|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1-1011 |
0e+00 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 1849.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 1 MAAKLSTCFLSHGWGSLdcrRSNGRFLAPSQRLLPASCKMRQRNFSSQHKRQQTKKVSPDRRPTNSHFQSNGDEDTEPEN 80
Cdd:PLN02939 1 AAAAESAALLSHGCGPI---RSRAPFYLPSRRRLAVSCRARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 81 ALADGVSSLNQGTIPDGEDADVDSHIAIEHINDNPLKHLTvseemtplgiNVKSGEQLSSFQLEDLVGMLKNAEKNILLL 160
Cdd:PLN02939 78 TSLRTVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQT----------NSKDGEQLSDFQLEDLVGMIQNAEKNILLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 161 NQARVRALQDLEKILTEKDALQGEINILEMRLAETNARIKVAAQEKIHVEILEEQLVNLRNELSHRGVTEGSGadmhenw 240
Cdd:PLN02939 148 NQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLC------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 241 nkafdgVHSLGKELSLLRTENVSLKDDILALKEELSHVQKTDKRVVMLEKERSFLESALKELEFKLVASQEDVSKLSTLK 320
Cdd:PLN02939 221 ------VHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQ 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 321 FECknLWDRVENLQVLLDRATDQADKAILVLEQNQELRKKVDMLEESLEEANVYKLSSEKMqqynDLMQKKIKLLEERLD 400
Cdd:PLN02939 295 YDC--WWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKV----ELLQQKLKLLEERLQ 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 401 RSDEEILSYVKLYQESIKEFQDTLNNLKEESKRRALNEPVDDMPWDFWSRLLLIVDGWLLEKKISANDAKLLREMVWKRD 480
Cdd:PLN02939 369 ASDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLEHPADDMPSEFWSRILLLIDGWLLEKKISNNDAKLLREMVWKRD 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 481 GRIRDAYLVCKDTNEHEAVAIFLKLTSSPKRSRLHVIHIAAEMAPVAKVGGLGDVVSGLSRALQKKGHLVEIVLPKYDCM 560
Cdd:PLN02939 449 GRIREAYLSCKGKNEREAVENFLKLTLSGTSSGLHIVHIAAEMAPVAKVGGLADVVSGLGKALQKKGHLVEIVLPKYDCM 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 561 QYDHIRDLRVLDMELESYFDGRLFRNKVWVGTVEGLPVYFIEPHHPSKFFWRGTVYGEHDDFRRFSYFSRAALELLLQAG 640
Cdd:PLN02939 529 QYDQIRNLKVLDVVVESYFDGNLFKNKIWTGTVEGLPVYFIEPQHPSKFFWRAQYYGEHDDFKRFSYFSRAALELLYQSG 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 641 KKPDIIHCHDWQTAFVAPLYWDLYAPKGLNSARICFTCHNFEYQGTAPASEMASCGLDVHHLNRPDRMQDNSaHDRVNPV 720
Cdd:PLN02939 609 KKPDIIHCHDWQTAFVAPLYWDLYAPKGFNSARICFTCHNFEYQGTAPASDLASCGLDVHQLDRPDRMQDNA-HGRINVV 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 721 KGAIVFSNIVTTVSPTYAQEVRTsEGGRGLHSTLNSHSKKFIGILNGIDTDAWDPATDVYLKSQFNANDLQGKAENKEAL 800
Cdd:PLN02939 688 KGAIVYSNIVTTVSPTYAQEVRS-EGGRGLQDTLKFHSKKFVGILNGIDTDTWNPSTDRFLKVQYNANDLQGKAANKAAL 766
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 801 RKHLGLSYADTRRPLVGCIARLVPQKGIHLIRHAIYRTLELGGQFVLLGSSPVPHIQVEFEGIANHFKGDDHIRLILKYD 880
Cdd:PLN02939 767 RKQLGLSSADASQPLVGCITRLVPQKGVHLIRHAIYKTAELGGQFVLLGSSPVPHIQREFEGIADQFQSNNNIRLILKYD 846
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 881 ESLSHSIYAASDMFLIPSMFEPCGLTQMIAMRYGSIPIARKTGGLNDSVFDVDDDTIPLQFRNGYTFLNPDEQGLNGALE 960
Cdd:PLN02939 847 EALSHSIYAASDMFIIPSMFEPCGLTQMIAMRYGSVPIVRKTGGLNDSVFDFDDETIPVELRNGFTFLTPDEQGLNSALE 926
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|.
gi 1847837041 961 RAFNHYKTNKESWQKLVKKDMNIDFSWESSALQYEEIYEKSVARARAASLV 1011
Cdd:PLN02939 927 RAFNYYKRKPEVWKQLVQKDMNIDFSWDSSASQYEELYQRAVARARAAANR 977
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
515-1000 |
0e+00 |
|
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.
Pssm-ID: 340822 [Multi-domain] Cd Length: 474 Bit Score: 620.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 515 HVIHIAAEMAPVAKVGGLGDVVSGLSRALQKKGHLVEIVLPKYDCMQYDHIRDLRVLDmeLESYFDGRLFRNKVWVGTVE 594
Cdd:cd03791 1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVLG--LEVKVGGRGEEVGVFELPVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 595 GLPVYFIEPHHPSKFFWR--GTVYGEHDDFRRFSYFSRAALELLLQAGKKPDIIHCHDWQTAFVAPLYWDLYAPKGLNSA 672
Cdd:cd03791 79 GVDYYFLDNPEFFDRPGLpgPPGYDYPDNAERFAFFSRAALELLRRLGFQPDIIHANDWHTALVPAYLKTRYRGPGFKKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 673 RICFTCHNFEYQGTAPASEMASCGLDVHHlnrpDRMQDNSAHDRVNPVKGAIVFSNIVTTVSPTYAQEVRTSEGGRGLHS 752
Cdd:cd03791 159 KTVFTIHNLAYQGLFPLDTLAELGLPPEL----FHIDGLEFYGQINFLKAGIVYADRVTTVSPTYAKEILTPEYGEGLDG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 753 TLNSHSKKFIGILNGIDTDAWDPATDVYLKSQFNANDLQGKAENKEALRKHLGLSyADTRRPLVGCIARLVPQKGIHLIR 832
Cdd:cd03791 235 VLRARAGKLSGILNGIDYDEWNPATDKLIPANYSANDLEGKAENKAALQKELGLP-VDPDAPLFGFVGRLTEQKGVDLIL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 833 HAIYRTLELGGQFVLLGSSPVPHIQVEFEgIANHFKgdDHIRLILKYDESLSHSIYAASDMFLIPSMFEPCGLTQMIAMR 912
Cdd:cd03791 314 DALPELLEEGGQLVVLGSGDPEYEQAFRE-LAERYP--GKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 913 YGSIPIARKTGGLNDSVFDVDDDTiplQFRNGYTFLNPDEQGLNGALERAFNHYKtNKESWQKLVKKDMNIDFSWESSAL 992
Cdd:cd03791 391 YGTLPIVRRTGGLADTVFDYDPET---GEGTGFVFEDYDAEALLAALRRALALYR-NPELWRKLQKNAMKQDFSWDKSAK 466
|
....*...
gi 1847837041 993 QYEEIYEK 1000
Cdd:cd03791 467 EYLELYRS 474
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
514-1000 |
0e+00 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 617.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 514 LHVIHIAAEMAPVAKVGGLGDVVSGLSRALQKKGHLVEIVLPKYDCMQyDHIRDLRVLdMELESYFDGRLFRNKVWVGTV 593
Cdd:COG0297 1 MKILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSID-DKLKDLEVV-ASLEVPLGGRTYYARVLEGPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 594 EGLPVYFIEphHPSkFFWRGTVYGE-----HDDFRRFSYFSRAALELLLQAGKKPDIIHCHDWQTAFVAPLYWDLYAPKG 668
Cdd:COG0297 79 DGVPVYFID--NPE-LFDRPGPYGDpdrdyPDNAERFAFFSRAALELLKGLDWKPDIIHCHDWQTGLIPALLKTRYADDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 669 LNSARICFTCHNFEYQGTAPASEMASCGLDvHHLNRPDRMQDnsaHDRVNPVKGAIVFSNIVTTVSPTYAQEVRTSEGGR 748
Cdd:COG0297 156 FKRIKTVFTIHNLAYQGIFPAEILELLGLP-PELFTPDGLEF---YGQINFLKAGIVYADRVTTVSPTYAREIQTPEFGE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 749 GLHSTLNSHSKKFIGILNGIDTDAWDPATDVYLKSQFNANDLQGKAENKEALRKHLGLSyADTRRPLVGCIARLVPQKGI 828
Cdd:COG0297 232 GLDGLLRARSGKLSGILNGIDYDVWNPATDPYLPANYSADDLEGKAANKAALQEELGLP-VDPDAPLIGMVSRLTEQKGL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 829 HLIRHAIYRTLELGGQFVLLGSSPvPHIQVEFEGIANHFKGddHIRLILKYDESLSHSIYAASDMFLIPSMFEPCGLTQM 908
Cdd:COG0297 311 DLLLEALDELLEEDVQLVVLGSGD-PEYEEAFRELAARYPG--RVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQM 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 909 IAMRYGSIPIARKTGGLNDSVFDVDDDTiplQFRNGYTFLNPDEQGLNGALERAFNHYKtNKESWQKLVKKDMNIDFSWE 988
Cdd:COG0297 388 YALRYGTVPIVRRTGGLADTVIDYNEAT---GEGTGFVFDEYTAEALLAAIRRALALYR-DPEAWRKLQRNAMKQDFSWE 463
|
490
....*....|..
