LEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDK 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1078 LLRDHEALVQ--------LQRRQETELEGLLVRHRDLKA--NMRALELAHR-ELQGRHEQLQAQRANV-----EAQEVAL 1141
Cdd:pfam05483 497 LLLENKELTQeasdmtleLKKHQEDIINCKKQEERMLKQieNLEEKEMNLRdELESVREEFIQKGDEVkckldKSEENAR 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1142 LAERERLMQDgHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQ----GERGELRS---RLARLELERA--------- 1205
Cdd:pfam05483 577 SIEYEVLKKE-KQMKILENKCNNLKKQIENKNKNIEELHQENKALKkkgsAENKQLNAyeiKVNKLELELAsakqkfeei 655
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907133161 1206 ----QLEIQSQQLRESNQQLDLSACRLTTqcELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRD 1272
Cdd:pfam05483 656 idnyQKEIEDKKISEEKLLEEVEKAKAIA--DEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERD 724
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
966-1225 |
7.80e-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: 7.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 966 LATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEM 1045
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1046 QGQELHRKLGVLEEEVRaarraqeetrgqqqallrdhEALVQLQRRQETELEGLLVRHRDLKANMRALELAH---RELQG 1122
Cdd:COG4942 91 EIAELRAELEAQKEELA--------------------ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKylaPARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1123 RHEQLQAQRANVEAQEVALLAERERLMQDghrQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLEL 1202
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERAELEAL---LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
250 260
....*....|....*....|...
gi 1907133161 1203 ERAQLEIQSQQLRESNQQLDLSA 1225
Cdd:COG4942 228 LIARLEAEAAAAAERTPAAGFAA 250
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
839-1223 |
1.24e-07 |
|
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: 56.06 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 839 LRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVlrgQELGDRLEHLQEELEQAALERQKFLQEQENqhq 918
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQR---RELESRVAELKEELRQSREKHEELEEKYKE--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 919 ryrhlEQRLEAELQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVErnnatlvAEK 998
Cdd:pfam07888 106 -----LSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEE-------AER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 999 AALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLE---EEVRAARRAQEETRGQQ 1075
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEallEELRSLQERLNASERKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1076 QALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQ-LQAQRANVEAqevallaERERLMQDGHR 1154
Cdd:pfam07888 254 EGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQeRETLQQSAEA-------DKDRIEKLSAE 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907133161 1155 QRGLEEelrRLQNEHERAQMLLAEVSRER-------GELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDL 1223
Cdd:pfam07888 327 LQRLEE---RLQEERMEREKLEVELGREKdcnrvqlSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQ 399
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1089-1307 |
1.36e-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: 56.60 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1089 QRRQETELegllvRHRDLKANMRALELAHRELQGRHEQLQAQ----------RANVEAQEVALLA--------ERERLMQ 1150
Cdd:TIGR02168 172 ERRKETER-----KLERTRENLDRLEDILNELERQLKSLERQaekaerykelKAELRELELALLVlrleelreELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1151 D----GHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSAC 1226
Cdd:TIGR02168 247 ElkeaEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1227 RLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLhREQREYLDQLNALRREKQKLVEKIMDQYRVL 1306
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL-EELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
.
gi 1907133161 1307 E 1307
Cdd:TIGR02168 406 E 406
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
133-474 |
1.40e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 133 EEAVDELESILRLLLGASVQCEHRELFIRHIRGLSLDVQSELAGAIQEVTQPGAGVVLALAGPESGELVAEELEMQLRSL 212
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 213 TGMMSRLARERDLGAQRLAELLLEREpahlllpeapanasaegvshHLALQLTNAKAQLRRLRQEVEEKAEQLLDSQAEV 292
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELE--------------------EAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 293 QGLEAEIRRLRQETQALSAQAKRA--ELYREEAEALRERAgrlprlqEELRRCREKLQAAEVFKGQLEEERVLSEALEAS 370
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALleRLERLEEELEELEE-------ALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 371 KVLLEEQLEVARERSARLHETQRENLLLRTRLgeahadldSLRHQLEQLVEENVELELELQRSLEPPPGSPGEASLPGAA 450
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARL--------LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE 533
|
330 340
....*....|....*....|....
gi 1907133161 451 PSLQDEVREAEAGRLRAVERENRE 474
Cdd:COG1196 534 AAYEAALEAALAAALQNIVVEDDE 557
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
732-1266 |
2.38e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 55.68 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 732 QALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELEAA 811
Cdd:PRK01156 193 KSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKN 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 812 ---SREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHlEEAEREHAEKQALREELEKAvlrgQEL 888
Cdd:PRK01156 273 nyyKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKY-HAIIKKLSVLQKDYNDYIKK----KSR 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 889 GDRLEHLQEELEQAALERQKFLQEQENQHQRYRhlEQRLEAELQAASTSKEEALMELKARALQLEEELIqlrqypvdlat 968
Cdd:PRK01156 348 YDDLNNQILELEGYEMDYNSYLKSIESLKKKIE--EYSKNIERMSAFISEILKIQEIDPDAIKKELNEI----------- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 969 garagprtvetqNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRL----QAEKSMME 1044
Cdd:PRK01156 415 ------------NVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIinhyNEKKSRLE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1045 MQGQELHRKLGVLEEEVRAARRAQEETRGQQ-------QALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAH 1117
Cdd:PRK01156 483 EKIREIEIEVKDIDEKIVDLKKRKEYLESEEinksineYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLED 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1118 RE--------------------LQGRHEQLQAQRANVEA--QEVALLAERERLMQDGHRQRgLEEELRRLQNEHERAQml 1175
Cdd:PRK01156 563 LDskrtswlnalavislidietNRSRSNEIKKQLNDLESrlQEIEIGFPDDKSYIDKSIRE-IENEANNLNNKYNEIQ-- 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1176 laEVSRERGELQGERGELRSRLARL-ELERAQLEIQSqQLRESNQQLDLSACRLTTQCELLTQLRSaQEEENRQLLAEVQ 1254
Cdd:PRK01156 640 --ENKILIEKLRGKIDNYKKQIAEIdSIIPDLKEITS-RINDIEDNLKKSRKALDDAKANRARLES-TIEILRTRINELS 715
|
570
....*....|..
gi 1907133161 1255 ALSRENRELLER 1266
Cdd:PRK01156 716 DRINDINETLES 727
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
202-498 |
3.15e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 202 AEELEMQLRSLTGMMSRLARERDLGAQRLAELLLEREPAHLLLpeapanASAEGVSHHLALQLTNAKAQLRRLRQEVEEK 281
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL------EELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 282 AEQLLDSQAEVQGLEAEIRRLRQETQAL-----SAQAKRAELYREEAEALRERAGRLPRLQEELRRCREKLQAAEVFKGQ 356
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELeeeleELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 357 LEEERVLSEALEASKVLLEEQLEVARERSARLHETQRENLLLRTRLGEAHADLDSLRHQLEQLVEENVELELELQRSLEp 436
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE- 459
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907133161 437 ppgspgeaslpGAAPSLQDEVREAEAGR--LRAVERENRELRGQLQMLQAQLGSQHPLLEEQRE 498
Cdd:COG1196 460 -----------ALLELLAELLEEAALLEaaLAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
266-435 |
3.40e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 266 NAKAQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQAL--------------SAQAKRAELyREEAEALRERAG 331
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdeidvaSAEREIAEL-EAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 332 RLPRLQEELRRCREKLQAAEVFKGQLEEERvlsEALEASKVLLEEQLEVARERSARLHETQRE--NLLLRTRLGEAHAD- 408
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEI---GRLEKELEQAEEELDELQDRLEAAEDLARLelRALLEERFAAALGDa 762
|
170 180
....*....|....*....|....*...
gi 1907133161 409 -LDSLRHQLEQLVEENVELELELQRSLE 435
Cdd:COG4913 763 vERELRENLEERIDALRARLNRAEEELE 790
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
844-1295 |
4.26e-07 |
|
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: 54.98 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 844 EAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHL 923
Cdd:pfam02463 161 EAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 924 EQRLEAELQAASTSKEEALMELKARALQLEEELIQLrqypvdlatgaragprtvETQNGRLIEVERnnATLVAEKAALQG 1003
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKE------------------EEKEKKLQEEEL--KLLAKEEEELKS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1004 QLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDH- 1082
Cdd:pfam02463 301 ELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKk 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1083 EALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLMQDGHRQRglEEEL 1162
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELE--KQEL 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1163 RRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQ 1242
Cdd:pfam02463 459 KLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAV 538
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1907133161 1243 EEENRQLLAEVQALsrenRELLERSLESRDHLHREQREYLDQLNALRREKQKL 1295
Cdd:pfam02463 539 ENYKVAISTAVIVE----VSATADEVEERQKLVRALTELPLGARKLRLLIPKL 587
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
916-1140 |
4.91e-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: 54.00 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 916 QHQRYRHLEQRLEaELQAASTSKEEALMELKARALQLEEELIQLRQYPVDLAtgaragpRTVETQNGRLIEVERNNATLV 995
Cdd:COG4942 18 QADAAAEAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA-------RRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 996 AEKAALQGQLQHLEGQLGSLQGRAQ--------ELLLQSQRAQEHSSRLQAEKSMMEM---QGQELHRKLGVLEEEVRAA 1064
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYrlgrqpplALLLSPEDFLDAVRRLQYLKYLAPArreQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907133161 1065 RRAQEETRGQQQALLRDHEALVQLQRRQETELegllvrhRDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVA 1140
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLL-------ARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1142-1299 |
9.09e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 9.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1142 LAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLEL--ERAQLEIQSQQLRESNQ 1219
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1220 QLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKI 1299
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
263-431 |
1.07e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 263 QLTNAKAQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALRERAG---RLPRLQEE 339
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAElpeRLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 340 LRRCREKLQAAEVFKGQLEE-ERVLSEALEASKVLLEEQLEVARERSARLHETQREnllLRTRLGEAHADLDSLRHQLEQ 418
Cdd:COG4717 155 LEELRELEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQRLAE---LEEELEEAQEELEELEEELEQ 231
|
170
....*....|...
gi 1907133161 419 LVEENVELELELQ 431
Cdd:COG4717 232 LENELEAAALEER 244
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
872-1304 |
1.57e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 53.27 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 872 QALREELEKavLRGQELGDRL------EHLQEELEQAALERQKFLQEQENQHQRYRHLEQR--LEAELQAASTSKEEALM 943
Cdd:PRK10246 194 KSARTELEK--LQAQASGVALltpeqvQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLdeLQQEASRRQQALQQALA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 944 ELKARA-----LQLEEELIQLR---QYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSL 1015
Cdd:PRK10246 272 AEEKAQpqlaaLSLAQPARQLRphwERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTW 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1016 QGRAQELLLQSQ-----RAQ-EHSSRLQAEKSMMEMQGQELHRKLGVL--------EEEVRAARRAQEETRGQQQALLRD 1081
Cdd:PRK10246 352 LAEHDRFRQWNNelagwRAQfSQQTSDREQLRQWQQQLTHAEQKLNALpaitltltADEVAAALAQHAEQRPLRQRLVAL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1082 HEALVQLQRRQETelegllvrhrdlkaNMRALELAHRELQGRHEQLQAQR-----ANVEAQEVALLAERERLMQDghrqr 1156
Cdd:PRK10246 432 HGQIVPQQKRLAQ--------------LQVAIQNVTQEQTQRNAALNEMRqrykeKTQQLADVKTICEQEARIKD----- 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1157 gLEEELRRLQ----------NEH---ERAQMLlaevsrergelqgERGELRSRLARLELERAQLEIQSQQLResnqqldl 1223
Cdd:PRK10246 493 -LEAQRAQLQagqpcplcgsTSHpavEAYQAL-------------EPGVNQSRLDALEKEVKKLGEEGAALR-------- 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1224 sacrltTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLER---SLESRDHLH---REQREYLDQLNALrREKQKLVE 1297
Cdd:PRK10246 551 ------GQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASlniTLQPQDDIQpwlDAQEEHERQLRLL-SQRHELQG 623
|
....*..
gi 1907133161 1298 KIMDQYR 1304
Cdd:PRK10246 624 QIAAHNQ 630
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
890-1144 |
1.61e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 890 DRLEHLQEELEQAAlERQKFLQEQENQHQRYRHLEQRLeAELQAastskeealMELKARALQLEEELIQLRQypvdlatg 969
Cdd:COG4913 235 DDLERAHEALEDAR-EQIELLEPIRELAERYAAARERL-AELEY---------LRAALRLWFAQRRLELLEA-------- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 970 aragprtvetqngrliEVERNNAtlvaEKAALQGQLQHLEGQLGSLQGRAQELllQSQRAQEHSSRLQAEKSMMEMQGQE 1049
Cdd:COG4913 296 ----------------ELEELRA----ELARLEAELERLEARLDALREELDEL--EAQIRGNGGDRLEQLEREIERLERE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1050 LHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQA 1129
Cdd:COG4913 354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
250
....*....|....*
gi 1907133161 1130 QRANVEAQEVALLAE 1144
Cdd:COG4913 434 RKSNIPARLLALRDA 448
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
730-1222 |
1.66e-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: 53.05 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 730 EEQALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEALCLSEELaQARRTEAEAHQEAEAQAREQARLREAVDTASLELE 809
Cdd:TIGR00618 373 QQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRT-SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTA 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 810 AASREREALAEALAAAGRERRQWERDGPRLRAQVE---AAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQ 886
Cdd:TIGR00618 452 QCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETrkkAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQ 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 887 ELGDRLEHLQEELEQAALErqkfLQEQENQHQRYRHLEQRLEAELQAAsTSKEEALMELKARALQLEEELIQLRQypvdl 966
Cdd:TIGR00618 532 RGEQTYAQLETSEEDVYHQ----LTSERKQRASLKEQMQEIQQSFSIL-TQCDNRSKEDIPNLQNITVRLQDLTE----- 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 967 atgARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQ-LGSLQGRAQELLLQSQRAQEHSSRLQAEKSmmem 1045
Cdd:TIGR00618 602 ---KLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALkLTALHALQLTLTQERVREHALSIRVLPKEL---- 674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1046 qGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQG-RH 1124
Cdd:TIGR00618 675 -LASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHqAR 753
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1125 EQLQAQRANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGE-----------LQGERGEL 1193
Cdd:TIGR00618 754 TVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSdedilnlqcetLVQEEEQF 833
|
490 500
....*....|....*....|....*....
gi 1907133161 1194 RSRLARLELERAQLEIQSQQLRESNQQLD 1222
Cdd:TIGR00618 834 LSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
736-1207 |
2.15e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.65 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 736 DEVAQLRREVAGLEVKLQAQAQRLEARSAEALCLSEELA------QARRTEAEAHQEAEAQAREQARLREAVDTASLELE 809
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESdleqdyQAASDHLNLVQTALRQQEKIERYQADLEELEERLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 810 AASRErealaealaaagRERRQWERDgpRLRAQVEAAEQQVQALESQ---VRCHLEEAERE----HAEKQALREE---LE 879
Cdd:PRK04863 366 EQNEV------------VEEADEQQE--ENEARAEAAEEEVDELKSQladYQQALDVQQTRaiqyQQAVQALERAkqlCG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 880 KAVLRGQELGDRLEHLQEELEQAALERqkflqeqenqhqryRHLEQRLEAElQAASTSKEEAlMELKARAlqleeeliql 959
Cdd:PRK04863 432 LPDLTADNAEDWLEEFQAKEQEATEEL--------------LSLEQKLSVA-QAAHSQFEQA-YQLVRKI---------- 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 960 rqypvdlatgarAGprtvetqngrliEVERNNAtlvaekaalqgqlqhlegqlgslQGRAQELLLQSQRAQEHSSRLQAe 1039
Cdd:PRK04863 486 ------------AG------------EVSRSEA-----------------------WDVARELLRRLREQRHLAEQLQQ- 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1040 ksmMEMQGQELHRKLgvleEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLlvrhRDLKANMRALELAHRE 1119
Cdd:PRK04863 518 ---LRMRLSELEQRL----RQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESL----SESVSEARERRMALRQ 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1120 LQgrhEQLQAQRANVEAQEVALLAERERLMQDGhRQRGLEEELRRlQNEHERAQMLLaevsRERgELQGERGELRSRLAR 1199
Cdd:PRK04863 587 QL---EQLQARIQRLAARAPAWLAAQDALARLR-EQSGEEFEDSQ-DVTEYMQQLLE----RER-ELTVERDELAARKQA 656
|
....*...