gi 1847837041 989 SSALQYEEIYEK 1000
Cdd:COG0297 464 KSAKEYLELYRE 475
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
514-1001 |
0e+00 |
|
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) synthases that use ADP-glucose (EC 2.4.1.21), rather than UDP-glucose (EC 2.4.1.11) as in animals, as the glucose donor. This enzyme is found in bacteria and plants. Whether the name given is glycogen synthase or starch synthase depends on context, and therefore on substrate. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
Pssm-ID: 273969 [Multi-domain] Cd Length: 473 Bit Score: 610.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 514 LHVIHIAAEMAPVAKVGGLGDVVSGLSRALQKKGHLVEIVLPKYDCMQYDHIRdlRVLDMELESYF-DGRLFRNKVWVGT 592
Cdd:TIGR02095 1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVDD--QVKVVELVDLSvGPRTLYVKVFEGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 593 VEGLPVYFIepHHPSKFFWRGTVYGE--HDDFRRFSYFSRAALELLLQAGKKPDIIHCHDWQTAFVAPLYWDLYAPkglN 670
Cdd:TIGR02095 79 VEGVPVYFI--DNPSLFDRPGGIYGDdyPDNAERFAFFSRAAAELLSGLGWQPDVVHAHDWHTALVPALLKAVYRP---N 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 671 SARICFTCHNFEYQGTAPASEMASCGLDVHHLNrpdrMQDNSAHDRVNPVKGAIVFSNIVTTVSPTYAQEVRTSEGGRGL 750
Cdd:TIGR02095 154 PIKTVFTIHNLAYQGVFPADDFSELGLPPEYFH----MEGLEFYGRVNFLKGGIVYADRVTTVSPTYAREILTPEFGYGL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 751 HSTLNSHSKKFIGILNGIDTDAWDPATDVYLKSQFNANDLQGKAENKEALRKHLGLSyADTRRPLVGCIARLVPQKGIHL 830
Cdd:TIGR02095 230 DGVLKARSGKLRGILNGIDTEVWNPATDPYLKANYSADDLAGKAENKEALQEELGLP-VDDDVPLFGVISRLTQQKGVDL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 831 IRHAIYRTLELGGQFVLLGSSPvPHIQVEFEGIAnhFKGDDHIRLILKYDESLSHSIYAASDMFLIPSMFEPCGLTQMIA 910
Cdd:TIGR02095 309 LLAALPELLELGGQLVVLGTGD-PELEEALRELA--ERYPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLYA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 911 MRYGSIPIARKTGGLNDSVFDVDDDTiplQFRNGYTFLNPDEQGLNGALERAFNHYKTNKESWQKLVKKDMNIDFSWESS 990
Cdd:TIGR02095 386 MRYGTVPIVRRTGGLADTVVDGDPEA---ESGTGFLFEEYDPGALLAALSRALRLYRQDPSLWEALQKNAMSQDFSWDKS 462
|
490
....*....|.
gi 1847837041 991 ALQYEEIYEKS 1001
Cdd:TIGR02095 463 AKQYVELYRSL 473
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
514-1004 |
0e+00 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 597.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 514 LHVIHIAAEMAPVAKVGGLGDVVSGLSRALQKKGHLVEIVLPKYDCMQyDHIRDLRVldmelesyfDGRLFRNKVWVGTV 593
Cdd:PRK00654 1 MKILFVASECAPLIKTGGLGDVVGALPKALAALGHDVRVLLPGYPAIR-EKLRDAQV---------VGRLDLFTVLFGHL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 594 E--GLPVYFIEPHHpskFFWRGTVYGEHDDFRRFSYFSRAALELLLQAGKKPDIIHCHDWQTAFVAPLYWDLYAPkGLNS 671
Cdd:PRK00654 71 EgdGVPVYLIDAPH---LFDRPSGYGYPDNGERFAFFSWAAAEFAEGLDPRPDIVHAHDWHTGLIPALLKEKYWR-GYPD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 672 ARICFTCHNFEYQGTAPASEMASCGLDVHHLNrPDRMQDnsaHDRVNPVKGAIVFSNIVTTVSPTYAQEVRTSEGGRGLH 751
Cdd:PRK00654 147 IKTVFTIHNLAYQGLFPAEILGELGLPAEAFH-LEGLEF---YGQISFLKAGLYYADRVTTVSPTYAREITTPEFGYGLE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 752 STLNSHSKKFIGILNGIDTDAWDPATDVYLKSQFNANDLQGKAENKEALRKHLGLsyADTRRPLVGCIARLVPQKGIHLI 831
Cdd:PRK00654 223 GLLRARSGKLSGILNGIDYDIWNPETDPLLAANYSADDLEGKAENKRALQERFGL--PDDDAPLFAMVSRLTEQKGLDLV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 832 RHAIYRTLELGGQFVLLGsSPVPHIQVEFEGIANHFKGddHIRLILKYDESLSHSIYAASDMFLIPSMFEPCGLTQMIAM 911
Cdd:PRK00654 301 LEALPELLEQGGQLVLLG-TGDPELEEAFRALAARYPG--KVGVQIGYDEALAHRIYAGADMFLMPSRFEPCGLTQLYAL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 912 RYGSIPIARKTGGLNDSVFDVDDDTiplQFRNGYTFLNPDEQGLNGALERAFNHYKTNKEsWQKLVKKDMNIDFSWESSA 991
Cdd:PRK00654 378 RYGTLPIVRRTGGLADTVIDYNPED---GEATGFVFDDFNAEDLLRALRRALELYRQPPL-WRALQRQAMAQDFSWDKSA 453
|
490
....*....|...
gi 1847837041 992 LQYEEIYEKSVAR 1004
Cdd:PRK00654 454 EEYLELYRRLLGK 466
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
510-998 |
4.20e-166 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 514.80 E-value: 4.20e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 510 KRSRLHVIHIAAEMAPVAKVGGLGDVVSGLSRALQKKGHLVEIVLPKYDCMQYDHIRDLRvldmELESYFDGRLfRNKVW 589
Cdd:PLN02316 584 KEPPMHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYDCLNLSHVKDLH----YQRSYSWGGT-EIKVW 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 590 VGTVEGLPVYFIEPHhpSKFFWRGTVYGEHDDFRRFSYFSRAALELLLQAGKKPDIIHCHDWQTAFVAPLYWDLYAPKGL 669
Cdd:PLN02316 659 FGKVEGLSVYFLEPQ--NGMFWAGCVYGCRNDGERFGFFCHAALEFLLQSGFHPDIIHCHDWSSAPVAWLFKDHYAHYGL 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 670 NSARICFTCHNFEYqgtapasemascglDVHHLNRpdrmqdnsahdrvnpvkgAIVFSNIVTTVSPTYAQEVRTseggrg 749
Cdd:PLN02316 737 SKARVVFTIHNLEF--------------GANHIGK------------------AMAYADKATTVSPTYSREVSG------ 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 750 lHSTLNSHSKKFIGILNGIDTDAWDPATDVYLKSQFNA-NDLQGKAENKEALRKHLGLSYADTrrPLVGCIARLVPQKGI 828
Cdd:PLN02316 779 -NSAIAPHLYKFHGILNGIDPDIWDPYNDNFIPVPYTSeNVVEGKRAAKEALQQRLGLKQADL--PLVGIITRLTHQKGI 855
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 829 HLIRHAIYRTLELGGQFVLLGSSPVPHIQVEFEGIANHFKGDDH--IRLILKYDESLSHSIYAASDMFLIPSMFEPCGLT 906
Cdd:PLN02316 856 HLIKHAIWRTLERNGQVVLLGSAPDPRIQNDFVNLANQLHSSHHdrARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLT 935
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 907 QMIAMRYGSIPIARKTGGLNDSVFDVDDDTIPLQFR----NGYTFLNPDEQGLNGALERAFNHYKTNKESWQKLVKKDMN 982
Cdd:PLN02316 936 QLTAMRYGSIPVVRKTGGLFDTVFDVDHDKERAQAQglepNGFSFDGADAAGVDYALNRAISAWYDGRDWFNSLCKRVME 1015
|
490
....*....|....*.
gi 1847837041 983 IDFSWESSALQYEEIY 998
Cdd:PLN02316 1016 QDWSWNRPALDYMELY 1031
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
512-1007 |
5.06e-89 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 293.55 E-value: 5.06e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 512 SRLHVIHIAAEMAPVAKVGGLGDVVSGLSRALQKKGHLVEIVLPKYDCM--QYDHIRDLRVLDMelesYFDG--RLFRnk 587
Cdd:PRK14099 2 TPLRVLSVASEIFPLIKTGGLADVAGALPAALKAHGVEVRTLVPGYPAVlaGIEDAEQVHSFPD----LFGGpaRLLA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 588 vwvGTVEGLPVYFIE-PHhpskFFWR-GTVY----GEH--DDFRRFSYFSRAALELLLQA--GKKPDIIHCHDWQTAFVA 657
Cdd:PRK14099 76 ---ARAGGLDLFVLDaPH----LYDRpGNPYvgpdGKDwpDNAQRFAALARAAAAIGQGLvpGFVPDIVHAHDWQAGLAP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 658 P--LYWDLYAPKGLnsaricFTCHNFEYQGTAPASEMASCGLDVHHLNrpdrMQDNSAHDRVNPVKGAIVFSNIVTTVSP 735
Cdd:PRK14099 149 AylHYSGRPAPGTV------FTIHNLAFQGQFPRELLGALGLPPSAFS----LDGVEYYGGIGYLKAGLQLADRITTVSP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 736 TYAQEVRTSEGGRGLHSTLNSHSKKFIGILNGIDTDAWDPATDVYLKSQFNANDLQGKAENKEALRKHLGLSyADTRRPL 815
Cdd:PRK14099 219 TYALEIQGPEAGMGLDGLLRQRADRLSGILNGIDTAVWNPATDELIAATYDVETLAARAANKAALQARFGLD-PDPDALL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 816 VGCIARLVPQKGIHLIRHAIYRTLELGGQFVLLGSSPvPHIQVEFEGIANHFKGddHIRLILKYDESLSHSIYAASDMFL 895
Cdd:PRK14099 298 LGVISRLSWQKGLDLLLEALPTLLGEGAQLALLGSGD-AELEARFRAAAQAYPG--QIGVVIGYDEALAHLIQAGADALL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 896 IPSMFEPCGLTQMIAMRYGSIPIARKTGGLNDSVFDVDDDTIPLQFRNGYTFLNPDEQGLNGALERAFNHYkTNKESWQK 975
Cdd:PRK14099 375 VPSRFEPCGLTQLCALRYGAVPVVARVGGLADTVVDANEMAIATGVATGVQFSPVTADALAAALRKTAALF-ADPVAWRR 453
|
490 500 510
....*....|....*....|....*....|..
gi 1847837041 976 LVKKDMNIDFSWESSALQYEEIYEKSVARARA 1007
Cdd:PRK14099 454 LQRNGMTTDVSWRNPAQHYAALYRSLVAERRP 485
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
516-755 |
1.68e-86 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 278.06 E-value: 1.68e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 516 VIHIAAEMAPVAKVGGLGDVVSGLSRALQKKGHLVEIVLPKYDCMQYDHIRDLRVLDMELESYFDGRLFRNKVWVGTVEG 595
Cdd:pfam08323 1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNIPEERNQLEDVIRLSVAAGVPVRPLTVGVARLELDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 596 LPVYFIEPHHpskFFWRGTVYGE-----HDDFRRFSYFSRAALELLLQAGKKPDIIHCHDWQTAFVAPLYWDLYAPKGLN 670
Cdd:pfam08323 81 VDVYFLDNPD---YFDRPGLYGDdgrdyEDNAERFAFFSRAALELAKKLGWIPDIIHCHDWHTALVPAYLKEAYADDPFK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 671 SARICFTCHNFEYQGTAPASEMASCGLDVHHLNrpdrMQDNSAHDRVNPVKGAIVFSNIVTTVSPTYAQEVRTSEGGRGL 750
Cdd:pfam08323 158 NIKTVFTIHNLAYQGRFPADLLDLLGLPPEDFN----LDGLEFYGQINFLKAGIVYADAVTTVSPTYAEEIQTPEFGGGL 233
|
....*
gi 1847837041 751 HSTLN 755
Cdd:pfam08323 234 DGLLR 238
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
511-1000 |
6.99e-71 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 244.26 E-value: 6.99e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 511 RSRLHVIHIAAEMAPVAKVGGLGDVVSGLSRALQKKGHLVEIVLPKYDCMQYDHIR--D-LRVLDMELESYFDGRLFRNK 587
Cdd:PRK14098 3 RRNFKVLYVSGEVSPFVRVSALADFMASFPQALEEEGFEARIMMPKYGTINDRKFRlhDvLRLSDIEVPLKEKTDLLHVK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 588 VWVGTVEGLPVYFIephHPSKFFWRGTVYGE---HDDFR----RFSYFSRAALELLLQAGKKPDIIHCHDWQTAFVAPLY 660
Cdd:PRK14098 83 VTALPSSKIQTYFL---YNEKYFKRNGLFTDmslGGDLKgsaeKVIFFNVGVLETLQRLGWKPDIIHCHDWYAGLVPLLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 661 WDLYAPKGL-NSARICFTCHNFEYQGTAPasemascgLDVHHLNRPDRMQD--NSAHDRVNPVKGAIVFSNIVTTVSPTY 737
Cdd:PRK14098 160 KTVYADHEFfKDIKTVLTIHNVYRQGVLP--------FKVFQKLLPEEVCSglHREGDEVNMLYTGVEHADLLTTTSPRY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 738 AQEVRT-SEGGRGLHSTLNSHSKKFIGILNGIDTDAWDPATDVYLKSQFNANDLQGKAENKEALRKHLGLSYaDTRRPLV 816
Cdd:PRK14098 232 AEEIAGdGEEAFGLDKVLEERKMRLHGILNGIDTRQWNPSTDKLIKKRYSIERLDGKLENKKALLEEVGLPF-DEETPLV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 817 GCIARLVPQKGIHLIRHAIYRTLELGGQFVLLGSSPVPHIQVEFEGIANHfkgDDHIRLILKYDESLSHSIYAASDMFLI 896
Cdd:PRK14098 311 GVIINFDDFQGAELLAESLEKLVELDIQLVICGSGDKEYEKRFQDFAEEH---PEQVSVQTEFTDAFFHLAIAGLDMLLM 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 897 PSMFEPCGLTQMIAMRYGSIPIARKTGGLNDSVFDVDDDTiplqfRNGYTFLNPDEQGLNGALERAFNHYKtNKESWQKL 976
Cdd:PRK14098 388 PGKIESCGMLQMFAMSYGTIPVAYAGGGIVETIEEVSEDK-----GSGFIFHDYTPEALVAKLGEALALYH-DEERWEEL 461
|
490 500
....*....|....*....|....
gi 1847837041 977 VKKDMNIDFSWESSALQYEEIYEK 1000
Cdd:PRK14098 462 VLEAMERDFSWKNSAEEYAQLYRE 485
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
515-999 |
7.32e-22 |
|
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.
Pssm-ID: 340831 [Multi-domain] Cd Length: 366 Bit Score: 98.76 E-value: 7.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 515 HVIHIAAEMAPVakVGGLGDVVSGLSRALQKKGHLVEIVLPKydcmqydhirdlrvldmelesyfdgrlfrnkvwvgtve 594
Cdd:cd03801 1 KILLLSPELPPP--VGGAERHVRELARALAARGHDVTVLTPA-------------------------------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 595 glpvyfiEPHHPSKFFWRGTVYGEHDDFRRFSYFSRAALEL-LLQAGKKPDIIHCHDWQTAFVAPLYwdlyapKGLNSAR 673
Cdd:cd03801 41 -------DPGEPPEELEDGVIVPLLPSLAALLRARRLLRELrPLLRLRKFDVVHAHGLLAALLAALL------ALLLGAP 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 674 ICFTCHNFEYQGTAPASEMAScgldvHHLNRPDRMQDNSAHdrvnpvkgaivfsniVTTVSPTYAQEvrtseggrgLHST 753
Cdd:cd03801 108 LVVTLHGAEPGRLLLLLAAER-----RLLARAEALLRRADA---------------VIAVSEALRDE---------LRAL 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 754 LNSHSKKFIGILNGIDTDAWDPATdvylksqfnandlqgkaenkealRKHLGLSyadTRRPLVGCIARLVPQKGIHLIRH 833
Cdd:cd03801 159 GGIPPEKIVVIPNGVDLERFSPPL-----------------------RRKLGIP---PDRPVLLFVGRLSPRKGVDLLLE 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 834 AIYRTLELGG--QFVLLGSSPvpHIQVEFEgiANHFKGDDHIRLILKYDESLSHSIYAASDMFLIPSMFEPCGLTQMIAM 911
Cdd:cd03801 213 ALAKLLRRGPdvRLVIVGGDG--PLRAELE--ELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAM 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 912 RYGSIPIARKTGGLNDSvfdVDDDTiplqfrNGYTFLNPDEQGLNGALERAFNH----YKTNKESWQKLVKKdmnidFSW 987
Cdd:cd03801 289 AAGLPVVATDVGGLPEV---VEDGE------GGLVVPPDDVEALADALLRLLADpelrARLGRAARERVAER-----FSW 354
|
490
....*....|..
gi 1847837041 988 ESSALQYEEIYE 999
Cdd:cd03801 355 ERVAERLLDLYR 366
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
702-1000 |
2.81e-11 |
|
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.
Pssm-ID: 340851 [Multi-domain] Cd Length: 364 Bit Score: 66.20 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 702 LNRPDRMQDNSAHDRVNPVKGAIVFSNI-VTTVSPTYAQEVRTSeggrglhsTLNSHSKKFIgILNGIDTDAWDPAtdvy 780
Cdd:cd03825 112 LNSYPPAKKDLSRQLFRRKREALAKKRLtIVAPSRWLADMVRRS--------PLLKGLPVVV-IPNGIDTEIFAPV---- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 781 lksqfnandlqgkaeNKEALRKHLGLSyadTRRPLVGCIARLV--PQKGI--------HLIRHAIYRTLELGGQFVLLGS 850
Cdd:cd03825 179 ---------------DKAKARKRLGIP---QDKKVILFGAESVtkPRKGFdeliealkLLATKDDLLLVVFGKNDPQIVI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 851 SPVPHIQVEFEgianhfkgDDHIRLilkydeslsHSIYAASDMFLIPSMFEPCGLTQMIAMRYGSIPIARKTGGLNDSVF 930
Cdd:cd03825 241 LPFDIISLGYI--------DDDEQL---------VDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQ 303
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 931 DVDddtiplqfrNGYTFLNPDEQGLNGALERAFNHYKTNKESWQKLVKKDMNiDFSWESSALQYEEIYEK 1000
Cdd:cd03825 304 HGV---------TGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAEN-HFDQRVQAQRYLELYKD 363
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
142-438 |
1.74e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.04 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 142 QLEDLVGMLKNAEKNILLLNQarvralqDLEKILTEKDALQGEINILEMRLAETNARIKVAAQE----KIHVEILEEQLV 217
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQLNE-------QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEnqsyKQEIKNLESQIN 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 218 NLRNELSHRgvtegsgadmhENWNKAFDG-VHSLGKELSLLRTENVSLKDDILALKEELSHvqktdkrvvmLEKERSFLE 296
Cdd:TIGR04523 395 DLESKIQNQ-----------EKLNQQKDEqIKKLQQEKELLEKEIERLKETIIKNNSEIKD----------LTNQDSVKE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 297 SALKELEFKLVASQEdvsKLSTLKFECKNLWDRVENLQVLLDRATDQADKAIlvlEQNQELRKKVDMLEESLEE--ANVY 374
Cdd:TIGR04523 454 LIIKNLDNTRESLET---QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN---EEKKELEEKVKDLTKKISSlkEKIE 527
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1847837041 375 KLSSEKMQQYNDLMQKKIKL-----------LEERLDRSDEEIlSYVKLYQESIKEFQDTLNNL--KEESKRRALNE 438
Cdd:TIGR04523 528 KLESEKKEKESKISDLEDELnkddfelkkenLEKEIDEKNKEI-EELKQTQKSLKKKQEEKQELidQKEKEKKDLIK 603
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
887-1000 |
7.70e-10 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 57.69 E-value: 7.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 887 IYAASDMFLIPSMFEPCGLTQMIAMRYGSIPIARKTGGLNDSVFDvdddtiplqFRNGYTFLNPDEQGLNGALERAFNHY 966
Cdd:COG0438 17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIED---------GETGLLVPPGDPEALAEAILRLLEDP 87
|
90 100 110
....*....|....*....|....*....|....
gi 1847837041 967 KTnKESWQKLVKKDMNIDFSWESSALQYEEIYEK 1000
Cdd:COG0438 88 EL-RRRLGEAARERAEERFSWEAIAERLLALYEE 120
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
818-931 |
9.75e-10 |
|
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340816 [Multi-domain] Cd Length: 235 Bit Score: 60.11 E-value: 9.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 818 CIARLVPQKGIHLIRHAI--YRTLELGGQFVLLGSSPVPhiQVEFEGIANHFKGDDHIRLILKYDESLSHSIYAASDMFL 895
Cdd:cd01635 115 SVGRLVPEKGIDLLLEALalLKARLPDLVLVLVGGGGER--EEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFV 192
|
90 100 110
....*....|....*....|....*....|....*.