gi 1907133161 1200 LELERAQL 1207
Cdd:PRK04863 657 LDEEIERL 664
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
923-1187 |
2.31e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 923 LEQRLEAELQAASTSK---EEALMELKARALQLEEELIQLRQypvdlatgaragprtvetQNGrLIEVERNNATLVAEKA 999
Cdd:COG3206 162 LEQNLELRREEARKALeflEEQLPELRKELEEAEAALEEFRQ------------------KNG-LVDLSEEAKLLLQQLS 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1000 ALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMmemqgQELHRKLGVLEeevraARRAQEETRgqqqaLL 1079
Cdd:COG3206 223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVI-----QQLRAQLAELE-----AELAELSAR-----YT 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1080 RDHEALVQLQRRQEtelegllvrhrDLKANMRalelahRELQGRHEQLQAQRANVEAQEVALLAERERLMQDGHRQRGLE 1159
Cdd:COG3206 288 PNHPDVIALRAQIA-----------ALRAQLQ------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELE 350
|
250 260
....*....|....*....|....*...
gi 1907133161 1160 EELRRLQNEHERAQMLLAEVSRERGELQ 1187
Cdd:COG3206 351 AELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
854-1288 |
2.59e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.65 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 854 ESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLQE---ELE---QAALERQKFLQE---QENQHQRYR--- 921
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEaesDLEqdyQAASDHLNLVQTalrQQEKIERYQadl 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 922 -HLEQRLEAELQAASTSKEEaLMELKARALQLEEELIQLRqypvdlatgaragprtvetqnGRLIEVERnnATLVAEKAA 1000
Cdd:PRK04863 358 eELEERLEEQNEVVEEADEQ-QEENEARAEAAEEEVDELK---------------------SQLADYQQ--ALDVQQTRA 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1001 LQGQ--LQHLEgqlgslqgRAQELLLQSQRAQEHSSRLQAEksmMEMQGQELHRKLGVLEEEVRAArraqeetrgqqQAL 1078
Cdd:PRK04863 414 IQYQqaVQALE--------RAKQLCGLPDLTADNAEDWLEE---FQAKEQEATEELLSLEQKLSVA-----------QAA 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1079 LRDHEALVQLQRRQETELEgllvrhrdlkaNMRALELAhRELQGRHEQLQAQRANVEAQEVALlaerERLMQDGHRQRGL 1158
Cdd:PRK04863 472 HSQFEQAYQLVRKIAGEVS-----------RSEAWDVA-RELLRRLREQRHLAEQLQQLRMRL----SELEQRLRQQQRA 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1159 EEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQL 1238
Cdd:PRK04863 536 ERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARL 615
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1907133161 1239 R--SAQEEENRQLLAE-VQALSRENRELlersLESRDHLHREQREYLDQLNAL 1288
Cdd:PRK04863 616 ReqSGEEFEDSQDVTEyMQQLLEREREL----TVERDELAARKQALDEEIERL 664
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
729-1208 |
2.59e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 729 PEEQALRDEVAQLRREVAGLE---VKLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLREavdtas 805
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEelkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE------ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 806 leLEAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRcHLEEAEREHAEKQALREELEKAVLRG 885
Cdd:PRK03918 288 --LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE-RLEELKKKLKELEKRLEELEERHELY 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 886 QELGDRLEHLQE-ELEQAALERQKFLQEQENQHQRYRHLEQRLE------AELQAASTSKEEALMELKA---------RA 949
Cdd:PRK03918 365 EEAKAKKEELERlKKRLTGLTPEKLEKELEELEKAKEEIEEEISkitariGELKKEIKELKKAIEELKKakgkcpvcgRE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 950 LQLEEELIQLRQYPVDLA----TGARAGPRTVETQNgRLIEVER---NNATLVAEKAALQgQLQHLEGQLGS-----LQG 1017
Cdd:PRK03918 445 LTEEHRKELLEEYTAELKriekELKEIEEKERKLRK-ELRELEKvlkKESELIKLKELAE-QLKELEEKLKKynleeLEK 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1018 RAQELLLQSQRAQEHSSRLQAEKSMMEmQGQELHRKLGVLEEEVRAARRAQEETRGQQQALlrDHEALVQLQRRQEtELE 1097
Cdd:PRK03918 523 KAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEEL--GFESVEELEERLK-ELE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1098 GLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLmqDGHRQRGLEEELRRLQNEHERAQMLLA 1177
Cdd:PRK03918 599 PFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL--EELEKKYSEEEYEELREEYLELSRELA 676
|
490 500 510
....*....|....*....|....*....|.
gi 1907133161 1178 EVSRERGELQGERGELRSRLARLELERAQLE 1208
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
261-418 |
2.68e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 261 ALQLTNAKAQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEA--EALRERAGRLPRLQE 338
Cdd:COG4913 273 ELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggDRLEQLEREIERLER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 339 ELRRCREKLQAAEVFKGQLEEERVLSEA-LEASKVLLEEQLEVARERSARLHETQRENLLLRTRLGEAHADLDSLRHQLE 417
Cdd:COG4913 353 ELEERERRRARLEALLAALGLPLPASAEeFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
.
gi 1907133161 418 Q 418
Cdd:COG4913 433 R 433
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
906-1270 |
4.07e-06 |
|
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: 50.83 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 906 RQKFLQEQENQHQRYRHLEQRLeaelQAASTSKEEAL-------MELKARALQLEEELIQLRQypvdlatgaragprTVE 978
Cdd:pfam15742 4 GEKLKYQQQEEVQQLRQNLQRL----QILCTSAEKELryergknLDLKQHNSLLQEENIKIKA--------------ELK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 979 TQNGRLIEVERNNATLVAEKAALQGQLQHLEGQ-LGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQgQELHRKLGVL 1057
Cdd:pfam15742 66 QAQQKLLDSTKMCSSLTAEWKHCQQKIRELELEvLKQAQSIKSQNSLQEKLAQEKSRVADAEEKILELQ-QKLEHAHKVC 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1058 EEEVRAARRAQEETRGQQ----QALLRDHEALVQLQRRQ-ETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRA 1132
Cdd:pfam15742 145 LTDTCILEKKQLEERIKEasenEAKLKQQYQEEQQKRKLlDQNVNELQQQVRSLQDKEAQLEMTNSQQQLRIQQQEAQLK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1133 NVEAqevallaerERLMQDGHR--QRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRL-ARLELERAQLEI 1209
Cdd:pfam15742 225 QLEN---------EKRKSDEHLksNQELSEKLSSLQQEKEALQEELQQVLKQLDVHVRKYNEKHHHHkAKLRRAKDRLVH 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907133161 1210 QSQQLRESNQQLDlsacrltTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLES 1270
Cdd:pfam15742 296 EVEQRDERIKQLE-------NEIGILQQQSEKEKAFQKQVTAQNEILLLEKRKLLEQLTEQ 349
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1036-1302 |
4.11e-06 |
|
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: 51.66 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1036 LQAEKSMMEMQGQELHRKLgvleeevraarrAQEETRGQQQALLRDHEALVQLQ-----RRQETELEGLLVRHRDLKANM 1110
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKM------------EQERLRQEKEEKAREVERRRKLEeaekaRQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1111 RALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLM----QDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGEL 1186
Cdd:pfam17380 346 RERELERIRQEERKRELERIRQEEIAMEISRMRELERLQmerqQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1187 QGERGELRSR-LARLELERAQlEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEvqalsrENRELLE 1265
Cdd:pfam17380 426 RAEQEEARQReVRRLEEERAR-EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEE------QRRKILE 498
|
250 260 270
....*....|....*....|....*....|....*..
gi 1907133161 1266 RSLESRDHLHREQreyldqlnalrREKQKLVEKIMDQ 1302
Cdd:pfam17380 499 KELEERKQAMIEE-----------ERKRKLLEKEMEE 524
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
723-1291 |
4.14e-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: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 723 TLVSAIPEEQALRDEVAQLRREVAGLEVKLQAQAQ--------RLEARSAEALCLSEEL---AQARRTEAEAHQEAEAQA 791
Cdd:COG3321 805 GLVRQCLAAAGDAVVLPSLRRGEDELAQLLTALAQlwvagvpvDWSALYPGRGRRRVPLptyPFQREDAAAALLAAALAA 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 792 REQARLREAVDTASLELEAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEK 871
Cdd:COG3321 885 ALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGAL 964
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 872 QALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALMELKARALQ 951
Cdd:COG3321 965 LLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAA 1044
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 952 LEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQE 1031
Cdd:COG3321 1045 AAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAAL 1124
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1032 HSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMR 1111
Cdd:COG3321 1125 LALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAAL 1204
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1112 ALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERG 1191
Cdd:COG3321 1205 LAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAA 1284
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1192 ELRSRLARLELERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESR 1271
Cdd:COG3321 1285 LALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALA 1364
|
570 580
....*....|....*....|
gi 1907133161 1272 DHLHREQREYLDQLNALRRE 1291
Cdd:COG3321 1365 AAAGAAAAAAALALAALAAA 1384
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
841-1072 |
4.39e-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: 50.92 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 841 AQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRY 920
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 921 RHLEQRLEAELQAASTSKEEALMELKARAlqleeeliqlrQYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAEKAA 1000
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSP-----------EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907133161 1001 LQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETR 1072
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
277-488 |
5.59e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 277 EVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSaqakRAELYREEAEALRERAGRLPRLQEELRRCREKlQAAEVFKGQ 356
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIELLE----PIRELAERYAAARERLAELEYLRAALRLWFAQ-RRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 357 LEEERVLSEALEASKVLLEEQLEVARERSARLHETQRENLLlrTRLGEAHADLDSLRHQLEQLVEENVELELELQRSLEP 436
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG--DRLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907133161 437 PPGSPGE-ASLPGAAPSLQDEVREAEAG---RLRAVERENRELRGQLQMLQAQLGS 488
Cdd:COG4913 375 LPASAEEfAALRAEAAALLEALEEELEAleeALAEAEAALRDLRRELRELEAEIAS 430
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
725-1280 |
8.53e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.49 E-value: 8.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 725 VSAIPEEQALRDE-VAQLRREVAGLEVKLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLREAVDT 803
Cdd:pfam05483 270 ANQLEEKTKLQDEnLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSF 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 804 ASLELEAASREREALAEAlaaagrERRQWERDGPRLRaqVEAAEQQVQALEsqvrchLEEAEREHAEKQALREELEKAVL 883
Cdd:pfam05483 350 VVTEFEATTCSLEELLRT------EQQRLEKNEDQLK--IITMELQKKSSE------LEEMTKFKNNKEVELEELKKILA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 884 RGQELGD---RLEHLQEELEQAALERQKFLQEQENQhqryrhlEQRLEAELQAASTSKEEALMELKARALQLEEELIQlr 960
Cdd:pfam05483 416 EDEKLLDekkQFEKIAEELKGKEQELIFLLQAREKE-------IHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLK-- 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 961 qypvdlatgaragpRTVETQNGRLIEVErnNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAE- 1039
Cdd:pfam05483 487 --------------NIELTAHCDKLLLE--NKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDEl 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1040 ---KSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRAlela 1116
Cdd:pfam05483 551 esvREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSA---- 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1117 hrelqgRHEQLQAQRANVEAQEVALLAERERL--MQDGHRQ----RGLEEElrRLQNEHERAQMLLAEVSRERGELQGE- 1189
Cdd:pfam05483 627 ------ENKQLNAYEIKVNKLELELASAKQKFeeIIDNYQKeiedKKISEE--KLLEEVEKAKAIADEAVKLQKEIDKRc 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1190 RGELRSRLARLELERAQLEiqsQQLRESNQQLDLSACRLTTQcellTQLRSAQEEENRQLLAEVQALSREnrelLERSLE 1269
Cdd:pfam05483 699 QHKIAEMVALMEKHKHQYD---KIIEERDSELGLYKNKEQEQ----SSAKAALEIELSNIKAELLSLKKQ----LEIEKE 767
|
570
....*....|.
gi 1907133161 1270 SRDHLHREQRE 1280
Cdd:pfam05483 768 EKEKLKMEAKE 778
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1127-1299 |
9.46e-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: 49.76 E-value: 9.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1127 LQAQRANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQ 1206
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1207 LEIQSQQLRESNQQLDLSACRLTTQCEL---------------------LTQLRSAQEEENRQLLAEVQALsrenRELLE 1265
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLalllspedfldavrrlqylkyLAPARREQAEELRADLAELAAL----RAELE 170
|
170 180 190
....*....|....*....|....*....|....
gi 1907133161 1266 RSLESRDHLHREQREYLDQLNALRREKQKLVEKI 1299
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARL 204
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
848-1252 |
1.01e-05 |
|
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: 50.56 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 848 QQVQALESQVRCHLEEAEREH----AEKQALREELE--------------KAVLRGQELGDRLEHLQEELEQAALERQKF 909
Cdd:pfam01576 15 QKVKERQQKAESELKELEKKHqqlcEEKNALQEQLQaetelcaeaeemraRLAARKQELEEILHELESRLEEEEERSQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 910 LQEQENQHQRYRHLEQRLEAElQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVER 989
Cdd:pfam01576 95 QNEKKKMQQHIQDLEEQLDEE-EAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 990 NNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAAR-RAQ 1068
Cdd:pfam01576 174 KAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALaRLE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1069 EETRGQQQALLRDHEALVQLQRRQEtelegllvrhrDLKANMRALELAHRELQGRHEQLQAQRANVE------AQEVALL 1142
Cdd:pfam01576 254 EETAQKNNALKKIRELEAQISELQE-----------DLESERAARNKAEKQRRDLGEELEALKTELEdtldttAAQQELR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1143 AERERlmQDGHRQRGLEEELRR----LQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESN 1218
Cdd:pfam01576 323 SKREQ--EVTELKKALEEETRSheaqLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430
....*....|....*....|....*....|....
gi 1907133161 1219 QQLDLSACRLTTQCELLtQLRSAQEEENRQLLAE 1252
Cdd:pfam01576 401 QDSEHKRKKLEGQLQEL-QARLSESERQRAELAE 433
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
844-1221 |
1.02e-05 |
|
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: 50.07 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 844 EAAEQQVQALESQVRCHLEEAEREHAEKQALRE---ELEKAVLRGQELGDRLEHLQEELEQaalerqkfLQEQ----ENQ 916
Cdd:pfam05622 10 DELAQRCHELDQQVSLLQEEKNSLQQENKKLQErldQLESGDDSGTPGGKKYLLLQKQLEQ--------LQEEnfrlETA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 917 HQRYRHLEQRLEAELQAAStSKEEALMELKARALQLEEELIQLRQypvdlatgaragprtvetQNGRLIEVErnnATLVA 996
Cdd:pfam05622 82 RDDYRIKCEELEKEVLELQ-HRNEELTSLAEEAQALKDEMDILRE------------------SSDKVKKLE---ATVET 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 997 EKAALQgQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEM---QGQELHRKLgvlEEEVRAARRAQEETR- 1072
Cdd:pfam05622 140 YKKKLE-DLGDLRRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETykrQVQELHGKL---SEESKKADKLEFEYKk 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1073 --GQQQALLRDHEALV----------------QLQRRQETELEGLLVRHRDLKANMRAlELAHRELQGRHEQLQAQ---- 1130
Cdd:pfam05622 216 leEKLEALQKEKERLIierdtlretneelrcaQLQQAELSQADALLSPSSDPGDNLAA-EIMPAEIREKLIRLQHEnkml 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1131 RANVEAQEVALLAERERLMQDGHRQR-GLEEELRRlqneherAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEI 1209
Cdd:pfam05622 295 RLGQEGSYRERLTELQQLLEDANRRKnELETQNRL-------ANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEE 367
|
410
....*....|..
gi 1907133161 1210 QSQQLRESNQQL 1221
Cdd:pfam05622 368 HLEKLHEAQSEL 379
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1125-1293 |
1.18e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1125 EQLQAQRANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLA--EVSRERGELQGERGELRSRLARLEL 1202
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1203 ERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYL 1282
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170
....*....|.