gi 1847837041 896 IPSMFEPCGLTQMIAMRYGSIPIARKTGGLNDSVFD 931
Cdd:cd01635 193 LPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVD 228
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
184-434 |
1.36e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 184 EINILEMRLAETNARIKVAAQEKIHVEI-------------LEEQLVNLRNELSHRGVTEgsgadMHENWnkafdgvhsl 250
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKvlkkeseliklkeLAEQLKELEEKLKKYNLEE-----LEKKA---------- 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 251 gKELSLLRTENVSLKDDILALKEELSHVQKTDKRVVMLEKERSFLESALKELEFKL----VASQEDV-SKLSTLK----- 320
Cdd:PRK03918 525 -EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELeelgFESVEELeERLKELEpfyne 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 321 -FECKNLWDRVENLQVLLDRATDQADKAIlvlEQNQELRKKVDMLEESLEEANVyKLSSEKMQQYNDLMQKkiklLEERL 399
Cdd:PRK03918 604 yLELKDAEKELEREEKELKKLEEELDKAF---EELAETEKRLEELRKELEELEK-KYSEEEYEELREEYLE----LSREL 675
|
250 260 270
....*....|....*....|....*....|....*
gi 1847837041 400 DRSDEEIlsyvKLYQESIKEFQDTLNNLKEESKRR 434
Cdd:PRK03918 676 AGLRAEL----EELEKRREEIKKTLEKLKEELEER 706
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
813-965 |
5.64e-09 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 55.60 E-value: 5.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 813 RPLVGCIARLVP-QKGIHLIRHAIYRTLELGG--QFVLLGSSPVPHIQVEFEGIAN--HFKGddHIRLILKYdeslshsi 887
Cdd:pfam13692 1 RPVILFVGRLHPnVKGVDYLLEAVPLLRKRDNdvRLVIVGDGPEEELEELAAGLEDrvIFTG--FVEDLAEL-------- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1847837041 888 YAASDMFLIPSMFEPCGLTQMIAMRYGsIP-IARKTGGLNDSVFDVdddtiplqfrNGYTFLNPDEQGLNGALERAFNH 965
Cdd:pfam13692 71 LAAADVFVLPSLYEGFGLKLLEAMAAG-LPvVATDVGGIPELVDGE----------NGLLVPPGDPEALAEAILRLLED 138
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
315-418 |
9.00e-09 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 55.00 E-value: 9.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 315 KLSTLKFECKNLWDRVENLQ----VLLDRATDQADKAILVLEQNQELRKKVDMLEESLEEANVYKLSSEKMQQYNDLMQK 390
Cdd:pfam12718 1 KMNSLKLEAENAQERAEELEekvkELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLTR 80
|
90 100
....*....|....*....|....*....
gi 1847837041 391 KIKLLEERLDRSDEEILSYV-KLYQESIK 418
Cdd:pfam12718 81 KIQLLEEELEESDKRLKETTeKLRETDVK 109
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
797-995 |
9.10e-09 |
|
sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.
Pssm-ID: 340830 [Multi-domain] Cd Length: 398 Bit Score: 58.79 E-value: 9.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 797 KEALRKHLGLsyaDTRRPLVGCIARLVPQKGIH-LIRhAIYRTLELGGQFVLL---GSSPVPHIQVEFE--GIANHFKGD 870
Cdd:cd03800 207 AEARRARLLL---PPDKPVVLALGRLDPRKGIDtLVR-AFAQLPELRELANLVlvgGPSDDPLSMDREElaELAEELGLI 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 871 DHIRLILKYDESLSHSIYAASDMFLIPSMFEPCGLTQMIAMRYGSIPIARKTGGLNDSVFDVdddtiplqfRNGYtFLNP 950
Cdd:cd03800 283 DRVRFPGRVSRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDG---------RTGL-LVDP 352
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1847837041 951 -DEQGLNGALERAFnhykTNKESWQKLvkKDMNID-----FSWESSALQYE 995
Cdd:cd03800 353 hDPEALAAALRRLL----DDPALWQRL--SRAGLErarahYTWESVADQLL 397
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
141-419 |
9.35e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 9.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 141 FQLEDLVGMLKNAEKNILLLNQARV-RALQDLEKILTEKDALQGEINILEMRLAETNARIKVAAQEKIHVEILEEQLVNL 219
Cdd:PRK03918 496 IKLKELAEQLKELEEKLKKYNLEELeKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 220 RNELSHRGVtegsgadmhenwnKAFDGVHSLGKELSLLRTENVSLKDDILALKEELSHVQKTDKRVVMLEKERSFLESAL 299
Cdd:PRK03918 576 LKELEELGF-------------ESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 300 KELEFKLvasqEDVSKLSTLKfECKNLWDRVENLQVLLDRATdqadkailvlEQNQELRKKVDMLEESLEEanvYKLSSE 379
Cdd:PRK03918 643 EELRKEL----EELEKKYSEE-EYEELREEYLELSRELAGLR----------AELEELEKRREEIKKTLEK---LKEELE 704
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1847837041 380 KMQQYndlmQKKIKLLEERLDRSdEEILSYVKLYQESIKE 419
Cdd:PRK03918 705 EREKA----KKELEKLEKALERV-EELREKVKKYKALLKE 739
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
143-437 |
1.36e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 143 LEDLVGMLKNAEKNILLLNQARVRALQDLEKILTEKDALQGEINILEMRLAETNARIKvAAQEKIHVeiLEEQLVNLRNE 222
Cdd:TIGR02169 711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE-ELEEDLHK--LEEALNDLEAR 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 223 LSHRGVTEGSGA-----DMHENWNKAFDGV----HSLGKELSLLRTENVSLKDDILALKEELSHVQKT------------ 281
Cdd:TIGR02169 788 LSHSRIPEIQAElskleEEVSRIEARLREIeqklNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEienlngkkeele 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 282 -------------DKRVVMLEKERSFLESALKELEFKLVASQEDVSKLStlkfecKNLWDRVENLQVLLDRATDQADK-- 346
Cdd:TIGR02169 868 eeleeleaalrdlESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR------KRLSELKAKLEALEEELSEIEDPkg 941
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 347 -------AILVLEQNQELRKKVDMLEESLEEANV-----YKlssEKMQQYNDLMQKKIKLLEERldrsdeeilsyvklyq 414
Cdd:TIGR02169 942 edeeipeEELSLEDVQAELQRVEEEIRALEPVNMlaiqeYE---EVLKRLDELKEKRAKLEEER---------------- 1002
|
330 340
....*....|....*....|...
gi 1847837041 415 ESIKEFQDTLNNLKEESKRRALN 437
Cdd:TIGR02169 1003 KAILERIEEYEKKKREVFMEAFE 1025
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
813-964 |
6.32e-08 |
|
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.
Pssm-ID: 425737 [Multi-domain] Cd Length: 158 Bit Score: 53.05 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 813 RPLVGCIARLVPQKGIHLIRHAIYRTLELGGQFVLL--GSSPVPHiqvEFEGIANHFKGDDHIRLILKYDESLSHSIYAA 890
Cdd:pfam00534 2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLViaGDGEEEK---RLKKLAEKLGLGDNVIFLGFVSDEDLPELLKI 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1847837041 891 SDMFLIPSMFEPCGLTQMIAMRYGSIPIARKTGGLNDSVFDvdddtiplqFRNGYTFLNPDEQGLNGALERAFN 964
Cdd:pfam00534 79 ADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKD---------GETGFLVKPNNAEALAEAIDKLLE 143
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
121-443 |
1.33e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.89 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 121 VSEEMTPLGINVKSGEQLSSfqleDLVGMLKNAEKNILLLN------QARVR-ALQDLEKILTEKDAL---QGEINILEM 190
Cdd:pfam15921 480 VVEELTAKKMTLESSERTVS----DLTASLQEKERAIEATNaeitklRSRVDlKLQELQHLKNEGDHLrnvQTECEALKL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 191 RLAEtnarikvaaQEKIhVEILEEQLVNLRNELSHRGVTegSGADMHEnwnKAfdgvhSLGKELSLLRTENVSLKddILA 270
Cdd:pfam15921 556 QMAE---------KDKV-IEILRQQIENMTQLVGQHGRT--AGAMQVE---KA-----QLEKEINDRRLELQEFK--ILK 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 271 LKEElSHVQKTDKRVVMLEKERSFLESALKE--------------LEFKLVASQEDVSKLSTlKFEC--KNLWDRVENLQ 334
Cdd:pfam15921 614 DKKD-AKIRELEARVSDLELEKVKLVNAGSErlravkdikqerdqLLNEVKTSRNELNSLSE-DYEVlkRNFRNKSEEME 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 335 VLLDRATDQADKAILVLEQNqelRKKVDMLEESleEANVYKLSSEKMQQYN------DLMQKKIKLLEERLDRSDEEiLS 408
Cdd:pfam15921 692 TTTNKLKMQLKSAQSELEQT---RNTLKSMEGS--DGHAMKVAMGMQKQITakrgqiDALQSKIQFLEEAMTNANKE-KH 765
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1847837041 409 YVKLYQESIKEFQDTLNNLKEE---------SKRRALNEPVDDM 443
Cdd:pfam15921 766 FLKEEKNKLSQELSTVATEKNKmagelevlrSQERRLKEKVANM 809
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
539-1000 |
1.59e-07 |
|
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.
Pssm-ID: 340844 [Multi-domain] Cd Length: 372 Bit Score: 54.59 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 539 LSRALQKKGHLVEIVLPKYDcmqydhirdlrvldmELESYFDGrlfrnkvwvgtveglPVYFIEPHHPSKFFWRGTVYGe 618
Cdd:cd03817 23 LARALEKRGHEVYVITPSDP---------------GAEDEEEV---------------VRYRSFSIPIRKYHRQHIPFP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 619 hddfRRFSYFSRAALelllqagKKPDIIHCHdwqTAFVAPLYWdLYAPKGLNsARICFTCHnfeyqgTAPASemascglD 698
Cdd:cd03817 72 ----FKKAVIDRIKE-------LGPDIIHTH---TPFSLGKLG-LRIARKLK-IPIVHTYH------TMYED-------Y 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 699 VHHLNRPDRmqdnsahdRVNPVKGAIV--FSN---IVTTVSPTYAQEVRTSEGGRglhstlnshsKKFIgILNGIDTDAW 773
Cdd:cd03817 123 LHYIPKGKL--------LVKAVVRKLVrrFYNhtdAVIAPSEKIKDTLREYGVKG----------PIEV-IPNGIDLDKF 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 774 dpatdvylksqfnandlqgKAENKEALRKHLGLsyaDTRRPLVGCIARLVPQKGIHLIRHAIYRTLELGG-QFVLLGSSP 852
Cdd:cd03817 184 -------------------EKPLNTEERRKLGL---PPDEPILLYVGRLAKEKNIDFLLRAFAELKKEPNiKLVIVGDGP 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 853 VPHiqvEFEGIANHFKGDDHIRLI--LKYDEsLSHsIYAASDMFLIPSMFEPCGLTQMIAMRYGsIP-IARKTGGLNDSV 929
Cdd:cd03817 242 ERE---ELKELARELGLADKVIFTgfVPREE-LPE-YYKAADLFVFASTTETQGLVYLEAMAAG-LPvVAAKDPAASELV 315
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1847837041 930 FDVDddtiplqfrNGYTFLNPDEqglngALERAFNHYKTNKESWQKLVKKDMNI--DFsweSSALQYEEIYEK 1000
Cdd:cd03817 316 EDGE---------NGFLFEPNDE-----TLAEKLLHLRENLELLRKLSKNAEISarEF---AFAKSVEKLYEE 371
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
767-929 |
2.26e-07 |
|
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.
Pssm-ID: 340842 [Multi-domain] Cd Length: 365 Bit Score: 54.22 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 767 GIDTDAWDPATdvylKSQfnandlqgkaenkeALRKHLGlsyaDTRRPLVGCIARLVPQKGIHLIRHAIYR-TLELGGQF 845
Cdd:cd03814 174 GVDTELFHPSR----RDA--------------ALRRRLG----PPGRPLLLYVGRLAPEKNLEALLDADLPlAASPPVRL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 846 VLLGSSPVPHiQVEFEGIANHFKGddhirliLKYDESLShSIYAASDMFLIPSMFEPCGLTQMIAMRYGsIP-IARKTGG 924
Cdd:cd03814 232 VVVGDGPARA-ELEARGPDVIFTG-------FLTGEELA-RAYASADVFVFPSRTETFGLVVLEAMASG-LPvVAADAGG 301
|
....*
gi 1847837041 925 LNDSV 929
Cdd:cd03814 302 PRDIV 306
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
150-432 |
2.54e-07 |
|
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: 54.64 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 150 LKNAEKNILLLNQARVRALQDLEKILTEKDALQGEINILEMRLAETNARIKvaaQEKIHVEILEEQLVNLRNELshrgvt 229
Cdd:TIGR04523 414 IKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE---SLETQLKVLSRSINKIKQNL------ 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 230 egsgadmhENWNKAFDgvhSLGKELSLLRTENVSLKDDILALKEELSHVQKTDKRvvmLEKERSFLESALKELEFKLVaS 309
Cdd:TIGR04523 485 --------EQKQKELK---SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK---LESEKKEKESKISDLEDELN-K 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 310 QEDVSKLSTLKFECKNLWDRVENL---QVLLDRATDQADKAILVLEQNQ-ELRKKVDMLEESLEEANvYKLSSEKMQQyn 385
Cdd:TIGR04523 550 DDFELKKENLEKEIDEKNKEIEELkqtQKSLKKKQEEKQELIDQKEKEKkDLIKEIEEKEKKISSLE-KELEKAKKEN-- 626
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1847837041 386 dlmqKKIKLLEERLDRSDEEILSYVKLYQESIKEFQDTLNNLKEESK 432
Cdd:TIGR04523 627 ----EKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIK 669
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
151-430 |
3.27e-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: 54.68 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 151 KNAEKNIlllnqARVRA-LQDLEKILTEkdaLQGEINILEM--RLAETNARIKvAAQEKIHVEILEEQLVNLRNELSHRG 227
Cdd:TIGR02168 175 KETERKL-----ERTREnLDRLEDILNE---LERQLKSLERqaEKAERYKELK-AELRELELALLVLRLEELREELEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 228 VTEGSGADMHENWNKAFDGVHSlgkELSLLRTENVSLKDDILALKEEL----SHVQKTDKRVVMLEKERSFLESALKELE 303
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEE---KLEELRLEVSELEEEIEELQKELyalaNEISRLEQQKQILRERLANLERQLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 304 FKLvasQEDVSKLSTLKFECKNLWDRVENLQVLLDRATDQADKAIlvlEQNQELRKKVDMLEESLEEAN--VYKLSSEKM 381
Cdd:TIGR02168 323 AQL---EELESKLDELAEELAELEEKLEELKEELESLEAELEELE---AELEELESRLEELEEQLETLRskVAQLELQIA 396
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1847837041 382 QQYNDL--MQKKIKLLEERLDRSDEEILSYVKLYQES-IKEFQDTLNNLKEE 430
Cdd:TIGR02168 397 SLNNEIerLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEE 448
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
573-994 |
3.93e-07 |
|
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.
Pssm-ID: 340846 [Multi-domain] Cd Length: 345 Bit Score: 53.13 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 573 MELESYFDGRLFRnkVWVGTVEGlpvyfiePHHPskffwRGTVYGEHDDFRRFSYFSRAALELLLQ---AGKKPDIIHCH 649
Cdd:cd03819 18 LDLARALAERGHR--VLVVTAGG-------PLLP-----RLRQIGIGLPGLKVPLLRALLGNVRLArliRRERIDLIHAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 650 dwqTAFVAPLYWDLyapKGLNSARICFTCHN---FEYQGTAPASEMascgldvhhLNRPDRmqdnsahdrvnpvkgAIVF 726
Cdd:cd03819 84 ---SRAPAWLGWLA---SRLTGVPLVTTVHGsylATYHPKDFALAV---------RARGDR---------------VIAV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 727 SNivttvsptYAQEVRTSEGGRGLhstlnshsKKFIGILNGIDTDAWDPatdvylksqfnandlqgkaENKEALRKHLGL 806
Cdd:cd03819 134 SE--------LVRDHLIEALGVDP--------ERIRVIPNGVDTDRFPP-------------------EAEAEERAQLGL 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 807 syaDTRRPLVGCIARLVPQKGIHLIRHAIYRtLELGGQFVLLGSSPVP-----HIQVEFEGIANHFKGDDHIRLIlkyde 881
Cdd:cd03819 179 ---PEGKPVVGYVGRLSPEKGWLLLVDAAAE-LKDEPDFRLLVAGDGPerdeiRRLVERLGLRDRVTFTGFREDV----- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 882 slsHSIYAASDMFLIPSMFEPCGLTQMIAMRYGSIPIARKTGGLNDSVfdvdddtipLQFRNGYTFLNPDEQGLNGALER 961
Cdd:cd03819 250 ---PAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIV---------VHGRTGLLVPPGDAEALADAIRA 317
|
410 420 430
....*....|....*....|....*....|...
gi 1847837041 962 AfnhyKTNKESWQKLVKKDMNIDfSWESSALQY 994
Cdd:cd03819 318 A----KLLPEAREKLQAAAALTE-AVRELLLRV 345
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
142-356 |
6.65e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 142 QLEDLVGMLKNAEKNIlllnQARVRALQ-DLEKILTEKDALQGEINILEMRLAETNARIKvAAQEKI--HVEILEEQLVN 218
Cdd:COG3883 20 AKQKELSELQAELEAA----QAELDALQaELEELNEEYNELQAELEALQAEIDKLQAEIA-EAEAEIeeRREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 219 LRNELSHRGVTE---GSgadmhENWNKAFDGVHSLGKelslLRTENVSLKDDILALKEELSHVQ-KTDKRVVMLEKERSF 294
Cdd:COG3883 95 LYRSGGSVSYLDvllGS-----ESFSDFLDRLSALSK----IADADADLLEELKADKAELEAKKaELEAKLAELEALKAE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1847837041 295 LESALKELEfKLVASQEdvSKLSTLKFECKNLWDRVENLQVLLDRATDQADKAILVLEQNQE 356
Cdd:COG3883 166 LEAAKAELE-AQQAEQE--ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
142-370 |
1.04e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 142 QLEDLVGMLKNAEKNILLLNQARVRALQDLEKILTEKDALQGEINILEMRLAETNARIK--------------------- 200
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlerqleeleaqleeleskld 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 201 -----VAAQEKIhVEILEEQLVNLRNELSHRgvtEGSGADMHENWNKAFDGVHSLGKELSLLRTENVSLKDDILALKEEL 275
Cdd:TIGR02168 334 elaeeLAELEEK-LEELKEELESLEAELEEL---EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 276 SHVQKTDKRvvmLEKERSFLESALKELEFKLVASQedvskLSTLKFECKNLWDRVENLQVLLDRATDQADKAILVL---- 351
Cdd:TIGR02168 410 ERLEDRRER---LQQEIEELLKKLEEAELKELQAE-----LEELEEELEELQEELERLEEALEELREELEEAEQALdaae 481
|
250
....*....|....*....
gi 1847837041 352 EQNQELRKKVDMLEESLEE 370
Cdd:TIGR02168 482 RELAQLQARLDSLERLQEN 500
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
166-438 |
1.20e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 166 RALQDLEKILTEKDALQGEINILEMRLAETNARIKVAAQEkihVEILEEQLVNLRNELSHRGVTEGSGADMHENWNKAFD 245
Cdd:PRK02224 346 SLREDADDLEERAEELREEAAELESELEEAREAVEDRREE---IEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 246 GVHSLGKELSL-LRT--ENVSLKDDILALK---------EELSHVQKTDKRvvmlEKERSFLESALKELEFKLVASQEDV 313
Cdd:PRK02224 423 ELREREAELEAtLRTarERVEEAEALLEAGkcpecgqpvEGSPHVETIEED----RERVEELEAELEDLEEEVEEVEERL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 314 SKLSTLKFECKNLWDRVENLQVLLDRATDQADKAILVLEQNQELRKKVDMLEESLEEANvyKLSSEKMQQYNDlMQKKIK 393
Cdd:PRK02224 499 ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKR--EAAAEAEEEAEE-AREEVA 575
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1847837041 394 LLEERLDRSDEEI--LSYVKLYQESIKEFQDTLNNLKEesKRRALNE 438
Cdd:PRK02224 576 ELNSKLAELKERIesLERIRTLLAAIADAEDEIERLRE--KREALAE 620
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
530-771 |
3.37e-06 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 48.30 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 530 GGLGDVVSGLSRALQKKGHLVEIVLPKYDcmqydhirdlrvldmelesyfdGRLFRNKVWVGTVEGLPVYFiephhpskf 609
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGP----------------------GPLAEEVVRVVRVPRVPLPL--------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 610 fwrgtvygeHDDFRRFSYFSRAALELLLQAgkKPDIIHCHDWqtafvAPLYWDLYAPKGLNSARICFTCHNFEYQGTAPa 689
Cdd:pfam13439 50 ---------PPRLLRSLAFLRRLRRLLRRE--RPDVVHAHSP-----FPLGLAALAARLRLGIPLVVTYHGLFPDYKRL- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 690 semascGLDVHHLNRPDRMQDNSAHDRVnpvkgaivfsNIVTTVSPTYAQEvrtseggrgLHSTLNSHSKKFIGILNGID 769
Cdd:pfam13439 113 ------GARLSPLRRLLRRLERRLLRRA----------DRVIAVSEAVADE---------LRRLYGVPPEKIRVIPNGVD 167
|
..