gi 1907133161 1283 DQLNALRREKQ 1293
Cdd:COG4717 234 NELEAAALEER 244
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
875-1247 |
1.33e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.97 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 875 REELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRlEAELQAASTSKEEALMELKARALQLEE 954
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA-KKALEYYQLKEKLELEEEYLLYLDYLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 955 ELIQLRQypvDLATGARAGPRTVETQNGRLIEVERNNAT---LVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQE 1031
Cdd:pfam02463 234 LNEERID---LLQELLRDEQEEIESSKQEIEKEEEKLAQvlkENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1032 HSSRlQAEKSMMEMQGQELHRKLgvLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKanmr 1111
Cdd:pfam02463 311 DDEE-KLKESEKEKKKAEKELKK--EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES---- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1112 alelAHRELQGRHEQLQAQRANVEAQEVALLAERERlmQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERG 1191
Cdd:pfam02463 384 ----ERLSSAAKLKEEELELKSEEEKEAQLLLELAR--QLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQE 457
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907133161 1192 ELRSRLaRLELERAQLEIQSQQLRESNQQLDLsACRLTTQCELLTQLRSAQEEENR 1247
Cdd:pfam02463 458 LKLLKD-ELELKKSEDLLKETQLVKLQEQLEL-LLSRQKLEERSQKESKARSGLKV 511
|
|
| MAP70 |
pfam07058 |
Microtubule-associated protein 70; This family represents a family of plant ... |
853-1106 |
1.40e-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: 49.81 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 853 LESQVRCHLEEAEREHAEKQALRE---ELEKAVLrgqELGDRLEHLQEELEQA-ALERQKFLQEQENQHQRYRHLEQRLE 928
Cdd:pfam07058 12 LENEVRDKDRELGEALAEIKALRLserLKEKAVE---ELTDELLKLDEKLKASeNLLESKNLEIKKINDEKKAALAAQFA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 929 AELQAA---STSKEEALMELKARALQLEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAeKAALQGQL 1005
Cdd:pfam07058 89 AEATLRrvhAAQKDEDMPPIEAILAPLEAELKLARQEINKLQDDNKALDRLTKSKEAALLEAERAVQIALA-KASLVDDL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1006 QHlegqlgslqgRAQELLLQSQRAQEHSSRLQAeksmMEMQgqelhrKLGVLEEEVRAARRAQEETrgqqQALLRDHEAL 1085
Cdd:pfam07058 168 QN----------KNQELMKQIEICQEENKILDK----AHRQ------KVAEVEKLSQTVRELEEAV----LAGGAAANAV 223
|
250 260
....*....|....*....|.
gi 1907133161 1086 VQLQRRQETELEGLLVRHRDL 1106
Cdd:pfam07058 224 RDYQRKVKEMNEERRTLEREL 244
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1027-1299 |
1.60e-05 |
|
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: 49.74 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1027 QRAQEHSSRLQAEKSMMEMqgqELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDL 1106
Cdd:pfam05557 5 IESKARLSQLQNEKKQMEL---EHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1107 KANMRALELAHRElqgrHEQLQAqranvEAQEVallaererlmqdghrQRGLEEELRRLQNEHERAQMLLAEVSRERGEL 1186
Cdd:pfam05557 82 KKYLEALNKKLNE----KESQLA-----DAREV---------------ISCLKNELSELRRQIQRAELELQSTNSELEEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1187 QGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENR--QLLAEVQAL-------- 1256
Cdd:pfam05557 138 QERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARipELEKELERLrehnkhln 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907133161 1257 -SRENRELLERSLES-RDHLHREQrEYLDQLNALRREKQKLVEKI 1299
Cdd:pfam05557 218 eNIENKLLLKEEVEDlKRKLEREE-KYREEAATLELEKEKLEQEL 261
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
863-1259 |
1.60e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.80 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 863 EAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLeaelqaastSKEEAL 942
Cdd:PRK10246 413 AALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQL---------ADVKTI 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 943 MELKARALQLEEELIQLRQYPVDLATGARAGPR-------TVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSL 1015
Cdd:PRK10246 484 CEQEARIKDLEAQRAQLQAGQPCPLCGSTSHPAveayqalEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRD 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1016 QGRAQELLLQSQ----RAQEHSSRLQAEKSMME-----MQGQELHRKL-----------GVLEEEVRAARRAQEETRGQQ 1075
Cdd:PRK10246 564 ESEAQSLRQEEQaltqQWQAVCASLNITLQPQDdiqpwLDAQEEHERQlrllsqrhelqGQIAAHNQQIIQYQQQIEQRQ 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1076 QAL--------------------LRDHEALVQLQRRQETELEGLLVRHRDLKANMRAL-----------ELAHRELQGRH 1124
Cdd:PRK10246 644 QQLltalagyaltlpqedeeaswLATRQQEAQSWQQRQNELTALQNRIQQLTPLLETLpqsddlphseeTVALDNWRQVH 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1125 EQ---LQAQRANVEAQEVallAERER--------------------------LMQDGHRQRgLEEELRRLQNEHERAQML 1175
Cdd:PRK10246 724 EQclsLHSQLQTLQQQDV---LEAQRlqkaqaqfdtalqasvfddqqaflaaLLDEETLTQ-LEQLKQNLENQRQQAQTL 799
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1176 LAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNqqldlsacrlTTQCELLTQLRsaQEEENRQ----LLA 1251
Cdd:PRK10246 800 VTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENT----------TRQGEIRQQLK--QDADNRQqqqaLMQ 867
|
....*...
gi 1907133161 1252 EVQALSRE 1259
Cdd:PRK10246 868 QIAQATQQ 875
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
656-1300 |
1.65e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 656 AELTLREPLKDQKALDRELELSKQQKETGRHEQRPKGLESKLGPQKPQQTSEgvpdaWSREeptpgetLVSAIPEEQALR 735
Cdd:PRK04863 445 EEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWD-----VARE-------LLRRLREQRHLA 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 736 DEVAQLRREVAGLEVKLQAQaqrleaRSAEALclseeLAQARRTEAEAHQEAEAQAREQARLREAVDTASLELEAASRER 815
Cdd:PRK04863 513 EQLQQLRMRLSELEQRLRQQ------QRAERL-----LAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERR 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 816 EALAEALAAAGRERRQWERDGP----------RLRAQVEAAEQQVQALESQVRCHLEEaERE--------HAEKQALREE 877
Cdd:PRK04863 582 MALRQQLEQLQARIQRLAARAPawlaaqdalaRLREQSGEEFEDSQDVTEYMQQLLER-EREltverdelAARKQALDEE 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 878 LEKAVLRGQELGDRLEHLQE--------------ELEQAA-----------------LERQKflqeqenqhqryRHLEQR 926
Cdd:PRK04863 661 IERLSQPGGSEDPRLNALAErfggvllseiyddvSLEDAPyfsalygparhaivvpdLSDAA------------EQLAGL 728
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 927 ---------LEAELQAASTSKEEAlmELKARALQLEEELIQLR--QYPVDLATGARAGPRTVETQNGRLIEVERNNATLV 995
Cdd:PRK04863 729 edcpedlylIEGDPDSFDDSVFSV--EELEKAVVVKIADRQWRysRFPEVPLFGRAAREKRIEQLRAEREELAERYATLS 806
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 996 AEKAALQGQLQHL----------------EGQLGSLQGRAQELL--LQSQRAQEHSSRLQAEKSMMEMQG-QELHRKLGV 1056
Cdd:PRK04863 807 FDVQKLQRLHQAFsrfigshlavafeadpEAELRQLNRRRVELEraLADHESQEQQQRSQLEQAKEGLSAlNRLLPRLNL 886
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1057 LEEEVRAARraQEETRGQQQALLRDhEALVQLQRRQETELEGLLvrhrdlkANMRALELAHRELQGRHEQLQAQRANVEA 1136
Cdd:PRK04863 887 LADETLADR--VEEIREQLDEAEEA-KRFVQQHGNALAQLEPIV-------SVLQSDPEQFEQLKQDYQQAQQTQRDAKQ 956
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1137 QEVALlaerERLMQdghrqrgleeelRRLQNEHERAQMLLAEVSrergelqgergELRSRLarleleRAQLEIQSQQLRE 1216
Cdd:PRK04863 957 QAFAL----TEVVQ------------RRAHFSYEDAAEMLAKNS-----------DLNEKL------RQRLEQAEQERTR 1003
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1217 SNQQLDLSACRLTTQCELLTQLRS---AQEEENRQLLAEVQALS-RENRELLERSLESRDHLH------REQREYLD-QL 1285
Cdd:PRK04863 1004 AREQLRQAQAQLAQYNQVLASLKSsydAKRQMLQELKQELQDLGvPADSGAEERARARRDELHarlsanRSRRNQLEkQL 1083
|
730
....*....|....*
gi 1907133161 1286 NALRREKQKLVEKIM 1300
Cdd:PRK04863 1084 TFCEAEMDNLTKKLR 1098
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1040-1246 |
1.71e-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: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1040 KSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEaLVQLQRRQETELEGLlvrhRDLKANMRALELAHRE 1119
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG-LVDLSEEAKLLLQQL----SELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1120 LQGRHEQLQAQRA----------------NVEAQEVALLAERERLMQ---DGHRQ-RGLEEELRRLQNE-HERAQMLLAE 1178
Cdd:COG3206 238 AEARLAALRAQLGsgpdalpellqspviqQLRAQLAELEAELAELSArytPNHPDvIALRAQIAALRAQlQQEAQRILAS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907133161 1179 VSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSACRLTTqceLLTQLRSAQEEEN 1246
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES---LLQRLEEARLAEA 382
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
839-1228 |
2.13e-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: 49.57 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 839 LRAQVEAAEQQVQALESQVRchLEEAEREHAEKQALREELEKAV-------------LRGQELGDRLEHLQEELEQAALE 905
Cdd:COG3096 288 LELRRELFGARRQLAEEQYR--LVEMARELEELSARESDLEQDYqaasdhlnlvqtaLRQQEKIERYQEDLEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 906 RQKFLQEQENQHQRYRHLEQRLEAELQAASTS---KEEALMELKARALQLEEELIQLRQypvdlatgARAgprtvetqng 982
Cdd:COG3096 366 QEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQladYQQALDVQQTRAIQYQQAVQALEK--------ARA---------- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 983 RLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQgraQELLLQSQRAQEHSSRLQAEKSMM-EMQGQELHrklGVLEEEV 1061
Cdd:COG3096 428 LCGLPDLTPENAEDYLAAFRAKEQQATEEVLELE---QKLSVADAARRQFEKAYELVCKIAgEVERSQAW---QTARELL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1062 RAAR--RAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQEV 1139
Cdd:COG3096 502 RRYRsqQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1140 ALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELrsrlarLELERaQLEIQSQQLRESNQ 1219
Cdd:COG3096 582 ELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQL------LERER-EATVERDELAARKQ 654
|
....*....
gi 1907133161 1220 QLDLSACRL 1228
Cdd:COG3096 655 ALESQIERL 663
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
871-1098 |
2.16e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 871 KQALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQE--NQHQRYRHLEQRLeAELQAASTSKEEALMELKAR 948
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQL-SELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 949 ALQLEEELIQLRQYPVDLAtgaragprtvetQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQ-SQ 1027
Cdd:COG3206 242 LAALRAQLGSGPDALPELL------------QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQQ 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907133161 1028 RAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEEtrgqQQALLRDHEALVQ-----LQRRQETELEG 1098
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE----LRRLEREVEVARElyeslLQRLEEARLAE 381
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
863-1307 |
2.59e-05 |
|
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: 48.95 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 863 EAEREHAEK--QALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEE 940
Cdd:pfam05483 175 EYEREETRQvyMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKEN 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 941 ALMELkarALQLEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNATL---VAEKAALQGQLQhlegqlgsLQG 1017
Cdd:pfam05483 255 KMKDL---TFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLqrsMSTQKALEEDLQ--------IAT 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1018 RAQELLLQSQRAQ-EHSSRLQAEKSMMEmqgQELHRKLGVLEEEVRAARRAQEETRGQQQALL-------RDHEALVQLQ 1089
Cdd:pfam05483 324 KTICQLTEEKEAQmEELNKAKAAHSFVV---TEFEATTCSLEELLRTEQQRLEKNEDQLKIITmelqkksSELEEMTKFK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1090 RRQETELEGL---LVRHRDLKANMRALELAHRELQGRHEQLqaqranveaqeVALLAERERLMQDghrqrgLEEELRRLQ 1166
Cdd:pfam05483 401 NNKEVELEELkkiLAEDEKLLDEKKQFEKIAEELKGKEQEL-----------IFLLQAREKEIHD------LEIQLTAIK 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1167 NEHeraQMLLAEVSRERGELQGER---GELRSRLARLELERAQL--EIQSQQLRESNQQLDLSACRLTTQcELLTQLRSA 1241
Cdd:pfam05483 464 TSE---EHYLKEVEDLKTELEKEKlknIELTAHCDKLLLENKELtqEASDMTLELKKHQEDIINCKKQEE-RMLKQIENL 539
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907133161 1242 QEEENrQLLAEVQALSRENREL-------LERSLESRDHLHREQREYLDQLNALRREKQKLVEKIMDQYRVLE 1307
Cdd:pfam05483 540 EEKEM-NLRDELESVREEFIQKgdevkckLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIE 611
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
272-1160 |
3.34e-05 |
|
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: 48.63 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 272 RRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEA-EALRERAGRLPRLQEELRRCREKLQAA 350
Cdd:pfam01576 211 RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNAlKKIRELEAQISELQEDLESERAARNKA 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 351 EvfkgqlEEERVLSEALEASKVLLE--------------------EQLEVARERSARLHETQRENllLRTRLGEAhadLD 410
Cdd:pfam01576 291 E------KQRRDLGEELEALKTELEdtldttaaqqelrskreqevTELKKALEEETRSHEAQLQE--MRQKHTQA---LE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 411 SLRHQLEQLVEENVELELELQrslepppgspgeaSLPGAAPSLQDEVREAEAGRLRaVERENRELRGQLQMLQAQLGSQH 490
Cdd:pfam01576 360 ELTEQLEQAKRNKANLEKAKQ-------------ALESENAELQAELRTLQQAKQD-SEHKRKKLEGQLQELQARLSESE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 491 PLLEEQRE--NSRQPPVPNRDPATPSA--LHHSPQSPACQIGGEGSESLDLPSPASYSDITRSPKCSQAPDSHPELESPL 566
Cdd:pfam01576 426 RQRAELAEklSKLQSELESVSSLLNEAegKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQL 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 567 -------QMVSQDPQTSDQALQESDPTVETH-QCLEksghrvplqspivwdppQGPEVRIEVQELLGETGSREAPQgelv 638
Cdd:pfam01576 506 eeeeeakRNVERQLSTLQAQLSDMKKKLEEDaGTLE-----------------ALEEGKKRLQRELEALTQQLEEK---- 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 639 hKAQVLKQESPKCRPRSAELTLREPLKDQKALDRELElsKQQKETGRHEQRPKGLESKLGPQKPQQTSEgvpdawSREEP 718
Cdd:pfam01576 565 -AAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLE--KKQKKFDQMLAEEKAISARYAEERDRAEAE------AREKE 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 719 TPGETLVSAIPEEQALRDEVAQLRREvaglevkLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLR 798
Cdd:pfam01576 636 TRALSLARALEEALEAKEELERTNKQ-------LRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDEL 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 799 EAVDTASLELEAASRERealaealaaagreRRQWERDgprLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREEL 878
Cdd:pfam01576 709 QATEDAKLRLEVNMQAL-------------KAQFERD---LQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAK 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 879 EKAVLRGQELGDRLEHLQEELEQaALERQKFLQEQENQHQRyrhleqrleaELQAASTSKEEALM---ELKARALQLEEE 955
Cdd:pfam01576 773 KKLELDLKELEAQIDAANKGREE-AVKQLKKLQAQMKDLQR----------ELEEARASRDEILAqskESEKKLKNLEAE 841
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 956 LIQLRQypvDLATGARAgPRTVETQNGRLIEVERNNAT----LVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQE 1031
Cdd:pfam01576 842 LLQLQE---DLAASERA-RRQAQQERDELADEIASGASgksaLQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTL 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1032 HSSRLQAE--------------KSMMEMQGQELHRKLGVLEEEVRA----------ARRAQEETRGQQQAllRDHEALVQ 1087
Cdd:pfam01576 918 QVEQLTTElaaerstsqksesaRQQLERQNKELKAKLQEMEGTVKSkfkssiaaleAKIAQLEEQLEQES--RERQAANK 995
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907133161 1088 LQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLmqdghrQRGLEE 1160
Cdd:pfam01576 996 LVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKL------QRELDD 1062
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
60-181 |
3.40e-05 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 45.48 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 60 LIDGALLLRVLGIIAPSSRGGLRMVRGRDGPAA---CRMWNLCHLWGRLRDFYQELQLLILS--PPPDLQTMG--CDPfs 132
Cdd:pfam19047 25 LTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDnwrLKVSNLKKILQSVVDYYQDVLGQQISdfLLPDVNLIGehSDP-- 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1907133161 133 eeavDELESILRLLLGASVQCEHRELFIRHIRGLSLDVQSELAGAIQEV 181
Cdd:pfam19047 103 ----AELGRLLQLILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQEL 147
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
982-1295 |
3.55e-05 |
|
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: 48.35 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 982 GRLIEVERNNATLVAEKAALQGQL----QHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVL 1057
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQRekekERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1058 EEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQ----------- 1126
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQteeelrslske 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1127 LQAQRANVEAQEVALLAERERLMQDGHR-----QRGLE-----EELRRLQNEHERAQMLLAEVSRERGELQGERGELRSR 1196
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKlttahRKEAEneallEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1197 LARLELERAQLEIqsqQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHR 1276
Cdd:pfam07888 274 LHQARLQAAQLTL---QLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGR 350
|
330
....*....|....*....
gi 1907133161 1277 EQREYLDQLNALRREKQKL 1295
Cdd:pfam07888 351 EKDCNRVQLSESRRELQEL 369
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
975-1295 |
5.76e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 975 RTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQG--RAQElllQSQRAQEHSSRLQAEKSMMEMQGQELHR 1052
Cdd:PRK04863 300 RQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTalRQQE---KIERYQADLEELEERLEEQNEVVEEADE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1053 KLGVLEEEVRAARRAQEETRGQqqalLRDH-EALVQLQRR--QETELEGLLVRHRDLKANMralELAHRELQGRHEQLQA 1129
Cdd:PRK04863 377 QQEENEARAEAAEEEVDELKSQ----LADYqQALDVQQTRaiQYQQAVQALERAKQLCGLP---DLTADNAEDWLEEFQA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1130 QRANVeAQEVALLAERERLMQDGHRQ--------RGLEEELRRLQnEHERAQMLLAEVSRERGELQgERGELRSRLARLE 1201
Cdd:PRK04863 450 KEQEA-TEELLSLEQKLSVAQAAHSQfeqayqlvRKIAGEVSRSE-AWDVARELLRRLREQRHLAE-QLQQLRMRLSELE 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1202 LERAQLEIQSQQLRESNQQLDLSacrlTTQCELLTQLRSAQEeenrqllAEVQALSRENRELLERSLESRDHLhreqrey 1281
Cdd:PRK04863 527 QRLRQQQRAERLLAEFCKRLGKN----LDDEDELEQLQEELE-------ARLESLSESVSEARERRMALRQQL------- 588
|
330
....*....|....
gi 1907133161 1282 lDQLNALRREKQKL 1295
Cdd:PRK04863 589 -EQLQARIQRLAAR 601
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1113-1225 |
6.93e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 46.96 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1113 LELAHRELQGRHEQLQAQRANVEAQEVALLAE---RERLMQDGHRQRGLEEELRRLQNEHERAQMLLAE--VSRErgELQ 1187
Cdd:COG1566 74 ARLDPTDLQAALAQAEAQLAAAEAQLARLEAElgaEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKgaVSQQ--ELD 151
|
90 100 110
....*....|....*....|....*....|....*...
gi 1907133161 1188 GERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSA 1225
Cdd:COG1566 152 EARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQA 189
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
260-418 |
7.95e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 7.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 260 LALQLTNAKAQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALRERAGRLPRLQEE 339
Cdd:COG3206 210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPN 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 340 ---LRRCREKLQAAEVFKGQLEEERVLS-----EALEASKVLLEEQLEVARERSARLHETQRENLLLRTRLGEAHADLDS 411
Cdd:COG3206 290 hpdVIALRAQIAALRAQLQQEAQRILASleaelEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
|
....*..
gi 1907133161 412 LRHQLEQ 418
Cdd:COG3206 370 LLQRLEE 376
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
203-384 |
9.56e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 9.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 203 EELEMQLRSLTGMMSRLARERDLGAQRLAELLLEREPAHLLLPEAPANASAEGVSHHLAlQLTNAKAQLRRLRQEVEEKA 282
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIA-ELEAELERLDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 283 EQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALRERAGRLPRLQEELRrcreklqAAEVFKGQLEEERV 362
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL-------LEERFAAALGDAVE 764
|
170 180
....*....|....*....|....
gi 1907133161 363 --LSEALEASKVLLEEQLEVARER 384
Cdd:COG4913 765 reLRENLEERIDALRARLNRAEEE 788
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
261-486 |
1.17e-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: 46.30 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 261 ALQLTNAKAQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEA-LRERAGRLPRLQEE 339
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAeLAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 340 LRRCREKL--QAAEVFK-GQLEEERVL---SEALEASKVL--LEEQLEVARERSARLHETQRENLLLRTRLGEAHADLDS 411
Cdd:COG4942 99 LEAQKEELaeLLRALYRlGRQPPLALLlspEDFLDAVRRLqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907133161 412 LRHQLEQLVEENVELELELQRSLEpppgspgeaslpgaapSLQDEVREAEAgRLRAVERENRELRGQLQMLQAQL 486
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLA----------------RLEKELAELAA-ELAELQQEAEELEALIARLEAEA 236
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
731-1225 |
1.22e-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: 46.76 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 731 EQALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEALCLSEELAQARRTEAEAHqeaeaqareqaRLREAVDTASLELEA 810
Cdd:pfam12128 421 ESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIE-----------RAREEQEAANAEVER 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 811 ASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQA--------LESQVRCHLEEAEREHAEKQALREELEKAV 882
Cdd:pfam12128 490 LQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPqagtllhfLRKEAPDWEQSIGKVISPELLHRTDLDPEV 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 883 LRGQELGDR-LEHLQEELEQAalerqkflqeqenQHQRYRHLEQRLEAELQAAstskEEALMELKARALQLEEELIQLRQ 961
Cdd:pfam12128 570 WDGSVGGELnLYGVKLDLKRI-------------DVPEWAASEEELRERLDKA----EEALQSAREKQAAAEEQLVQANG 632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 962 yPVDLA----TGARAGPRTVETQNGRLIEVERN-----NATLVAEKAALQGQLQHLEGQLGSLqGRAQELLLQSQRAQEH 1032
Cdd:pfam12128 633 -ELEKAsreeTFARTALKNARLDLRRLFDEKQSekdkkNKALAERKDSANERLNSLEAQLKQL-DKKHQAWLEEQKEQKR 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1033 SSRLQAEKSMMEMQGqELHRKLGVLEEEVRAAR-RAQEETRGQQQALLRDHEAL---VQLQRRQETELEGLLVRHRDLKA 1108
Cdd:pfam12128 711 EARTEKQAYWQVVEG-ALDAQLALLKAAIAARRsGAKAELKALETWYKRDLASLgvdPDVIAKLKREIRTLERKIERIAV 789
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1109 NMRALELAHRELQGRHEQ----LQAQRANVEAQEVALLAERERLMQDGHRQRgleEELRRLQNEHERAQMLLAEvsrerg 1184
Cdd:pfam12128 790 RRQEVLRYFDWYQETWLQrrprLATQLSNIERAISELQQQLARLIADTKLRR---AKLEMERKASEKQQVRLSE------ 860
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1185 ELQGERGELRsRLARLEL----ERAQLEI-----QSQQLRESNQQLDLSA 1225
Cdd:pfam12128 861 NLRGLRCEMS-KLATLKEdansEQAQGSIgerlaQLEDLKLKRDYLSESV 909
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
904-1225 |
1.37e-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: 46.66 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 904 LERQKFLQEQENQHQRYRHLEQRLEAElqaastsKEEALMELKARALQLEEELIQL----RQYPVDLATGARAGPRTVET 979
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQE-------KEEKAREVERRRKLEEAEKARQaemdRQAAIYAEQERMAMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 980 QNGRLIEVERNNATLVAEKAALQ-GQLQHLEgqlgslqgraqELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLE 1058
Cdd:pfam17380 351 ERIRQEERKRELERIRQEEIAMEiSRMRELE-----------RLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1059 EEVRAARRAQEETRGQQ-QALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQ 1137
Cdd:pfam17380 420 VEMEQIRAEQEEARQREvRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1138 EV-----ALLAER------ERLMQDghRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERaq 1206
Cdd:pfam17380 500 ELeerkqAMIEEErkrkllEKEMEE--RQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERER-- 575
|
330
....*....|....*....
gi 1907133161 1207 lEIQSQQLRESNQQLDLSA 1225
Cdd:pfam17380 576 -EMMRQIVESEKARAEYEA 593
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
742-1291 |
1.49e-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: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 742 RREVAGLEVKLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELEAASREREALAEA 821
Cdd:pfam05557 26 KRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 822 LAAAGRERRqwerdgpRLRAQVEAAEQQVQALESqvrchleeaerehaEKQALREELEKAVLRGQELGDRLEHLQEEleq 901
Cdd:pfam05557 106 ISCLKNELS-------ELRRQIQRAELELQSTNS--------------ELEELQERLDLLKAKASEAEQLRQNLEKQ--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 902 aalerQKFLQEQEnqhQRYRHLEQRLeaELQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGARAGPRTVETQN 981
Cdd:pfam05557 162 -----QSSLAEAE---QRIKELEFEI--QSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 982 GRLIEVERNNATLvAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSR----------LQAEKSMMEMQGQELH 1051
Cdd:pfam05557 232 DLKRKLEREEKYR-EEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRieqlqqreivLKEENSSLTSSARQLE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1052 RKLGVLEEEVRAARRAQEEtrgqQQALLRDHEALVQ-LQRR-----QETELEGLLVRHRDLKANM----RALELAHRELQ 1121
Cdd:pfam05557 311 KARRELEQELAQYLKKIED----LNKKLKRHKALVRrLQRRvllltKERDGYRAILESYDKELTMsnysPQLLERIEEAE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1122 GRHEQLQAQRANVEAQEVALLAErerlmQDGHRQRG--LEEEL--RRLQNEHERAQMLLAEVS---RERGELQGERGELR 1194
Cdd:pfam05557 387 DMTQKMQAHNEEMEAQLSVAEEE-----LGGYKQQAqtLERELqaLRQQESLADPSYSKEEVDslrRKLETLELERQRLR 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1195 SRLARLELERAQLEIQsqqlresnQQLDLSACR-LTTQCELLTQLRSAQEEENRQLLAEVQALSRENReLLERSLESRDH 1273
Cdd:pfam05557 462 EQKNELEMELERRCLQ--------GDYDPKKTKvLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLK-KLEDDLEQVLR 532
|
570
....*....|....*....
gi 1907133161 1274 LHREQREYLDQ-LNALRRE 1291
Cdd:pfam05557 533 LPETTSTMNFKeVLDLRKE 551
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
866-1283 |
1.50e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 866 REHAEKQALREELEKAVLrGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEA-LME 944
Cdd:COG4913 587 GTRHEKDDRRRIRSRYVL-GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdVAS 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 945 LKARALQLEEELIQLRQYPVDLATgaragprtvetqngrlievernnatlvaekaalqgqlqhLEGQLGSLQGRAQELLL 1024
Cdd:COG4913 666 AEREIAELEAELERLDASSDDLAA---------------------------------------LEEQLEELEAELEELEE 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1025 QSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRgQQQALLRDHEAlvQLQRRQETELEGLlvrHR 1104
Cdd:COG4913 707 ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER-FAAALGDAVER--ELRENLEERIDAL---RA 780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1105 DLKANMRALELAHRELQGR-HEQLQAQRANVEAQEvALLAERERLMQDG-HRqrgLEEELRRLQNEHERAQM--LLAEVS 1180
Cdd:COG4913 781 RLNRAEEELERAMRAFNREwPAETADLDADLESLP-EYLALLDRLEEDGlPE---YEERFKELLNENSIEFVadLLSKLR 856
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1181 RERGELQGERGELRSRLARLEL---ERAQLEIQSQQLRESNqqldlsacrlttqcELLTQLRSAQeeENRQLLAEVQALS 1257
Cdd:COG4913 857 RAIREIKERIDPLNDSLKRIPFgpgRYLRLEARPRPDPEVR--------------EFRQELRAVT--SGASLFDEELSEA 920
|
410 420 430
....*....|....*....|....*....|
gi 1907133161 1258 RENR--ELLERsLESRDHLH--REQREYLD 1283
Cdd:COG4913 921 RFAAlkRLIER-LRSEEEESdrRWRARVLD 949
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
133-475 |
1.57e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 133 EEAVDELESILRLLLGASVQCEHRELFIRHIRGLSLDVQSELAGAIQEVTQ--PGAGVVLALAGPESGELVAEELEMQLR 210
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEaaARLLLLLEAEADYEGFLEGVKAALLLA 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 211 SLTGMMSRLARERDLGAQRLAELLLEREPAHLLLPEAPANASAEGVSHHLALQLtnAKAQLRRLRQEVEEKAEQLLDSQA 290
Cdd:COG1196 518 GLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA--GRATFLPLDKIRARAALAAALARG 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 291 EVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALRERAGRLPRLQEELRRcREKLQAAEVFKGQLEEERVLSEALEAS 370
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLR-EVTLEGEGGSAGGSLTGGSRRELLAAL 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 371 KVLLEEQLEVARERSARLHETQRENLLLRTRLGEAHADLDSLRHQLEQLVEENVELELELQRSLEPPPGSPGEASLPGAA 450
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALE 754
|
330 340
....*....|....*....|....*
gi 1907133161 451 PSLQDEVREAEAGRLRAVERENREL 475
Cdd:COG1196 755 ELPEPPDLEELERELERLEREIEAL 779
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
723-985 |
1.61e-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: 45.91 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 723 TLVSAIPEEQALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLREAVD 802
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 803 TASLELEAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAV 882
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 883 LRGQELGDRLEHLQEELEQAALERQKflqeqenqhqryrhleqrLEAELQAASTSKEEALMELKARALQLEEELIQLRQY 962
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQK------------------LLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
250 260
....*....|....*....|...