gi 1847837041 770 TD 771
Cdd:pfam13439 168 LE 169
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
142-446 |
4.34e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 142 QLEDLVGMLKNAEKNILLLNQARVRALQDLEKILTEKDALQGEINILEMRLAETNARIKVAAQEKIHVEILEEQLVNLRN 221
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 222 ELSHRGVtegsgadmhenwnkafdgvhSLGKELSLLRTENVSLKDDILALKEELSHVQKTDKRVV--MLEKERSfLESAL 299
Cdd:COG1196 327 ELEEELE--------------------ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEaeLAEAEEE-LEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 300 KELEFKLVASQEDVSKLSTLKFECKNLWDRVENLQV-LLDRATDQADKAILVLEQNQELRKKVDMLEESLEEANVYKLSS 378
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEeLEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1847837041 379 EKMQQYNDLMQKKIKLLEERLDRSDEEILSYVKLYQESIKEFQDTLnNLKEESKRRALNEPVDDMPWD 446
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK-AALLLAGLRGLAGAVAVLIGV 532
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
171-443 |
5.70e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 171 LEKILTEKDALQGEINILEMRLAETNARIKVAAQekihVEILEEQLVNLRNELshrgvtegsgADMHENWNKAFDGVHSL 250
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERLERAEDLVEAEDR----IERLEERREDLEELI----------AERRETIEEKRERAEEL 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 251 GKELSLLRTENVSLKDDILALKEElshVQKTDKRVVMLEKERSFLESALKELEfKLVASQEDVSklstlkfeckNLWDRV 330
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEE---AEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIA----------DAEDEI 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 331 ENLQvllDRATDQADKAILVLEQNQELRKKVDMLEESLEEANVYKLSSEKMQ--QYNDLMQKKIKLLEERLDrsdeEILS 408
Cdd:PRK02224 609 ERLR---EKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERaeEYLEQVEEKLDELREERD----DLQA 681
|
250 260 270
....*....|....*....|....*....|....*
gi 1847837041 409 YVKLYQESIKEfqdtLNNLKEEskRRALNEPVDDM 443
Cdd:PRK02224 682 EIGAVENELEE----LEELRER--REALENRVEAL 710
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
203-438 |
5.98e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 203 AQEKIhvEILEEQLVNLRNELShrgVTEGSGADMhENWNKAFDGVHSLGKELSLLRTENV---SLKDDILALKEELSHVQ 279
Cdd:COG4913 608 NRAKL--AALEAELAELEEELA---EAEERLEAL-EAELDALQERREALQRLAEYSWDEIdvaSAEREIAELEAELERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 280 KTDKRVVMLEKERSFLESALKELEFKLVASQEDVSKLStlkfecknlwDRVENLQVLLDRATDQADKAILVLEQNQELRk 359
Cdd:COG4913 682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE----------KELEQAEEELDELQDRLEAAEDLARLELRAL- 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 360 kvdmLEESLEEANVYKLSSEKMQQYndlmQKKIKLLEERLDRSDEEILSYVKLYQ--------------ESIKEFQDTLN 425
Cdd:COG4913 751 ----LEERFAAALGDAVERELRENL----EERIDALRARLNRAEEELERAMRAFNrewpaetadldadlESLPEYLALLD 822
|
250 260
....*....|....*....|
gi 1847837041 426 NLKE------ESK-RRALNE 438
Cdd:COG4913 823 RLEEdglpeyEERfKELLNE 842
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
152-400 |
6.00e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.56 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 152 NAEKNIL---------LLNQA---RVRAL---QDLEKILTEkdalqgeiniLEMRLAETNARIKVAAQEK----IHVEIL 212
Cdd:pfam01576 39 CEEKNALqeqlqaeteLCAEAeemRARLAarkQELEEILHE----------LESRLEEEEERSQQLQNEKkkmqQHIQDL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 213 EEQLVN---LRNELSHRGVT-EGSGADMHENWNKAFDGVHSLGKELSLLRtENVSLKDDILALKEELS-HVQK-TDKRVV 286
Cdd:pfam01576 109 EEQLDEeeaARQKLQLEKVTtEAKIKKLEEDILLLEDQNSKLSKERKLLE-ERISEFTSNLAEEEEKAkSLSKlKNKHEA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 287 ML----------EKERSFLESALKELEFKLVASQEDVSKLSTLKFECK-NLWDRVENLQVLLDRATDQADKAILVLEQNQ 355
Cdd:pfam01576 188 MIsdleerlkkeEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRaQLAKKEEELQAALARLEEETAQKNNALKKIR 267
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1847837041 356 ELRKKVDMLEESLEEANVYKLSSEKmqQYNDLMQKKIKL---LEERLD 400
Cdd:pfam01576 268 ELEAQISELQEDLESERAARNKAEK--QRRDLGEELEALkteLEDTLD 313
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
142-371 |
6.80e-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: 49.38 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 142 QLEDLVGMLKNAEKNILLLNQARVRALQDLEKILTEKDALQGEINILEMRLAETNARIKVAAQE----KIHVEILEEQLV 217
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaelEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 218 NLRNELSHRGVTegsgADMHENWNK-----AFDGVHSLGKELSLLRTENVSLKDDILALKEELSHVQKTDKRvvmLEKER 292
Cdd:COG4942 101 AQKEELAELLRA----LYRLGRQPPlalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE---LEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 293 SFLESALKELefklvasQEDVSKLSTLKfecknlwDRVENLQVLLDRATDQADKAILVLEQN-QELRKKVDMLEESLEEA 371
Cdd:COG4942 174 AELEALLAEL-------EEERAALEALK-------AERQKLLARLEKELAELAAELAELQQEaEELEALIARLEAEAAAA 239
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
143-443 |
1.08e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 143 LEDLVGMLKNAEKNILLLNQARVRALQDLEKILTEKDALQGEINILEMRLAETNARIKVAAQEkihVEILEEQLVNLRNE 222
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE---VEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 223 LshrgvtegsgADMHENWNKAFDGVHSLGKELSLLRTENVSLKDDILALKEELSHvqktdkrvvmlekersfLESALKEL 302
Cdd:TIGR02168 756 L----------TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA-----------------LREALDEL 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 303 EfklvasqedvSKLSTLKfecknlwdrvENLQVLLDRATDQADKAILVLEQNQELRKKVDMLEESLEEANvykLSSEKMQ 382
Cdd:TIGR02168 809 R----------AELTLLN----------EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA---AEIEELE 865
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1847837041 383 QYNDLMQKKIKLLEERLDRSDEEILSYVKLYQESIKEFQDTLNNLKE-ESKRRALNEPVDDM 443
Cdd:TIGR02168 866 ELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSElRRELEELREKLAQL 927
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
143-430 |
1.77e-05 |
|
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: 48.91 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 143 LEDLVGMLKNAEKNILLLNQARVRA-LQDLEKILT----EKDALQGEINILEMRLAETNARIK-------VAAQEKIHVe 210
Cdd:TIGR02169 220 KREYEGYELLKEKEALERQKEAIERqLASLEEELEklteEISELEKRLEEIEQLLEELNKKIKdlgeeeqLRVKEKIGE- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 211 iLEEQLVNLRNELShrgVTEGSGADMHENWNKAFDGVHSLGKELSLLRTENVSLKDDILALKEELSHvqktdkrvvmLEK 290
Cdd:TIGR02169 299 -LEAEIASLERSIA---EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE----------LKE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 291 ERSFLESALKELEfklVASQEDVSKLSTLKFECKNLWDRVENLQVLLDRatdqadkailVLEQNQELRKKVDMLEESLE- 369
Cdd:TIGR02169 365 ELEDLRAELEEVD---KEFAETRDELKDYREKLEKLKREINELKRELDR----------LQEELQRLSEELADLNAAIAg 431
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1847837041 370 -EANVYKLSSEKmqqynDLMQKKIKLLEERLDRSDEEILSYVKLY---QESIKEFQDTLNNLKEE 430
Cdd:TIGR02169 432 iEAKINELEEEK-----EDKALEIKKQEWKLEQLAADLSKYEQELydlKEEYDRVEKELSKLQRE 491
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
171-430 |
1.91e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 171 LEKILTEKDALQGEINILEMRLAETNARIKVAAQEKihvEILEEQLVNLRNELshrgvtegsgADMHENWNKAFDGVHSL 250
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKR---DELNAQVKELREEA----------QELREKRDELNEKVKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 251 GKELSLLRTENVSLKDDILALKEELSHVQKTDKRVVMLEKErsflesaLKELEFKLvasqeDVSKLSTLKfEcKNLWDRV 330
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKE-------IERLEWRQ-----QTEVLSPEE-E-KELVEKI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 331 ENLQVLLDRAtdqaDKAILVLEQNQELRKKVDMLEESLEEAN--VYKLSsEKMQQYNDLMQKKIKLLEERLDRSDEeils 408
Cdd:COG1340 143 KELEKELEKA----KKALEKNEKLKELRAELKELRKEAEEIHkkIKELA-EEAQELHEEMIELYKEADELRKEADE---- 213
|
250 260
....*....|....*....|..
gi 1847837041 409 yvklYQESIKEFQDTLNNLKEE 430
Cdd:COG1340 214 ----LHKEIVEAQEKADELHEE 231
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
166-370 |
2.16e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 166 RALQDLEKILTEKDALQGEINILEMRLAETNARIkvaaqekihvEILEEQLVNLRNELShrgvtegsgadmhenwnkafd 245
Cdd:COG1579 7 RALLDLQELDSELDRLEHRLKELPAELAELEDEL----------AALEARLEAAKTELE--------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 246 gvhSLGKELSLLRTENVSLKDDILALKEELSHVQKTD------KRVVMLEKERSFLESALKELEFKLVASQEDVSKLStl 319
Cdd:COG1579 56 ---DLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyealqKEIESLKRRISDLEDEILELMERIEELEEELAELE-- 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1847837041 320 kfecknlwDRVENLQVLLDRATDQADKAILVLEQN-QELRKKVDMLEESLEE 370
Cdd:COG1579 131 --------AELAELEAELEEKKAELDEELAELEAElEELEAEREELAAKIPP 174
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
142-316 |
2.39e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 142 QLEDLVGMLKNAEKNILLLNQARVRALQDLEKILTEKDALQGEINILEMRLAETNARIKVaaqekihveiLEEQLVNLRN 221
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK----------YEEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 222 elshrgvtegsgadmhenwNKAFDgvhSLGKELSLLRTENVSLKDDILALKEELSHVQKTDKRV-VMLEKERSFLESALK 300
Cdd:COG1579 88 -------------------NKEYE---ALQKEIESLKRRISDLEDEILELMERIEELEEELAELeAELAELEAELEEKKA 145
|
170
....*....|....*.