gi 1907133161 963 PVDLATGARAGPrtVETQNGRLI 985
Cdd:COG4942 236 AAAAAERTPAAG--FAALKGKLP 256
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
975-1291 |
2.12e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 975 RTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMmemqgQELHRKL 1054
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAEL-----AELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1055 GVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRR----QETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQ 1130
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1131 RANVEAQEVALlAERERLMQDGHRQRGL----------EEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARL 1200
Cdd:COG4717 229 LEQLENELEAA-ALEERLKEARLLLLIAaallallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1201 ELERAQLEIQSQQLRESNQQLDLSAC-----------RLTTQCELLTQLRSAQEE--------ENRQLLAEVQALSREnr 1261
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDlspeellelldRIEELQELLREAEELEEElqleeleqEIAALLAEAGVEDEE-- 385
|
330 340 350
....*....|....*....|....*....|
gi 1907133161 1262 ellerSLESRDHLHREQREYLDQLNALRRE 1291
Cdd:COG4717 386 -----ELRAALEQAEEYQELKEELEELEEQ 410
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
264-499 |
2.14e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 264 LTNAKAQLRRLRQEVEEKaeqlldsqaEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALRERAgrlprlQEELRRC 343
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEK---------EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA------DEVLEEH 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 344 REKLQAAEVFKGQLEEERVLSEALEASKVLLEEQLEVARERSARLhETQRENLLLRTRLGEAHA------------DLDS 411
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEEL-EEERDDLLAEAGLDDADAeavearreeledRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 412 LRHQLEQLVEENVELELELQRSLEPPPGSPGEAS-LPGAAPSLQDEVREAEA------GRLRAVERENRELRGQLQMLQA 484
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEeLREEAAELESELEEAREavedrrEEIEELEEEIEELRERFGDAPV 405
|
250
....*....|....*
gi 1907133161 485 QLGSQHPLLEEQREN 499
Cdd:PRK02224 406 DLGNAEDFLEELREE 420
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
202-396 |
2.21e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 202 AEELEMQLRSLTGMMSRLARERDLGAQRLAELLLEREPAH----LLLPEAPANASAEGVSHHlalQLTNAKAQLRRLRQE 277
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARieevMKLYEEEKKMKAEEAKKA---EEAKIKAEELKKAEE 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 278 VEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKR--------AELYREEAEALRERAGRLPRLQEELRRCRE--KL 347
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKkaeedkkkAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkKK 1710
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907133161 348 QAAEVFKGQ--LEEERVLSEALEASKVLLEEQLEVARErsARLHETQRENL 396
Cdd:PTZ00121 1711 EAEEKKKAEelKKAEEENKIKAEEAKKEAEEDKKKAEE--AKKDEEEKKKI 1759
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
729-1300 |
2.24e-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: 46.10 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 729 PEEQALRDEVAQLRREVAGLEvklqaqaqRLEARSAEALCLSEELAQArrtEAEAHQEAEAQAREQARLREAVDTASLEL 808
Cdd:COG3096 505 RSQQALAQRLQQLRAQLAELE--------QRLRQQQNAERLLEEFCQR---IGQQLDAAEELEELLAELEAQLEELEEQA 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 809 EAASREREALAEALAAAGRERRQWERDGP----------RLRAQVEAA---EQQVQALESQVRCHLEEAEREHAEKQALR 875
Cdd:COG3096 574 AEAVEQRSELRQQLEQLRARIKELAARAPawlaaqdaleRLREQSGEAladSQEVTAAMQQLLEREREATVERDELAARK 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 876 EELEKAVLR-----GQE------LGDRL--EHLQEELEQAALERQKFLQeqenqhQRY----------------RHLEQR 926
Cdd:COG3096 654 QALESQIERlsqpgGAEdprllaLAERLggVLLSEIYDDVTLEDAPYFS------ALYgparhaivvpdlsavkEQLAGL 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 927 ---------LEAELQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAE 997
Cdd:COG3096 728 edcpedlylIEGDPDSFDDSVFDAEELEDAVVVKLSDRQWRYSRFPEVPLFGRAAREKRLEELRAERDELAEQYAKASFD 807
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 998 KAALQGQLQHLEGQLGS----------------LQGRAQEL--LLQSQRAQEHSSRLQAEKSMmemQGQELHRKL----G 1055
Cdd:COG3096 808 VQKLQRLHQAFSQFVGGhlavafapdpeaelaaLRQRRSELerELAQHRAQEQQLRQQLDQLK---EQLQLLNKLlpqaN 884
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1056 VLEEEVRAARRaqEETRGQQQALLRDhEALVQLQRRQETELEGLLvrhrdlkANMRALELAHRELQGRHEQLQAQRANVE 1135
Cdd:COG3096 885 LLADETLADRL--EELREELDAAQEA-QAFIQQHGKALAQLEPLV-------AVLQSDPEQFEQLQADYLQAKEQQRRLK 954
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1136 AQEVALlaerERLMQdghrqrgleeelRRLQNEHERAQMLLAEVSrergelqgergELRSRLarleleRAQLEIQSQQLR 1215
Cdd:COG3096 955 QQIFAL----SEVVQ------------RRPHFSYEDAVGLLGENS-----------DLNEKL------RARLEQAEEARR 1001
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1216 ESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLA---EVQALS-RENRELLERSLESRDHLH------REQREYLD-Q 1284
Cdd:COG3096 1002 EAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQEleqELEELGvQADAEAEERARIRRDELHeelsqnRSRRSQLEkQ 1081
|
650
....*....|....*.
gi 1907133161 1285 LNALRREKQKLVEKIM 1300
Cdd:COG3096 1082 LTRCEAEMDSLQKRLR 1097
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
187-498 |
2.38e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 187 GVVLALAGPESGELVAEELEMQLRSLTGMMSRLARERDLGAQRLAEL--------LLEREPAHLLLPEAPANASAEGVSH 258
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELsdasrkigEIEKEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 259 HL-ALQ--LTNAKAQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAeALRERAGRLPR 335
Cdd:TIGR02169 745 DLsSLEqeIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEA-RLREIEQKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 336 LQEELRRCREKLQAAEVFKGQLEEERV-LSEALEASKVLLEEQLEVARERSARLHE---------TQRENLL-----LRT 400
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRIDLKEQIKsIEKEIENLNGKKEELEEELEELEAALRDlesrlgdlkKERDELEaqlreLER 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 401 RLGEAHADLDSLRHQLEQ-------LVEENVELELELQRSLEPPPGSPGEASLPGAAPSLQDEVREAEAGRLRAVERENR 473
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSElkakleaLEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEE 983
|
330 340
....*....|....*....|....*
gi 1907133161 474 ELRGQLqmlqaQLGSQHPLLEEQRE 498
Cdd:TIGR02169 984 VLKRLD-----ELKEKRAKLEEERK 1003
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
730-1099 |
2.40e-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: 46.10 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 730 EEQALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEALCLSE---ELAQARRTEAEAHQEAEAQAREQ---ARLREAVDT 803
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSAresDLEQDYQAASDHLNLVQTALRQQekiERYQEDLEE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 804 ASLELEAASREREALAEALAAAGRERRQWERDGPRLRAQVE--------------AAEQQVQALE-SQVRCHLEEAEREH 868
Cdd:COG3096 359 LTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqqaldvqqtraiQYQQAVQALEkARALCGLPDLTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 869 AEkqalrEELEKAVLRGQELGDRLEHLQEELEQAALERQKF----------------------LQEQENQHQRYRHLEQR 926
Cdd:COG3096 439 AE-----DYLAAFRAKEQQATEEVLELEQKLSVADAARRQFekayelvckiageversqawqtARELLRRYRSQQALAQR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 927 LEAelQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGAragPRTVETQNGRLIEVERNNATLVAEKAALQGQLQ 1006
Cdd:COG3096 514 LQQ--LRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEEL---EELLAELEAQLEELEEQAAEAVEQRSELRQQLE 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1007 HLEGQLGSLQGRAQELLlqsqRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALV 1086
Cdd:COG3096 589 QLRARIKELAARAPAWL----AAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLS 664
|
410
....*....|...
gi 1907133161 1087 QLQRRQETELEGL 1099
Cdd:COG3096 665 QPGGAEDPRLLAL 677
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
983-1291 |
2.91e-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: 45.71 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 983 RLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEksmmeMQGQElhrKLGVLEEEVR 1062
Cdd:COG3096 286 RALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTA-----LRQQE---KIERYQEDLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1063 AARRAQEEtrgQQQALLRDHEALVQLQ-RRQETELEgllvrHRDLKANMRALELAHRELQGRHEQL-QAQRANVEAQEVA 1140
Cdd:COG3096 358 ELTERLEE---QEEVVEEAAEQLAEAEaRLEAAEEE-----VDSLKSQLADYQQALDVQQTRAIQYqQAVQALEKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1141 LLAE-------------RERLMQDGHRQRGLEEELRRLQ---NEHERAQMLL----AEVSRERG-----ELQGERGELRS 1195
Cdd:COG3096 430 GLPDltpenaedylaafRAKEQQATEEVLELEQKLSVADaarRQFEKAYELVckiaGEVERSQAwqtarELLRRYRSQQA 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1196 RLARLELERAQLEIQSQQLRESNQqldlsACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLH 1275
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLRQQQN-----AERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELR 584
|
330
....*....|....*.
gi 1907133161 1276 REqreyLDQLNALRRE 1291
Cdd:COG3096 585 QQ----LEQLRARIKE 596
|
|
| MASE1 |
COG3447 |
Integral membrane sensor domain MASE1 [Signal transduction mechanisms]; |
827-1170 |
2.91e-04 |
|
Integral membrane sensor domain MASE1 [Signal transduction mechanisms];
Pssm-ID: 442670 [Multi-domain] Cd Length: 637 Bit Score: 45.57 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 827 RERRQWERDgpRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQAALER 906
Cdd:COG3447 291 AERRRQRLR--ERELALRAALELLALGLLLAALDDALLLLNARGLLLLALSLAALLLLRLALLLLLLALDALLLLLADDD 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 907 QKFLQEQENQHQRYRHLEQRLEAELQ-AASTSKEEALMELKARALQLEEELIQLRQYPVDLATGARAGPRTVETQNGRLI 985
Cdd:COG3447 369 RGELRGDLLRRRGATRLGAVVARLLRrSGGRGEEVVVLLVIAQVEEALELALRERREERLLERLALALELLAITAALLAA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 986 EVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQ---RAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVR 1062
Cdd:COG3447 449 ALLLALADLLLLLLAEAAQLLARALLLGLDRLLADAALAALAalaDLLGALLSAGLRRRGGRRLGARLIRSLLSRVLAEL 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1063 AARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAH-RELQGRHEQLQAQRANVEAQEVAL 1141
Cdd:COG3447 529 GAVELLLALIADLTEVALGAEALERLLERLLLALLGLGLAVAALLATLGLLLALLaALALSGAAALLALGAALLLAAAIL 608
|
330 340
....*....|....*....|....*....
gi 1907133161 1142 LAERERLMQDGHRQRGLEEELRRLQNEHE 1170
Cdd:COG3447 609 GLAAALLALLRLLGERARLLETRRLVGAL 637
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1147-1308 |
3.05e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1147 RLMQDGHRQRGLEEELRRLQNEheraqmlLAEVSRERGELQGERGELRSRLARLELERAQLEiqsQQLRESNQQL----- 1221
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDE-------LAALEARLEAAKTELEDLEKEIKRLELEIEEVE---ARIKKYEEQLgnvrn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1222 --DLSAcrLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKI 1299
Cdd:COG1579 88 nkEYEA--LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
....*....
gi 1907133161 1300 MDQYRVLEP 1308
Cdd:COG1579 166 EELAAKIPP 174
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
733-1228 |
3.18e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 45.62 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 733 ALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEAL-CLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELEAA 811
Cdd:COG3899 746 ALLLELAEALYLAGRFEEAEALLERALAARALAALaALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGD 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 812 SREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDR 891
Cdd:COG3899 826 RRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALA 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 892 LEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGAR 971
Cdd:COG3899 906 AAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAA 985
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 972 AGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELH 1051
Cdd:COG3899 986 AAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAA 1065
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1052 RKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQR 1131
Cdd:COG3899 1066 AALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALA 1145
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1132 ANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQS 1211
Cdd:COG3899 1146 LAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLL 1225
|
490
....*....|....*..
gi 1907133161 1212 QQLRESNQQLDLSACRL 1228
Cdd:COG3899 1226 LLLAALALAAALLALRL 1242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
263-467 |
3.59e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 263 QLTNAKAQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQ-AKRAELYREEAEALRERAGRLPRL----- 336
Cdd:COG3883 31 ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEiEERREELGERARALYRSGGSVSYLdvllg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 337 ----QEELRRCREKLQAAEVFKGQLEEERVLSEALEASKVLLEEQLEVARERSARLHETQREnllLRTRLGEAHADLDSL 412
Cdd:COG3883 111 sesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE---LEAQQAEQEALLAQL 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907133161 413 RHQLEQLVEENVELELELQRSLEPPPGSPGEASLPGAAPSLQDEVREAEAGRLRA 467
Cdd:COG3883 188 SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1004-1148 |
3.60e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1004 QLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQ-------- 1075
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnke 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907133161 1076 -QALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQR----ANVEAQEVALLAERERL 1148
Cdd:COG1579 91 yEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELdeelAELEAELEELEAEREEL 168
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
263-445 |
3.76e-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: 44.75 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 263 QLTNAKAQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALsaQAKRAELYREEAEALRE--RAGRLPRLQ--- 337
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL--RAELEAQKEELAELLRAlyRLGRQPPLAlll 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 338 ------EELRR-------CREKLQAAEVFKGQLEEERVLSEALEASKVLLEEQLEVARERSARL--HETQRENLL--LRT 400
Cdd:COG4942 127 spedflDAVRRlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALeaLKAERQKLLarLEK 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907133161 401 RLGEAHADLDSLRHQLEQLVEENVELELELQRSLEPPPGSPGEAS 445
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
268-418 |
3.87e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 268 KAQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALRERAGRLPRLQEELRRCREKL 347
Cdd:PRK03918 230 VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDEL 309
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907133161 348 QAAEVFKGQLEEERvlsEALEASKVLLEEQLEVARERSARLHETQRENLLLRTRLgEAHADLDSLRHQLEQ 418
Cdd:PRK03918 310 REIEKRLSRLEEEI---NGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELER 376
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
238-378 |
3.91e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 45.33 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 238 EPAHLLLPEAPANASAEgvshhlalqltnAKAQLRRLRQEVEEKAEqlldsqaEVQGLEAEIRRLRQETQALSAQAKRAE 317
Cdd:PRK11448 130 KPGPFVPPEDPENLLHA------------LQQEVLTLKQQLELQAR-------EKAQSQALAEAQQQELVALEGLAAELE 190
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907133161 318 LYREEAEA----LRERAGRLPRlQEELRRCREKLQAAEVFKgqleeervLSEALeaSKVLLEEQL 378
Cdd:PRK11448 191 EKQQELEAqleqLQEKAAETSQ-ERKQKRKEITDQAAKRLE--------LSEEE--TRILIDQQL 244
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
870-1077 |
3.98e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 870 EKQALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLeAELQAASTSKEEALMELkARA 949
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI-AEAEAEIEERREELGER-ARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 950 LQLEE------ELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELL 1023
Cdd:COG3883 95 LYRSGgsvsylDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907133161 1024 LQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQA 1077
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
252-349 |
4.05e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 252 SAEGVSHHLALQLTNAKAQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALRERAG 331
Cdd:COG2433 396 EAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIE 475
|
90
....*....|....*...
gi 1907133161 332 RLPRLQEELRRCREKLQA 349
Cdd:COG2433 476 RLERELEEERERIEELKR 493
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
838-1156 |
4.76e-04 |
|
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: 44.29 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 838 RLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELgdRLEHLQEELEQAALERQKFLQEQENQH 917
Cdd:pfam19220 59 QERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEEL--RIELRDKTAQAEALERQLAAETEQNRA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 918 qryrhleqrLEAELQAASTSKEEAlmelKARALQLEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAE 997
Cdd:pfam19220 137 ---------LEEENKALREEAQAA----EKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 998 KAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEhssRLQAEKSMMEMQGQELHRKLGVLE--------------EEVRA 1063
Cdd:pfam19220 204 LDATRARLRALEGQLAAEQAERERAEAQLEEAVE---AHRAERASLRMKLEALTARAAATEqllaearnqlrdrdEAIRA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1064 ARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRH-----------RDLKANMRALELAHRELQGRHEQLQAQRA 1132
Cdd:pfam19220 281 AERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARaeleeraemltKALAAKDAALERAEERIASLSDRIAELTK 360
|
330 340
....*....|....*....|....
gi 1907133161 1133 NVEAQEVALLAERERLMQDGHRQR 1156
Cdd:pfam19220 361 RFEVERAALEQANRRLKEELQRER 384
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
740-1263 |
5.52e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 740 QLRREVAGLEVKLQAQAQRLEARSAEALCLSEELAQarrteaeahqeaeaQAREQARLREAVDTaslELEAASREREALA 819
Cdd:pfam01576 458 KLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQ--------------LEDERNSLQEQLEE---EEEAKRNVERQLS 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 820 EALAAAGRERRQWERDGprlrAQVEAAEQQVQALESQvrchLEEAEREHAEKQALREELEKAVLR-GQELGDRLEHLQEE 898
Cdd:pfam01576 521 TLQAQLSDMKKKLEEDA----GTLEALEEGKKRLQRE----LEALTQQLEEKAAAYDKLEKTKNRlQQELDDLLVDLDHQ 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 899 ------LEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAAST---SKEEALMELKARALQLEEELIQLRQYPVDLATG 969
Cdd:pfam01576 593 rqlvsnLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETralSLARALEEALEAKEELERTNKQLRAEMEDLVSS 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 970 ARAGPRTVEtqngrliEVERNNATLVAEKAALQGQLQHLEGQLGSLQgraqelllqsqraqehSSRLQAEKSMMEMQGQe 1049
Cdd:pfam01576 673 KDDVGKNVH-------ELERSKRALEQQVEEMKTQLEELEDELQATE----------------DAKLRLEVNMQALKAQ- 728
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1050 lhrklgvLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEG----LLVRHRDLKANMRALELAHRELQGRHE 1125
Cdd:pfam01576 729 -------FERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAakkkLELDLKELEAQIDAANKGREEAVKQLK 801
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1126 QLQAQRANVEAQEVALLAERERLM----QDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLE 1201
Cdd:pfam01576 802 KLQAQMKDLQRELEEARASRDEILaqskESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQ 881
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907133161 1202 LERAQLEIQSQQLRESNQQLDLSA-------CRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENREL 1263
Cdd:pfam01576 882 DEKRRLEARIAQLEEELEEEQSNTellndrlRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKEL 950
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
202-351 |
6.11e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 202 AEELEMQLRSLTGMMSRLARERDLGAQRLAELLLEREPAHLLLPEAPANAsaegvshhlalQLTNAKAQLRRLRQEVEEK 281
Cdd:COG3206 214 AKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP-----------VIQQLRAQLAELEAELAEL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 282 AEQLLDSQAEVQGLEAEIRRLRQ-------------ETQALSAQAKRAELyREEAEALRERAGRLPRLQEELRRCREKLQ 348
Cdd:COG3206 283 SARYTPNHPDVIALRAQIAALRAqlqqeaqrilaslEAELEALQAREASL-QAQLAQLEARLAELPELEAELRRLEREVE 361
|
...
gi 1907133161 349 AAE 351
Cdd:COG3206 362 VAR 364
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1104-1307 |
6.41e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1104 RDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLMQdghrqrgLEEELRRLQNEHERAQMLLAEVSRER 1183
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ-------LEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1184 GELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSACRLTTQCELLtqlrsaqEEENRQLLAEVQALSRENREL 1263
Cdd:COG4372 104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL-------EEQLESLQEELAALEQELQAL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907133161 1264 LERSLESR-DHLHREQREYLDQLNALRREKQKLVEKIMDQYRVLE 1307
Cdd:COG4372 177 SEAEAEQAlDELLKEANRNAEKEEELAEAEKLIESLPRELAEELL 221
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
828-959 |
6.64e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.31 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 828 ERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLqEELEQAALERQ 907
Cdd:PRK12705 33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKL-DNLENQLEERE 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1907133161 908 KFLQEQENQhqrYRHLEQRLEAELQAASTSKEEALMELKARALQ--LEEELIQL 959
Cdd:PRK12705 112 KALSARELE---LEELEKQLDNELYRVAGLTPEQARKLLLKLLDaeLEEEKAQR 162
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
896-1155 |
7.36e-04 |
|
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: 44.25 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 896 QEELEQAALERQkfLQEQENQHQRYRHLEQRLEAELQAASTSKEEALMELKARALQLEEELIQLRQyPVDLATGARAGPR 975
Cdd:pfam05667 223 EEEWNSQGLASR--LTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSG-SSTTDTGLTKGSR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 976 TVETQNGRLIEVERNNATLVAEKAALQGQLQ-HLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKL 1054
Cdd:pfam05667 300 FTHTEKLQFTNEAPAATSSPPTKVETEEELQqQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQN 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1055 GVLEEEVRAARRAQE---ETRGQQQALLRDHEA----LVQLQRRQETELEGLLVRHRDLK--ANMRALELAHR--ELQGR 1123
Cdd:pfam05667 380 EELEKQYKVKKKTLDllpDAEENIAKLQALVDAsaqrLVELAGQWEKHRVPLIEEYRALKeaKSNKEDESQRKleEIKEL 459
|
250 260 270
....*....|....*....|....*....|....*..
gi 1907133161 1124 HEQLQ-----AQRAnvEAQEVALLAERERLMQDGHRQ 1155
Cdd:pfam05667 460 REKIKevaeeAKQK--EELYKQLVAEYERLPKDVSRS 494
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1142-1288 |
8.32e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1142 LAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQsqqlresnqql 1221
Cdd:COG4913 237 LERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELA----------- 305
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907133161 1222 dlsacRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNAL 1288
Cdd:COG4913 306 -----RLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEAL 367
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
827-1172 |
9.70e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 9.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 827 RERRQWERDGPRLRAQVEAAEQQVQALESQVrchleeaerehaekQALREEL-EKAVLRGQELGDRLEHLQEELEQaALE 905
Cdd:PRK04863 844 RRRVELERALADHESQEQQQRSQLEQAKEGL--------------SALNRLLpRLNLLADETLADRVEEIREQLDE-AEE 908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 906 RQKFLQeqenQHQRYRHLEQRLEAELQaastSKEEALMELKARALQLEEELIQLRQypvdlatGARAGPRTVETQNGRLI 985
Cdd:PRK04863 909 AKRFVQ----QHGNALAQLEPIVSVLQ----SDPEQFEQLKQDYQQAQQTQRDAKQ-------QAFALTEVVQRRAHFSY 973
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 986 EverNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQ-RAQEHSSRLQAEKSMMEMQGQELHRKLGVLEE-EVRA 1063
Cdd:PRK04863 974 E---DAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQaQLAQYNQVLASLKSSYDAKRQMLQELKQELQDlGVPA 1050
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1064 ARRAQEETRGQQQALlrdHEALVQlQRRQETELEGLLVRhrdLKANMRALELAHRELQgrhEQLQAQRANVEAQEVALLA 1143
Cdd:PRK04863 1051 DSGAEERARARRDEL---HARLSA-NRSRRNQLEKQLTF---CEAEMDNLTKKLRKLE---RDYHEMREQVVNAKAGWCA 1120
|
330 340
....*....|....*....|....*....
gi 1907133161 1144 ERERLMQDGHRQRGLEEELRRLQNEHERA 1172
Cdd:PRK04863 1121 VLRLVKDNGVERRLHRRELAYLSADELRS 1149
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
94-181 |
9.73e-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: 41.37 E-value: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 94 RMWNLCHLWGRLRDFYQEL--QLLILSPPPDLQTMG--CDPFseeavdELESILRLLLGASVQCEHRELFIRHIRGLSLD 169
Cdd:cd22225 61 KMSNLKKILQGIVDYYHEFldQQISEFLLPDLNRIAehSDPV------ELGRLLQLILGCAVNCEKKQEHIQNIMTLEES 134
|
90
....*....|..
gi 1907133161 170 VQSELAGAIQEV 181
Cdd:cd22225 135 VQHVVMTAIQEL 146
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
619-1036 |
1.01e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 619 EVQELLGETGSREAPQGELVH---------KAQVLKQESPKCRPRSAELTLREPLKDQKALDRELELSKQ-----QKETG 684
Cdd:TIGR00618 408 EQATIDTRTSAFRDLQGQLAHakkqqelqqRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTkeqihLQETR 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 685 RHEQRPKGLESKLGPQKP--QQTSEGVPDAWSREEPTPGETLVSAIPEE---------------QALRDEVAQLRREVAG 747
Cdd:TIGR00618 488 KKAVVLARLLELQEEPCPlcGSCIHPNPARQDIDNPGPLTRRMQRGEQTyaqletseedvyhqlTSERKQRASLKEQMQE 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 748 LEVKLQAQAQRLEARSAEA----------LCLSEELAQARRTEAEAHQEAEAQAREQARLRE--AVDTASLELEAASRER 815
Cdd:TIGR00618 568 IQQSFSILTQCDNRSKEDIpnlqnitvrlQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDvrLHLQQCSQELALKLTA 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 816 EALAEALAAAGRERRQWER---DGPRLRAQVEAAEQQVQALESQVRCHLE----------EAEREHAEKQALREELEKAV 882
Cdd:TIGR00618 648 LHALQLTLTQERVREHALSirvLPKELLASRQLALQKMQSEKEQLTYWKEmlaqcqtllrELETHIEEYDREFNEIENAS 727
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 883 L-RGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYrhlEQRLEAELQAAsTSKEEALMELKARALQLEEELIQLRQ 961
Cdd:TIGR00618 728 SsLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNN---NEEVTAALQTG-AELSHLAAEIQFFNRLREEDTHLLKT 803
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907133161 962 YPVDLATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRL 1036
Cdd:TIGR00618 804 LEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
269-418 |
1.07e-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: 42.60 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 269 AQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALRERA-GRLPRL--QEELRRCRE 345
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeEQLGNVrnNKEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907133161 346 KLQAAEVFKGQLEEE-RVLSEALEASKVLLEEQLEVARERSARLHETQREnllLRTRLGEAHADLDSLRHQLEQ 418
Cdd:COG1579 97 EIESLKRRISDLEDEiLELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREE 167
|
|
| FtsB |
COG2919 |
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning]; |
270-319 |
1.08e-03 |
|
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442163 [Multi-domain] Cd Length: 96 Bit Score: 39.86 E-value: 1.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1907133161 270 QLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAkRAELY 319
Cdd:COG2919 30 AYRELRQEIAELEAENAKLKARNAELEAEVADLKDGPDYIEERA-REELG 78
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
731-1166 |
1.13e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 43.36 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 731 EQALRDEVAQLRREVAGlEVKLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELEA 810
Cdd:COG5278 85 RAEIDELLAELRSLTAD-NPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 811 ASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGD 890
Cdd:COG5278 164 ALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 891 RLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGA 970
Cdd:COG5278 244 LLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 971 RAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQEL 1050
Cdd:COG5278 324 ALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1051 HRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQ 1130
Cdd:COG5278 404 AEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAA 483
|
410 420 430
....*....|....*....|....*....|....*.
gi 1907133161 1131 RANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQ 1166
Cdd:COG5278 484 LAEAEAAAALAAAAALSLALALAALLLAAAEAALAA 519
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
273-404 |
1.14e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 273 RLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSaqAKRAELYREEAEALREragRLPRLQEELRRCREKLQAAEV 352
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEAS--FERLAELRDELAELEE---ELEALKARWEAEKELIEEIQE 475
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907133161 353 FKGQLEEERVLSEALEASKVLLEEQLEVARERS---------------------ARLHETQRENLL-LRTRLGE 404
Cdd:COG0542 476 LKEELEQRYGKIPELEKELAELEEELAELAPLLreevteediaevvsrwtgipvGKLLEGEREKLLnLEEELHE 549
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
246-962 |
1.17e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 246 EAPANASAEGVSHHLALQLTNAKAQLRRLrqEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEA 325
Cdd:pfam02463 298 LKSELLKLERRKVDDEEKLKESEKEKKKA--EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 326 LRERAGRLPRLQEELRRCREKLQAaevfkgQLEEERVLSEALEASKVLLEEQLEVARERSARLHETQRENLLLRTRLGEA 405
Cdd:pfam02463 376 LAKKKLESERLSSAAKLKEEELEL------KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEE 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 406 HADLDSLRHQLEQLVEENVELELELQrslepppgspgEASLPGAAPSLQDEVREAEAGRLRAVERENRELRGQLQMLQAQ 485
Cdd:pfam02463 450 KEELEKQELKLLKDELELKKSEDLLK-----------ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKD 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 486 LGSQHPLLEEQRENSRQPPVPNRDPAT----PSALHHSPQSPACQIGGEGSESLDLPSPASYSDITRSPKCSQAPDSHPE 561
Cdd:pfam02463 519 GVGGRIISAHGRLGDLGVAVENYKVAIstavIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLE 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 562 LESPLQMVSQDPQT----SDQALQESDPTVETHQCLEKSGHRVPLQSPIVWDPPQGPEVRIEVQELLGETGSREAPQGEL 637
Cdd:pfam02463 599 IDPILNLAQLDKATleadEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEI 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 638 VHKAQVLKQESPKCRPRSAELTLREPLKDQKALDRELELSKQQKETGRH--EQRPKGLESKLGPQKPQQTSEgVPDAWSR 715
Cdd:pfam02463 679 QELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVqeAQDKINEELKLLKQKIDEEEE-EEEKSRL 757
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 716 EEPTPGETLVSAIPEEQALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEALcLSEELAQARRTEAEAHQEAEAQAREQA 795
Cdd:pfam02463 758 KKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEE-LKEEAELLEEEQLLIEQEEKIKEEELE 836
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 796 RLREAVDTASLELEAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRchlEEAEREHAEKQALR 875
Cdd:pfam02463 837 ELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEK---KELEEESQKLNLLE 913
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 876 EELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALME----------L 945
Cdd:pfam02463 914 EKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEfeekeerynkD 993
|
730
....*....|....*..
gi 1907133161 946 KARALQLEEELIQLRQY 962
Cdd:pfam02463 994 ELEKERLEEEKKKLIRA 1010
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
873-1259 |
1.24e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 43.36 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 873 ALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAA----STSKEEALMELKAR 948
Cdd:pfam15964 318 SVRSSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKELASQqekrAQEKEALRKEMKKE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 949 ALQLEEELIQLRQYPVDLatgaragprtvetqNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQR 1028
Cdd:pfam15964 398 REELGATMLALSQNVAQL--------------EAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQLNQTKM 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1029 AQEHSSRLQAEKSM-----MEMQGQELhRKLGV--------LEEEVRAARRAQEETRGQQQaLLRDHEALVQLQRRQETE 1095
Cdd:pfam15964 464 KKDEAEKEHREYRTktgrqLEIKDQEI-EKLGLelseskqrLEQAQQDAARAREECLKLTE-LLGESEHQLHLTRLEKES 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1096 LEGLLvrHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLMqdghrqRGLEEEL----RRLQNEHER 1171
Cdd:pfam15964 542 IQQSF--SNEAKAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFI------AKLKEECctlaKKLEEITQK 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1172 AQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDlSACRLTTQceLLTQLRSAQeeenRQLLA 1251
Cdd:pfam15964 614 SRSEVEQLSQEKEYLQDRLEKLQKRNEELEEQCVQHGRMHERMKQRLRQLD-KHCQATAQ--QLVQLLSKQ----NQLFK 686
|
....*...
gi 1907133161 1252 EVQALSRE 1259
Cdd:pfam15964 687 ERQNLTEE 694
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1125-1297 |
1.25e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1125 EQLQAQRANVEAQEVALLA--ERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLeL 1202
Cdd:COG3206 182 EQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL-L 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1203 ERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYL 1282
Cdd:COG3206 261 QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLE 340
|
170
....*....|....*
gi 1907133161 1283 DQLNALRREKQKLVE 1297
Cdd:COG3206 341 ARLAELPELEAELRR 355
|
|
| Mating_C |
pfam12737 |
C-terminal domain of homeodomain 1; Mating in fungi is controlled by the loci that determine ... |
467-565 |
1.52e-03 |
|
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: 42.67 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 467 AVERENRELRGQLQMLQAQLgsqhpLLEEQRENSRQP-PVPNRDPATPSALHHSPQSPACQIGGEGsESLDLP---SPAS 542
Cdd:pfam12737 34 AVKDMTPDLKEQLKDEKKRK-----RQAERSMRDALAyPSPERSPASSPERNLSPQVDVCQLTIRQ-NNLNLKrrsSSSS 107
|
90 100
....*....|....*....|...
gi 1907133161 543 YSDITRSPKCSQAPDSHPELESP 565
Cdd:pfam12737 108 DVDSSNAERCHKRPRLDSPSSSS 130
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1031-1302 |
1.59e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.20 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1031 EHSSRLQAEKSMMEMQGQELHRklgvLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLlvrhrdlKANM 1110
Cdd:pfam07111 56 EGSQALSQQAELISRQLQELRR----LEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGL-------RAAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1111 RALELAHRELQ-GRHEQLQA-QRANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRE----RG 1184
Cdd:pfam07111 125 AGAEMVRKNLEeGSQRELEEiQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEaellRK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1185 ELQGERGELRSRLARLE--------------------LERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEE 1244
Cdd:pfam07111 205 QLSKTQEELEAQVTLVEslrkyvgeqvppevhsqtweLERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEE 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907133161 1245 ENRQLLAEVQAL----SRENRELLERSLES----RDHLHREQREYLDQLNALRREKQKLVEKIMDQ 1302
Cdd:pfam07111 285 ELTRKIQPSDSLepefPKKCRSLLNRWREKvfalMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQ 350
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
268-418 |
1.70e-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: 43.19 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 268 KAQLRRLRQEVEEKAEQL----------------LDSQAEVQG--------LEAEIRRLRQETQALSAQAKRAELYREEA 323
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVerrrkleeaekarqaeMDRQAAIYAeqermameRERELERIRQEERKRELERIRQEEIAMEI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 324 EALRERAGRLPRLQEELRRCREKLQAAEVFKGQLEEERVLSEALEASKVLLEEQLEVARERSARLHETQRENLLLRTRLG 403
Cdd:pfam17380 375 SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE 454
|
170
....*....|....*..