gi 1847837041 301 ELEFKLVASQEDVSKL 316
Cdd:COG1579 146 ELDEELAELEAELEEL 161
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
252-439 |
3.17e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 252 KELSLLRTENVSLKDDILALKEELSHVQKTDKRVVMLEKERSFLESALKELEFKLVASQEdvsKLSTLKFECKNLWDRVE 331
Cdd:PRK03918 207 REINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE---RIEELKKEIEELEEKVK 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 332 NLQVLLDRATDQADKAILVLEQNQELRkKVDMLEESLEE--ANVYKLSSEKMQQYNDLmqKKIKLLEERLDRSDEEILSY 409
Cdd:PRK03918 284 ELKELKEKAEEYIKLSEFYEEYLDELR-EIEKRLSRLEEeiNGIEERIKELEEKEERL--EELKKKLKELEKRLEELEER 360
|
170 180 190
....*....|....*....|....*....|
gi 1847837041 410 VKLYQEsIKEFQDTLNNLKeesKRRALNEP 439
Cdd:PRK03918 361 HELYEE-AKAKKEELERLK---KRLTGLTP 386
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
758-999 |
4.61e-05 |
|
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.
Pssm-ID: 340836 [Multi-domain] Cd Length: 362 Bit Score: 46.93 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 758 SKKFIGILNGIDTDawdpatdvylksqfnanDLQGKAENKEALRKHLGLSyADTRrpLVGCIARLVPQKGIHLIRHAIYR 837
Cdd:cd03807 155 KNKIVVIYNGIDLF-----------------KLSPDDASRARARRRLGLA-EDRR--VIGIVGRLHPVKDHSDLLRAAAL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 838 TLELGGQ--FVLLGSSPV-PHIQVEFE--GIANHFK----GDDHIRLilkydeslshsiYAASDMFLIPSMFEPCGLTQM 908
Cdd:cd03807 215 LVETHPDlrLLLVGRGPErPNLERLLLelGLEDRVHllgeRSDVPAL------------LPAMDIFVLSSRTEGFPNALL 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 909 IAMRYGsIP-IARKTGGLNDSvfdVDDDTiplqfrnGYTFLNPDEQGLNGALERAFNHyktnKESWQKLVKKD---MNID 984
Cdd:cd03807 283 EAMACG-LPvVATDVGGAAEL---VDDGT-------GFLVPAGDPQALADAIRALLED----PEKRARLGRAArerIANE 347
|
250
....*....|....*
gi 1847837041 985 FSWESSALQYEEIYE 999
Cdd:cd03807 348 FSIDAMVRRYETLYY 362
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
104-436 |
6.33e-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: 47.27 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 104 SHIAIEHINDNPLKHLTVSEEMTPLGINVKSGEQLSSFQLEDLVGMLKNAEKNILLLNQARVRA-LQDLEKILTEKDALQ 182
Cdd:pfam02463 731 QDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEkLKAQEEELRALEEEL 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 183 GEINILEMRLAETNARIKVAAQEKIHVEILEEQLVNLRNELshrgvtegsgADMHENWNKAFDGVHSLGKELSLLRtenv 262
Cdd:pfam02463 811 KEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKL----------AEEELERLEEEITKEELLQELLLKE---- 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 263 sLKDDILALKEELSHVQKTDKrvvMLEKERSFLESALKELEFKLVASQEDvSKLSTLKFECKNLWDRVENLQVLLDRATD 342
Cdd:pfam02463 877 -EELEEQKLKDELESKEEKEK---EEKKELEEESQKLNLLEEKENEIEER-IKEEAEILLKYEEEPEELLLEEADEKEKE 951
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 343 QADKAILVLEQNQELRKKvdmLEESLEEANVYKLSSEKMQQYNDLMQKKIKLLEERLDRSDEEILSYVKLYQESIKEFQD 422
Cdd:pfam02463 952 ENNKEEEEERNKRLLLAK---EELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVS 1028
|
330
....*....|....
gi 1847837041 423 TLNNLKEESKRRAL 436
Cdd:pfam02463 1029 INKGWNKVFFYLEL 1042
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
729-914 |
1.01e-04 |
|
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.
Pssm-ID: 340826 [Multi-domain] Cd Length: 355 Bit Score: 45.73 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 729 IVTTvSPTYaqeVRTSEggrglhsTLNSHSKKFIGILNGIDtdawdpatdvylKSQFNANDLQGKAENKEALRKHLGLSy 808
Cdd:cd03795 141 IIAT-SPNY---VETSP-------TLREFKNKVRVIPLGID------------KNVYNIPRVDFENIKREKKGKKIFLF- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 809 adtrrplvgcIARLVPQKGIH-LIRHAIYRTLELggqfVLLGSSPvphIQVEFEGIAnHFKGDDHIRLILKYDESLSHSI 887
Cdd:cd03795 197 ----------IGRLVYYKGLDyLIEAAQYLNYPI----VIGGEGP---LKPDLEAQI-ELNLLDNVKFLGRVDDEEKVIY 258
|
170 180
....*....|....*....|....*....
gi 1847837041 888 YAASDMFLIPSMF--EPCGLTQMIAMRYG 914
Cdd:cd03795 259 LHLCDVFVFPSVLrsEAFGIVLLEAMMCG 287
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
513-997 |
1.12e-04 |
|
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.
Pssm-ID: 340828 [Multi-domain] Cd Length: 376 Bit Score: 45.83 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 513 RLHVIHIAaemaPVAKVGGLGDVVSGLSRALQKKGHLVEIVLPkydcmqydhirdlrvldmelESYFDGRLFRNKVWVGT 592
Cdd:cd03798 1 VLILTNIY----PNANSPGRGIFVRRQVRALSRRGVDVEVLAP--------------------APWGPAAARLLRKLLGE 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 593 VEGlPVYFIEPHHpskffWRGTVYGehddfrRFSYFSRAALELLLQA-GKKPDIIHCHdWqtafvapLYWDLYAP---KG 668
Cdd:cd03798 57 AVP-PRDGRRLLP-----LKPRLRL------LAPLRAPSLAKLLKRRrRGPPDLIHAH-F-------AYPAGFAAallAR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 669 LNSARICFTCHNFEYQGTAPASEMAScgLDVHHLNRPDRmqdnsahdrvnpvkgaivfsniVTTVSPTYAQEVRtSEGGR 748
Cdd:cd03798 117 LYGVPYVVTEHGSDINVFPPRSLLRK--LLRWALRRAAR----------------------VIAVSKALAEELV-ALGVP 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 749 GLHSTLnshskkfigILNGIDTDAWDPATDvylksqfnandlqgkaenkealRKHLGLSYadtrrPLVGCIARLVPQKGI 828
Cdd:cd03798 172 RDRVDV---------IPNGVDPARFQPEDR----------------------GLGLPLDA-----FVILFVGRLIPRKGI 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 829 HLIRHAIYRtLELGGQFVLL-----GSSPVPH-IQVEFEGIAN--HFKGddhirlilkydeSLSHS----IYAASDMFLI 896
Cdd:cd03798 216 DLLLEAFAR-LAKARPDVVLlivgdGPLREALrALAEDLGLGDrvTFTG------------RLPHEqvpaYYRACDVFVL 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 897 PSMFEPCGLTQMIAMRYGSIPIARKTGGLNDSVFDVdddtiplqfRNGYTFLNPDEQGLNGALERAfnHYKTNK-ESWQ- 974
Cdd:cd03798 283 PSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDP---------ETGLLVPPGDADALAAALRRA--LAEPYLrELGEa 351
|
490 500
....*....|....*....|....*
gi 1847837041 975 --KLVKKDMNIDFSWESSALQYEEI 997
Cdd:cd03798 352 arARVAERFSWVKAADRIAAAYRDV 376
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
177-303 |
1.36e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 42.63 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 177 EKDALQGEINILEMRLAETNARIKVAAQE-KIHVEILEEQLVNLRNEL-SHrgvtegsGADMhenwnkafdgvhslgKEL 254
Cdd:pfam07926 2 ELSSLQSEIKRLKEEAADAEAQLQKLQEDlEKQAEIAREAQQNYERELvLH-------AEDI---------------KAL 59
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1847837041 255 SLLRTENVSLKDDILALKEELSHVQKT--------DKRVVMLEKERSFLESALKELE 303
Cdd:pfam07926 60 QALREELNELKAEIAELKAEAESAKAEleeseeswEEQKKELEKELSELEKRIEDLN 116
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
266-433 |
1.67e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 266 DDILALKEELSHVQKTDKRVVMLEKERSFLESALKELEFKLVASQEDVSKLSTLKfECKNLWDRVENLQVLLDRATDQAD 345
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 346 KAILVLEQNQELRKKVDMLEESLEEANvyKLSSEKMQQYNDLMQKKIKLLEERLDRSDEEIlsyvKLYQESIKEFQDTLN 425
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQ--EELEELLEQLSLATEEELQDLAEELEELQQRL----AELEEELEEAQEELE 223
|
....*...