gi 1907133161 404 EA--HADLDSLRHQLEQ 418
Cdd:pfam17380 455 EQerQQQVERLRQQEEE 471
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1078-1176 |
1.72e-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: 42.68 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1078 LLRDHEALVQlqrrqetelEGLLVRHRDLKAN-MRALELAHRELQGRHEQLQAQRaNVEAQEVALL----AERERLMQD- 1151
Cdd:COG0172 6 LIRENPEAVK---------EALAKRGFDLDVDeLLELDEERRELQTEVEELRAER-NALSKEIGKAkkkgEEAEALIAEv 75
|
90 100
....*....|....*....|....*...
gi 1907133161 1152 ---GHRQRGLEEELRRLQNEHERAQMLL 1176
Cdd:COG0172 76 kelKEEIKELEEELKELEEELDELLLSI 103
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
827-1222 |
1.78e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.25 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 827 RERRQWERDGPRLRAQVEAAEQQVQALESqvrchleEAEREHAEKQALREELekavlrgQELGDRLE---HLQEELeqaa 903
Cdd:PRK10246 537 KEVKKLGEEGAALRGQLDALTKQLQRDES-------EAQSLRQEEQALTQQW-------QAVCASLNitlQPQDDI---- 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 904 lerQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALME--LKARALQLEEeliQLRQYPVDLATgaragprtvetqn 981
Cdd:PRK10246 599 ---QPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQqqIEQRQQQLLT---ALAGYALTLPQ------------- 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 982 grlievERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELL-LQSQRAQEHSSRLQAEKSMMEmQGQELHRKLGVLEee 1060
Cdd:PRK10246 660 ------EDEEASWLATRQQEAQSWQQRQNELTALQNRIQQLTpLLETLPQSDDLPHSEETVALD-NWRQVHEQCLSLH-- 730
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1061 vraarrAQEETRGQQ--QALLRDHEALVQLqrrqETELEGllVRHRDLKANMRAleLAHRELQGRHEQLQAQRANVEAQE 1138
Cdd:PRK10246 731 ------SQLQTLQQQdvLEAQRLQKAQAQF----DTALQA--SVFDDQQAFLAA--LLDEETLTQLEQLKQNLENQRQQA 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1139 VALLAERERLMQDGHRQR--GLEEELRRLQNEHERAQmlLAEVSRERGELQgerGELRSRLARLELERAQLEIQSQQLRE 1216
Cdd:PRK10246 797 QTLVTQTAQALAQHQQHRpdGLDLTVTVEQIQQELAQ--LAQQLRENTTRQ---GEIRQQLKQDADNRQQQQALMQQIAQ 871
|
....*.
gi 1907133161 1217 SNQQLD 1222
Cdd:PRK10246 872 ATQQVE 877
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
827-1181 |
1.78e-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: 43.02 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 827 RERRQWERDgprlRAQVEAAEQQVQALESQVRCHLeeaerehaekQALREELEKAVLRGQE-LGDRLEHLQEELEQaALE 905
Cdd:COG3096 843 QRRSELERE----LAQHRAQEQQLRQQLDQLKEQL----------QLLNKLLPQANLLADEtLADRLEELREELDA-AQE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 906 RQKFLQeqenQHQRYRHLEQRLEAELQAASTSKEealmELKARALQLEEELIQLRQYPVDLA-TGARAGPRTVETQNGRL 984
Cdd:COG3096 908 AQAFIQ----QHGKALAQLEPLVAVLQSDPEQFE----QLQADYLQAKEQQRRLKQQIFALSeVVQRRPHFSYEDAVGLL 979
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 985 IEvernNATLVaekAALQGQLQHLEGQlgslQGRAQELLLQSQ-RAQEHSSRLQAEKSMMEMQGQELHRKLGVLEE-EVR 1062
Cdd:COG3096 980 GE----NSDLN---EKLRARLEQAEEA----RREAREQLRQAQaQYSQYNQVLASLKSSRDAKQQTLQELEQELEElGVQ 1048
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1063 AARRAQEETRGQQQALlrdHEALVQL-QRRQETElEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRA--------- 1132
Cdd:COG3096 1049 ADAEAEERARIRRDEL---HEELSQNrSRRSQLE-KQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAgwcavlrla 1124
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907133161 1133 ---NVEAQevalLAERERLMQDGHRQRG-LEEELRRLQ-----NEHERAQMLLAEVSR 1181
Cdd:COG3096 1125 rdnDVERR----LHRRELAYLSADELRSmSDKALGALRlavadNEHLRDALRLSEDPR 1178
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
792-1291 |
2.24e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 42.92 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 792 REQARLREAVDTASLELEAASREREALAEALAAAGRERRQWERDG-PRLRAQVEAAEQQVQALESQVRCHLEEAEREHAE 870
Cdd:COG3899 742 EYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGnPPASARAYANLGLLLLGDYEEAYEFGELALALAE 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 871 KQALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALMELKARAL 950
Cdd:COG3899 822 RLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAA 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 951 QLEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQ 1030
Cdd:COG3899 902 AALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAA 981
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1031 EHSSRLQAeksmmemQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANM 1110
Cdd:COG3899 982 AAAAAAAA-------ALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAA 1054
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1111 RALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGER 1190
Cdd:COG3899 1055 AAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAA 1134
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1191 GELRSRLARLELERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLES 1270
Cdd:COG3899 1135 LLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALAL 1214
|
490 500
....*....|....*....|.
gi 1907133161 1271 RDHLHREQREYLDQLNALRRE 1291
Cdd:COG3899 1215 LALEAAALLLLLLLAALALAA 1235
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
272-418 |
2.43e-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: 42.03 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 272 RRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALREragRLPRLQEELRRCREKLQAAE 351
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQA---AVKAAQAQLAQAQIDLARRR 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907133161 352 VF-------KGQLEEERVLSEALEASKVLLEEQLEVARERSARLHETQREnlLLRTRLGEAHADLDSLRHQLEQ 418
Cdd:pfam00529 131 VLapiggisRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQA--EVRSELSGAQLQIAEAEAELKL 202
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
732-937 |
2.61e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 732 QALRDEVAQLRREVAGLEVKLQA--QAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELE 809
Cdd:COG3206 178 EFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 810 AASREREALAEALAAAGRERR------QWERDGP---RLRAQVEAAEQQVQALESQVrchLEEAEREHAEKQALREELEK 880
Cdd:COG3206 258 ELLQSPVIQQLRAQLAELEAElaelsaRYTPNHPdviALRAQIAALRAQLQQEAQRI---LASLEAELEALQAREASLQA 334
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907133161 881 AVlrgQELGDRLEHLQE-ELEQAALERqkflqEQENQHQRYRHLEQRL-EAELQAASTS 937
Cdd:COG3206 335 QL---AQLEARLAELPElEAELRRLER-----EVEVARELYESLLQRLeEARLAEALTV 385
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
839-1019 |
2.69e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.67 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 839 LRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQElgdRLEHLQEELEQAALERQKFLQEQENQHQ 918
Cdd:pfam09787 73 LRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQE---ELRYLEEELRRSKATLQSRIKDREAEIE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 919 RyrhleQRLEAELQAASTSKEEalmELKARALQLEEELIQlRQYPVDlatgaragprtvetqngrlievernnaTLVAEK 998
Cdd:pfam09787 150 K-----LRNQLTSKSQSSSSQS---ELENRLHQLTETLIQ-KQTMLE---------------------------ALSTEK 193
|
170 180
....*....|....*....|.
gi 1907133161 999 AALQGQLQHLEGQLGSLQGRA 1019
Cdd:pfam09787 194 NSLVLQLERMEQQIKELQGEG 214
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
997-1225 |
2.77e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 997 EKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKsmmemqgQELHRKLGVLEEEVRAARRAQEetrgQQQ 1076
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL-------EALQAEIDKLQAEIAEAEAEIE----ERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1077 ALLRDHEALVQLQRRQETELEGLLVRH--RDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLMQdghR 1154
Cdd:COG3883 86 EELGERARALYRSGGSVSYLDVLLGSEsfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA---L 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907133161 1155 QRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSA 1225
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1102-1302 |
2.95e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.98 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1102 RHRDLKANMRALELAHRELQGRHEQLQAQ-----RANVEAQE-VALLAERERLMQDGHRQRGLEEELRRLQNEHERAQML 1175
Cdd:COG0497 166 AWRALKKELEELRADEAERARELDLLRFQleeleAAALQPGEeEELEEERRRLSNAEKLREALQEALEALSGGEGGALDL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1176 LAEVSRERGELQGERGELRSRLARleLERAQLEIQ--SQQLRESNQQLDLSACRLTTQCELLTQLRSAQ-------EEen 1246
Cdd:COG0497 246 LGQALRALERLAEYDPSLAELAER--LESALIELEeaASELRRYLDSLEFDPERLEEVEERLALLRRLArkygvtvEE-- 321
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907133161 1247 rqlLAEVQALSRENRELLERSLESRDHLHRE----QREYLD---QLNALRREK-QKLVEKIMDQ 1302
Cdd:COG0497 322 ---LLAYAEELRAELAELENSDERLEELEAElaeaEAELLEaaeKLSAARKKAaKKLEKAVTAE 382
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
834-1225 |
3.09e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.20 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 834 RDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQAALERQKFLQEQ 913
Cdd:COG5278 131 RAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 914 ENQHQRYRHLEQRLEAELQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATGARAGPRTVETQNGRLIEVERNNAT 993
Cdd:COG5278 211 AELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALE 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 994 LVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRG 1073
Cdd:COG5278 291 LAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1074 QQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRANVEAQEVALLAERERLMQDGH 1153
Cdd:COG5278 371 AALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELA 450
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907133161 1154 RQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQQLRESNQQLDLSA 1225
Cdd:COG5278 451 EAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALA 522
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
263-351 |
3.20e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 263 QLTNAKAQLRRLRQEVEE-KAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAK----RAELYREEAEALRERAGRLPRLQ 337
Cdd:COG0542 412 ELDELERRLEQLEIEKEAlKKEQDEASFERLAELRDELAELEEELEALKARWEaekeLIEEIQELKEELEQRYGKIPELE 491
|
90
....*....|....
gi 1907133161 338 EELRRCREKLQAAE 351
Cdd:COG0542 492 KELAELEEELAELA 505
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1020-1208 |
3.61e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1020 QELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGL 1099
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1100 lvrhrdlkANMRALELAHRELqgrhEQLQAQRANVEAQEVALLAERERlmqdghrqrgLEEELRRLQNEHERAQmllAEV 1179
Cdd:COG1579 86 --------RNNKEYEALQKEI----ESLKRRISDLEDEILELMERIEE----------LEEELAELEAELAELE---AEL 140
|
170 180
....*....|....*....|....*....
gi 1907133161 1180 SRERGELQGERGELRSRLARLELERAQLE 1208
Cdd:COG1579 141 EEKKAELDEELAELEAELEELEAEREELA 169
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1003-1262 |
3.62e-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: 41.59 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1003 GQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQqqalLRDH 1082
Cdd:pfam19220 20 EDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVAR----LAKL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1083 EALVqlqRRQETELEGLLVRHRDLKANMRALE----LAHRELQGRHEQLQAQRANVEAQEvALLAERERLMQDGHRQRGL 1158
Cdd:pfam19220 96 EAAL---REAEAAKEELRIELRDKTAQAEALErqlaAETEQNRALEEENKALREEAQAAE-KALQRAEGELATARERLAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1159 -EEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLEL----ERAQLEIQSQQLRESNQQLDLSACRLTTQCE 1233
Cdd:pfam19220 172 lEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGqlaaEQAERERAEAQLEEAVEAHRAERASLRMKLE 251
|
250 260
....*....|....*....|....*....
gi 1907133161 1234 LLTqlrsAQEEENRQLLAEVQALSRENRE 1262
Cdd:pfam19220 252 ALT----ARAAATEQLLAEARNQLRDRDE 276
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
654-1076 |
3.79e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 654 RSAELTLREPLKDQKALDRELELSKQQKETGRHEQRpkGLESKLGPQKPQQTSEGVPDAWSREEPTPgETLVSAIPEEQA 733
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEELREELE--KLEKLLQLLPLYQELEALEAELAELPERL-EELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 734 LRDEVAQLRREVAGLEVKLQAQAQRLEARSAEALC-LSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELEAAS 812
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATEEELQdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 813 REREALAEA--------------LAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREEL 878
Cdd:COG4717 241 LEERLKEARlllliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 879 EKAVLRGQELGDRLE-HLQEELEQAALERQKFLQEQENQHQRYR--HLEQRLEAELQAASTSKEEALMELKARALQLEEE 955
Cdd:COG4717 321 LEELLAALGLPPDLSpEELLELLDRIEELQELLREAEELEEELQleELEQEIAALLAEAGVEDEEELRAALEQAEEYQEL 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 956 LIQLRQYPVDLAtgARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELllqsqRAQEHSSR 1035
Cdd:COG4717 401 KEELEELEEQLE--ELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQL-----EEDGELAE 473
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1907133161 1036 LQAEKSMMEMQGQELHRKLGVLEEEVRAARRAQEETRGQQQ 1076
Cdd:COG4717 474 LLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
253-496 |
4.44e-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: 41.86 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 253 AEGVSHHLALQLTNAKAQLRRLRQEVEEKAEQLLDSQaevQGLEAEIRRLRQETQALSAQAKRAELYREEAEALRERAGR 332
Cdd:COG3096 366 QEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQ---QALDVQQTRAIQYQQAVQALEKARALCGLPDLTPENAEDY 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 333 LPRLQ-------EELRRCREKLQAAEVFKGQLEEERVLSEALeASKVLLEEQLEVARE--RSARLHETQRENL-LLRTRL 402
Cdd:COG3096 443 LAAFRakeqqatEEVLELEQKLSVADAARRQFEKAYELVCKI-AGEVERSQAWQTAREllRRYRSQQALAQRLqQLRAQL 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 403 GEahadldsLRHQLEQLVEENVELELELQRSlepppgspgeASLPGAAPSLQDEVREAEAGRLRAVE--RENRELRGQLQ 480
Cdd:COG3096 522 AE-------LEQRLRQQQNAERLLEEFCQRI----------GQQLDAAEELEELLAELEAQLEELEEqaAEAVEQRSELR 584
|
250
....*....|....*.
gi 1907133161 481 MLQAQLGSQHPLLEEQ 496
Cdd:COG3096 585 QQLEQLRARIKELAAR 600
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1115-1279 |
4.79e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.23 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1115 LAHRELQGRHEQLQAQRANVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAevsrERGELQGERGElr 1194
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLV----QKEEQLDARAE-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1195 srlaRLELERAQLEIQSQQLRESNQQLDLSACRLTTQCELLTQLRsaQEEENRQLLAEVQALSRENRELLERSLESRDHL 1274
Cdd:PRK12705 99 ----KLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLT--PEQARKLLLKLLDAELEEEKAQRVKKIEEEADL 172
|
....*
gi 1907133161 1275 HREQR 1279
Cdd:PRK12705 173 EAERK 177
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
203-960 |
4.94e-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: 41.59 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 203 EELEMQLRSLTGMMSRLARERDLGAQRLAELLLEREPAHLLLPEAPANASAEGVSHHLALQ--LTNAKAQLRRLRQEVEE 280
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKekIGELEAEIASLERSIAE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 281 KAEQLLDSQAEVQGLEAEIRRLRQETQALSaqaKRAELYREEAEALRERagrLPRLQEELRRCREKLQAAEVFKGQLEEE 360
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELE---REIEEERKRRDKLTEE---YAELKEELEDLRAELEEVDKEFAETRDE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 361 rvLSEALEASKVLLEEQLEVARERSARLHETQRenllLRTRLGEAHADLDSLRHQLEQLVEENVELELELQRSlepppgs 440
Cdd:TIGR02169 387 --LKDYREKLEKLKREINELKRELDRLQEELQR----LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ------- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 441 pgEASLPGAAPSLQDEVREAEAGR--LRAVERENRELRGQLQMLQAQLGSqhpLLEEQRENSRQPPVPNRD--------- 509
Cdd:TIGR02169 454 --EWKLEQLAADLSKYEQELYDLKeeYDRVEKELSKLQRELAEAEAQARA---SEERVRGGRAVEEVLKASiqgvhgtva 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 510 ----------PATPSALHHSPQSPACQIGGEGSESLDL-----PSPASYSDITR---SPKCSQAPDSHPELESPLQMVSQ 571
Cdd:TIGR02169 529 qlgsvgeryaTAIEVAAGNRLNNVVVEDDAVAKEAIELlkrrkAGRATFLPLNKmrdERRDLSILSEDGVIGFAVDLVEF 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 572 DPQTS--------DQALQESDPTVETH-----------QCLEKSG-----HRVP--LQSPIVWDPPQGPEVRIEVQELLG 625
Cdd:TIGR02169 609 DPKYEpafkyvfgDTLVVEDIEAARRLmgkyrmvtlegELFEKSGamtggSRAPrgGILFSRSEPAELQRLRERLEGLKR 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 626 EtgsREAPQGELVHKAQVLKQESPKCRPRSAELTLREplKDQKALDRELELSKQQKETGRHEQRP------------KGL 693
Cdd:TIGR02169 689 E---LSSLQSELRRIENRLDELSQELSDASRKIGEIE--KEIEQLEQEEEKLKERLEELEEDLSSleqeienvkselKEL 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 694 ESKLGPQkpQQTSEGVPDAWSREEPTPGEtlvSAIPEeqaLRDEVAQLRREVAGLEVKLQAQAQRLEARSAEALCLSEEL 773
Cdd:TIGR02169 764 EARIEEL--EEDLHKLEEALNDLEARLSH---SRIPE---IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 774 AQARRTEAEAHQEAEAQAREQARLREAVDTASLELEAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQAL 853
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK 915
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 854 E---SQVRCHLEEAEREHAEKQALREELEKAVLRGQELGD---RLEHLQEELEqaALERQKFLQEQEnqhqrYRHLEQRL 927
Cdd:TIGR02169 916 RkrlSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDvqaELQRVEEEIR--ALEPVNMLAIQE-----YEEVLKRL 988
|
810 820 830
....*....|....*....|....*....|...
gi 1907133161 928 EaELQaastSKEEALMELKARALQLEEELIQLR 960
Cdd:TIGR02169 989 D-ELK----EKRAKLEEERKAILERIEEYEKKK 1016
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
263-341 |
5.01e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 263 QLTNAKAQLRRL---RQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYREEAEALR-ERAGRLPRLQE 338
Cdd:PHA02562 307 KLKELQHSLEKLdtaIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFvDNAEELAKLQD 386
|
...
gi 1907133161 339 ELR 341
Cdd:PHA02562 387 ELD 389
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
730-1106 |
5.42e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 41.38 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 730 EEQALRDEVAQLRREVAGLEVKLQAQAQRLEARSAEALCLSEELAQARRTEAEAHQEAEAQAREQARLREAVDTASLELE 809
Cdd:COG3899 862 ETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAA 941
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 810 AASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELG 889
Cdd:COG3899 942 AAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLA 1021
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 890 DRLEHLQEELEQAALERQKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALMELKARALQLEEELIQLRQYPVDLATG 969
Cdd:COG3899 1022 AALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAA 1101
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 970 ARAGPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQE 1049
Cdd:COG3899 1102 AAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAA 1181
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907133161 1050 LHRKLGVLEEEVRAARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDL 1106
Cdd:COG3899 1182 LLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALL 1238
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
827-1171 |
5.85e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 827 RERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLQEELEQAALER 906
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEI 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 907 QKFLQEQENQHQRYRHLEQRLeaelqaasTSKEEALMELKARALQLEEELIQL-RQYpvdlatgaRAGPRTVETQNGRLI 985
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQD--------SVKELIIKNLDNTRESLETQLKVLsRSI--------NKIKQNLEQKQKELK 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 986 EVERNNATLVAEKAALQGQLQHLEGQlgslqgraQELLLQSQRAqehssrLQAEKSMMEMQGQELHRKLGVLEEEVRAAr 1065
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKK--------ISSLKEKIEK------LESEKKEKESKISDLEDELNKDDFELKKE- 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1066 RAQEETRGQQQallrdhealvqlqrrqetELEgllvrhrDLKANMRALELAHRELQGRHEQLQAQRANVEAQevalLAER 1145
Cdd:TIGR04523 558 NLEKEIDEKNK------------------EIE-------ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE----IEEK 608
|
330 340
....*....|....*....|....*.
gi 1907133161 1146 ERLMQDghrqrgLEEELRRLQNEHER 1171
Cdd:TIGR04523 609 EKKISS------LEKELEKAKKENEK 628
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
907-1323 |
6.10e-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: 41.57 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 907 QKFLQEQENQHQRYRHLEQRLEAELQAASTSKEEALMELKaralQLEEELIQLRQYPVDlATGARAGPRTVETQNGRLIE 986
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELE----SKEEQLSSYEDKLFD-VCGSQDEESDLERLKEEIEK 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 987 VERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEMQGQELHRKLGVLEEE-----V 1061
Cdd:TIGR00606 651 SSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRrdemlG 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1062 RAARRAQE---------ETRGQQQALLRDHEALVQLQRRQETELEGLLVRH---RDLKANMRALELAHRELQGRHEQLQA 1129
Cdd:TIGR00606 731 LAPGRQSIidlkekeipELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEesaKVCLTDVTIMERFQMELKDVERKIAQ 810
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1130 QRANVEAQEVALLAE--RERLMQDGHRQRGLEEELRRLQNEHERAQMLLAEVSRERGELQGERGELRSRLARLELERAQL 1207
Cdd:TIGR00606 811 QAAKLQGSDLDRTVQqvNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQL 890
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1208 EIQSQQLRESNQQLDLSACRL----TTQCELLTQ---LRSAQEEENRQLLAEVQALSRE-------NRELLERSLESRDH 1273
Cdd:TIGR00606 891 VELSTEVQSLIREIKDAKEQDspleTFLEKDQQEkeeLISSKETSNKKAQDKVNDIKEKvknihgyMKDIENKIQDGKDD 970
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1274 LHREQREYLDQLNALRREKQKLVEKIMDQYRVLEPGPLPRTKKGSWLADK 1323
Cdd:TIGR00606 971 YLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDN 1020
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
260-523 |
6.49e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 260 LALQLTNAKAQLRRLRQEVEEKAEQLldsQAEVQGLEAEIRRLRQETQALSAQakraelyrEEAEALREragRLPRLQEE 339
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPEL---RKELEEAEAALEEFRQKNGLVDLS--------EEAKLLLQ---QLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 340 LRRCREKLQAAEVFKGQLEEErvLSEALEASKVLLEEQleVARERSARLHETQRENLLLRTRLGEAHADLDSLRHQLEQL 419
Cdd:COG3206 228 LAEARAELAEAEARLAALRAQ--LGSGPDALPELLQSP--VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 420 VEENVELELELQRSLEpppgsPGEASLPGAAPSLQDEVR--EAEAGRLRAVERENRELRGQLQMLQAQLGSQHPLLEEQR 497
Cdd:COG3206 304 RAQLQQEAQRILASLE-----AELEALQAREASLQAQLAqlEARLAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
250 260
....*....|....*....|....*...
gi 1907133161 498 ENSRQPPVPNR--DPATPSALHHSPQSP 523
Cdd:COG3206 379 LAEALTVGNVRviDPAVVPLKPVSPKKL 406
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
842-1301 |
6.75e-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: 41.19 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 842 QVEAAEQQVQALESQVRchLEEAEREHAEKQALREELEKAVLRGQElgdrlehlqeelEQAALERQKFLQEQENQhQRYR 921
Cdd:TIGR00606 465 QLEGSSDRILELDQELR--KAERELSKAEKNSLTETLKKEVKSLQN------------EKADLDRKLRKLDQEME-QLNH 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 922 HLEQRLEAE-LQAASTSKEEALMELKARAlqlEEELIQLRQY---PVDLATGARAGPRTVETQNGRLIEVERNNATLVAE 997
Cdd:TIGR00606 530 HTTTRTQMEmLTKDKMDKDEQIRKIKSRH---SDELTSLLGYfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQN 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 998 KAALQGQLQHLEGQLGSLQGR--------AQELLLQSQRAQEHSSRLQ--------------AEKSMMEMQG-------- 1047
Cdd:TIGR00606 607 KNHINNELESKEEQLSSYEDKlfdvcgsqDEESDLERLKEEIEKSSKQramlagatavysqfITQLTDENQSccpvcqrv 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1048 ----QELHRKLGVLEEEVRAARRAQEETRGQqqallrdheaLVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGR 1123
Cdd:TIGR00606 687 fqteAELQEFISDLQSKLRLAPDKLKSTESE----------LKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKV 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1124 HEQLQAQRANVEAQEVAL--LAERERLMQDGHRQRGLEEELRRLQNEHERAQMLLAE----------VSRERGELQGERG 1191
Cdd:TIGR00606 757 NRDIQRLKNDIEEQETLLgtIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAklqgsdldrtVQQVNQEKQEKQH 836
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1192 ELRSRLARLELERAQLEIQSQQLRESNQQL-DLSACRLTTQCELltQLRSAQEEENRQLLAEVQALSRENRELLERSLES 1270
Cdd:TIGR00606 837 ELDTVVSKIELNRKLIQDQQEQIQHLKSKTnELKSEKLQIGTNL--QRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPL 914
|
490 500 510
....*....|....*....|....*....|.
gi 1907133161 1271 RDHLHREQREYLDQLNALRREKQKLVEKIMD 1301
Cdd:TIGR00606 915 ETFLEKDQQEKEELISSKETSNKKAQDKVND 945
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
827-949 |
7.46e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 827 RERRQWERDGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHAEKQALREELEKAVLRGQELGDRLEHLQEElEQAALER 906
Cdd:PRK12704 68 KLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE-QLQELER 146
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907133161 907 QKFLQEQENQHQRYRHLEQrlEAELQAAST---SKEEALMELKARA 949
Cdd:PRK12704 147 ISGLTAEEAKEILLEKVEE--EARHEAAVLikeIEEEAKEEADKKA 190
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
261-418 |
7.62e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 261 ALQLTNAKAQLRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQALSAQAKRAELYR----EEAEALRERAgrlprl 336
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAeagvEDEEELRAAL------ 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 337 qEELRRCREKLQAAEVFKGQLEEErvLSEALEASKVLLEEQLEvarersARLHETQRENLLLRTRLGEAHADLDSLRHQL 416
Cdd:COG4717 392 -EQAEEYQELKEELEELEEQLEEL--LGELEELLEALDEEELE------EELEELEEELEELEEELEELREELAELEAEL 462
|
..
gi 1907133161 417 EQ 418
Cdd:COG4717 463 EQ 464
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
203-371 |
8.28e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 203 EELEMQLRSLTGMMSRLARERDLGAQRLAELL-------LEREPAHLLLPEAPANASAEG-VSHHLALQLTNAKAQLRRL 274
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLralyrlgRQPPLALLLSPEDFLDAVRRLqYLKYLAPARREQAEELRAD 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 275 RQEVEEKAEQLLDSQAEVQGLEAEIRRLRQETQAlsAQAKRAELYREEAEALRERAGRLPRLQEELRRCREKLQAAEVfK 354
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEA--LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA-E 235
|
170
....*....|....*..
gi 1907133161 355 GQLEEERVLSEALEASK 371
Cdd:COG4942 236 AAAAAERTPAAGFAALK 252
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
436-614 |
8.43e-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: 40.91 E-value: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 436 PPPGSPGEASLPGAAPSLQDEVREAEAGRLRAVERenrelrgQLQMLQAQLGSQHPLLEEqrenSRQPPVPNRDP--ATP 513
Cdd:pfam03154 199 PTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQ-------TPTLHPQRLPSPHPPLQP----MTQPPPPSQVSpqPLP 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 514 SALHHSPQSPACQIGGEGSESLDLP-SPASYSDITRSPKCSQAPDSHPELESPLQMVSQDPQTSDQALQESDPTvethqc 592
Cdd:pfam03154 268 QPSLHGQMPPMPHSLQTGPSHMQHPvPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPR------ 341
|
170 180
....*....|....*....|..
gi 1907133161 593 lEKSGHRVPLQSPIVWDPPQGP 614
Cdd:pfam03154 342 -EQPLPPAPLSMPHIKPPPTTP 362
|
|
| HAUS6_N |
pfam14661 |
HAUS augmin-like complex subunit 6 N-terminus; This family includes the N-terminus of HAUS ... |
230-346 |
8.64e-03 |
|
HAUS augmin-like complex subunit 6 N-terminus; This family includes the N-terminus of HAUS augmin-like complex subunit 6. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.
Pssm-ID: 464244 [Multi-domain] Cd Length: 233 Bit Score: 39.56 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 230 LAELLLEREPAHLLLPE-----APANASAEGVSHHLALQLTNAKaqlRRLRQEVEEKAEQLLDSQAEVQGLEAEIRRLRQ 304
Cdd:pfam14661 119 LKKVLKTRSKNGGGFPAlaqklALENRGYSGEQAELAALILAHR---SSLLRILEEKDALIQKYQQFAQLLVKKIRALRA 195
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1907133161 305 ETQALSAQAKRAELYREEAEALREragrlpRLQEELRRCREK 346
Cdd:pfam14661 196 EREKLDALLKKMEKDNRSRSAEQD------ALQEKIDKVRNL 231
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
260-500 |
8.78e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.71 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 260 LALQLTNAKAQLRRLRQEVEEKAEQLldsqaevqgleaeirRLRQETQALSAQAKRAELYREEAEALRERAGRLPRLQEE 339
Cdd:COG5185 280 LNENANNLIKQFENTKEKIAEYTKSI---------------DIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 340 LRRCREKLQAAEVFKGQLEEERVLSEALEASKVLLEE---QLEVARERSARLHETQRE-----NLLLRTRLGEAHADLDS 411
Cdd:COG5185 345 IEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSfkdTIESTKESLDEIPQNQRGyaqeiLATLEDTLKAADRQIEE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 412 LRHQLEQlveeNVELELELQRSLEPPPGSpGEASLPGAAPSLQDEVREAEAGRLRAVERENRELRGQLQMLQAQLGSQHP 491
Cdd:COG5185 425 LQRQIEQ----ATSSNEEVSKLLNELISE-LNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKA 499
|
....*....
gi 1907133161 492 LLEEQRENS 500
Cdd:COG5185 500 TLEKLRAKL 508
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
996-1274 |
9.62e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 9.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 996 AEKAALQGQLQhlegqlgslqgRAQELLLQSQRAQEHSSRL-----QAEKSMMEMQgqelhRKLGVLEEEVRAARRAQEE 1070
Cdd:PRK11281 56 AEDKLVQQDLE-----------QTLALLDKIDRQKEETEQLkqqlaQAPAKLRQAQ-----AELEALKDDNDEETRETLS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1071 TRGQQQALLRDHEALVQLQRRQET--ELEGLLVrhrdlkANMRALELAHREL---QGRHEQLQAQRANVEAQEVALLAER 1145
Cdd:PRK11281 120 TLSLRQLESRLAQTLDQLQNAQNDlaEYNSQLV------SLQTQPERAQAALyanSQRLQQIRNLLKGGKVGGKALRPSQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 1146 ERLMQdghrqrgLEEELRRLQNEHERAqmLLAEVSRERGELQGERGELRSRLARLELERAQLE--IQSQQLRESNQQLdl 1223
Cdd:PRK11281 194 RVLLQ-------AEQALLNAQNDLQRK--SLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQeaINSKRLTLSEKTV-- 262
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907133161 1224 sacrlttqcellTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHL 1274
Cdd:PRK11281 263 ------------QEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEKL 301
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
799-1039 |
9.67e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 799 EAVDTASLELEAASREREALAEALAAAGRERRQWERDGPRLRAQVEAAEQQVQALESQvrchLEEAEREHAEKQALREEL 878
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE----LAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 879 EKAV-LRGQELGDRLEHLQEELEQAALerqKFLQEQENQHQRYRHLEQrleaeLQAASTSKEEALMELKARAlqleEELI 957
Cdd:COG4942 96 RAELeAQKEELAELLRALYRLGRQPPL---ALLLSPEDFLDAVRRLQY-----LKYLAPARREQAEELRADL----AELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907133161 958 QLRQYPVDLAtgaragprtvETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQ 1037
Cdd:COG4942 164 ALRAELEAER----------AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
..
gi 1907133161 1038 AE 1039
Cdd:COG4942 234 AE 235
|
|
| |