gi 1847837041 426 NLKEESKR 433
Cdd:COG4717 224 ELEEELEQ 231
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
142-438 |
1.92e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 142 QLEDLVGMLKNAEKNILLLNqARVRALQDL--------EKILTEKDALQG---EINILEMRLAETNARIKVAAQEKIHVE 210
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIK-RRIERLEKFikrtenieELIKEKEKELEEvlrEINEISSELPELREELEKLEKEVKELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 211 ILEEQLVNLRNELSHRgvtEGSGADMHENWNKAFDGVHSLGKELSLLRtENVS-------LKDDILALKEELShvqKTDK 283
Cdd:PRK03918 235 ELKEEIEELEKELESL---EGSKRKLEEKIRELEERIEELKKEIEELE-EKVKelkelkeKAEEYIKLSEFYE---EYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 284 RVVMLEKERSFLESALKELEFKLVASQEDVSKLSTLKFECKNLWDRVEnlqvlldratdqadkailvleqnqELRKKVDM 363
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE------------------------ELEERHEL 363
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1847837041 364 LEESLE-EANVYKLSSEKMQQYNDLMQKKIKLLEERldrsDEEIlsyvklyQESIKEFQDTLNNLKEESKRR--ALNE 438
Cdd:PRK03918 364 YEEAKAkKEELERLKKRLTGLTPEKLEKELEELEKA----KEEI-------EEEISKITARIGELKKEIKELkkAIEE 430
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
142-430 |
2.67e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 142 QLEDLVGMLKNAEKNILLLNQ--ARVRALQDLEKILTEKDALQGEINILEMRLAETNARIKVAAQEKIHVEILEEQLVNL 219
Cdd:COG4717 96 ELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 220 RNEL-----SHRGVTEGSGADMHENWNKAFDGVHSLGKELSLLRTENVSLKDDILALKEELSHVQKTDKrvvmLEKERSF 294
Cdd:COG4717 176 QEELeelleQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER----LKEARLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 295 LESA-------------------------------------LKELEFKLVASQEDVSKLSTLKFECKNLWDR-VENLQVL 336
Cdd:COG4717 252 LLIAaallallglggsllsliltiagvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEElLAALGLP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 337 LDRATDQADKAILVLEQNQELRKKVDMLEESLEEANVYKLSS------------------EKMQQYNDLmQKKIKLLEER 398
Cdd:COG4717 332 PDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAallaeagvedeeelraalEQAEEYQEL-KEELEELEEQ 410
|
330 340 350
....*....|....*....|....*....|....*..
gi 1847837041 399 LDRSDEEILSYVKLYQES-----IKEFQDTLNNLKEE 430
Cdd:COG4717 411 LEELLGELEELLEALDEEeleeeLEELEEELEELEEE 447
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
136-465 |
2.84e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 136 EQLSSFQLEDLVGMLKNAEKNILLLNQARVRALQ--------DLEKILTEKDALQGEINILEMRLAETNARIKVaaqeki 207
Cdd:COG4372 11 ARLSLFGLRPKTGILIAALSEQLRKALFELDKLQeeleqlreELEQAREELEQLEEELEQARSELEQLEEELEE------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 208 hveiLEEQLVNLRNELshrgvtegsgADMHEnwnkafdgvhslgkELSLLRTENVSLKDDILALKEELShvqktdkrvvM 287
Cdd:COG4372 85 ----LNEQLQAAQAEL----------AQAQE--------------ELESLQEEAEELQEELEELQKERQ----------D 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 288 LEKERSFLESALKELEFKLVASQEDVSKLSTlkfECKNLWDRVENLQVLLDRATDQ-ADKAILVLEQNQELRKKVDMLEE 366
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEELKELEE---QLESLQEELAALEQELQALSEAeAEQALDELLKEANRNAEKEEELA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 367 SLEEANVYKLSSEKMQQYNDLMQKKIKLLEERLDRSDEEILSYVKLYQESIKEFQDTLNNLKEESKRRALNEPVDDMPWD 446
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
330
....*....|....*....
gi 1847837041 447 FWSRLLLIVDGWLLEKKIS 465
Cdd:COG4372 284 ELEALEEAALELKLLALLL 302
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
798-965 |
2.85e-04 |
|
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).
Pssm-ID: 340850 [Multi-domain] Cd Length: 357 Bit Score: 44.24 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 798 EALRKHLGLSYADTRRPLVGCIARLVPQKGIHLIRHAIYRTLELGGQFVLLGSSPvphiqvefEGIANHFKGDDHIRLIL 877
Cdd:cd03823 176 EPDLAPPPRRRPGTERLRFGYIGRLTEEKGIDLLVEAFKRLPREDIELVIAGHGP--------LSDERQIEGGRRIAFLG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 878 KYDESLSHSIYAASDMFLIPSMF-EPCGLTQMIAMRYGSIPIARKTGGLNDSVFDVdddtiplqfRNGYTFLNPDEQGLN 956
Cdd:cd03823 248 RVPTDDIKDFYEKIDVLVVPSIWpEPFGLVVREAIAAGLPVIASDLGGIAELIQPG---------VNGLLFAPGDAEDLA 318
|
....*....
gi 1847837041 957 GALERAFNH 965
Cdd:cd03823 319 AAMRRLLTD 327
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
157-445 |
3.08e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 157 ILLLNQARVRALQDLEKiltEKDALQGEINILEMRLAETNARIKVAAQEkihVEILEEQLVNLRNELshrgvtegsgadm 236
Cdd:COG4942 11 LALAAAAQADAAAEAEA---ELEQLQQEIAELEKELAALKKEEKALLKQ---LAALERRIAALARRI------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 237 henwNKAFDGVHSLGKELSLLRTENVSLKDDILALKEELShvqktdKRVVMLEK--ERSFLesalkelefKLVASQEDVS 314
Cdd:COG4942 72 ----RALEQELAALEAELAELEKEIAELRAELEAQKEELA------ELLRALYRlgRQPPL---------ALLLSPEDFL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 315 KLSTlkfecknlwdRVENLQVLL----DRATDQADKAILVLEQNQELRKKVDMLEESLEEAnvyklsSEKMQQYNDLMQK 390
Cdd:COG4942 133 DAVR----------RLQYLKYLAparrEQAEELRADLAELAALRAELEAERAELEALLAEL------EEERAALEALKAE 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1847837041 391 KIKLLeERLDRSDEEILSYVKLYQESIKEFQDTLNNLKEESKRRALNEPVDD-------MPW 445
Cdd:COG4942 197 RQKLL-ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGfaalkgkLPW 257
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
136-383 |
3.26e-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: 44.73 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 136 EQLSS-FQLEDLVGMLKNAEKN-----ILLLNQARVRAlQDLEKILTEKDALQGEINILEMRLAEtnarikvaAQEKIHV 209
Cdd:pfam05557 3 ELIESkARLSQLQNEKKQMELEhkrarIELEKKASALK-RQLDRESDRNQELQKRIRLLEKREAE--------AEEALRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 210 EILEEQLVNLRNELSHRGVTEGSgadmhENWNKAFDGVHSLGKELSLLRTEnvsLKDDILALKEELSHVQKT-------D 282
Cdd:pfam05557 74 QAELNRLKKKYLEALNKKLNEKE-----SQLADAREVISCLKNELSELRRQ---IQRAELELQSTNSELEELqerldllK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 283 KRVVMLEKERSFLESA----------LKELEFKLV----------ASQEDVSKLSTLKFECKNLWDRVENLQvlldraTD 342
Cdd:pfam05557 146 AKASEAEQLRQNLEKQqsslaeaeqrIKELEFEIQsqeqdseivkNSKSELARIPELEKELERLREHNKHLN------EN 219
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1847837041 343 QADKAILVlEQNQELRKKVDMLEESLEEANVYKLSSEKMQQ 383
Cdd:pfam05557 220 IENKLLLK-EEVEDLKRKLEREEKYREEAATLELEKEKLEQ 259
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
265-433 |
3.30e-04 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 464704 [Multi-domain] Cd Length: 258 Bit Score: 43.40 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 265 KDDILALKEELshvQKTDKrvvMLEKERSFLESALKELEFKLVASQEDVSKLSTLK---FECKNLwdRVENLQVLLDRAT 341
Cdd:pfam15397 62 KKQLQQAKAEL---QEWEE---KEESKLNKLEQQLEQLNAKIQKTQEELNFLSTYKdkeYPVKAV--QIANLVRQLQQLK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 342 D-QADKailvLEQNQELRKKV-DMLEESL---EEANVYKLSSEKMQQYNDLMQKKIklleerldRSDEEILSYVKLYQES 416
Cdd:pfam15397 134 DsQQDE----LDELEEMRRMVlESLSRKIqkkKEKILSSLAEKTLSPYQESLLQKT--------RDNQVMLKEIEQFREF 201
|
170
....*....|....*..
gi 1847837041 417 IKEFQDTLNNLKEESKR 433
Cdd:pfam15397 202 IDELEEEIPKLKAEVQQ 218
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
157-430 |
3.43e-04 |
|
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: 44.56 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 157 ILLLNQARVRALQDLEKILTEKDALQGEINILEMR--LAETNARIKVAAQEKIH--VEILEEQLVNLRNELSHRGVTEGS 232
Cdd:COG5185 109 LPNYEWSADILISLLYLYKSEIVALKDELIKVEKLdeIADIEASYGEVETGIIKdiFGKLTQELNQNLKKLEIFGLTLGL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 233 GADMH-ENWNKAFDGVHSLGKELSL-LRTENVSL--KDDILALKEELSHVQKTDKRVVMLEKERSFLESALK---ELEFK 305
Cdd:COG5185 189 LKGISeLKKAEPSGTVNSIKESETGnLGSESTLLekAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEqntDLRLE 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 306 LVASQEDVSKlsTLKFECKNLWDRVENLQVLLDRATDQADKAILVLEQNQELRK--KVDMLEESLEE--ANVYKLSSEKM 381
Cdd:COG5185 269 KLGENAESSK--RLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAaeAEQELEESKREteTGIQNLTAEIE 346
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1847837041 382 QQYNDLMQKKIKLLEERLDRSDEEILSyvkLYQESIKEFQDTLNNLKEE 430
Cdd:COG5185 347 QGQESLTENLEAIKEEIENIVGEVELS---KSSEELDSFKDTIESTKES 392
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
282-429 |
4.36e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 282 DKRVVMLEKERSFLESALKELEFKLVASqedvsKLSTLKFECKNLWDRVEN-------LQVLLDRATDQADKAIlvlEQN 354
Cdd:PRK04778 255 EKEIQDLKEQIDENLALLEELDLDEAEE-----KNEEIQERIDQLYDILERevkarkyVEKNSDTLPDFLEHAK---EQN 326
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1847837041 355 QELRKKVDMLEESleeanvYKLSSEKMQQYNDLmQKKIKLLEERLDRSDEEILSYVKLYQESIKEFQDTLNNLKE 429
Cdd:PRK04778 327 KELKEEIDRVKQS------YTLNESELESVRQL-EKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEE 394
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
530-659 |
5.82e-04 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 41.62 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 530 GGLGDVVSGLSRALQKKGHLVEIVLPKYdcmqydhirdlrvldmelesyfDGRLFRNKVWVGTVEGLPVyfiePHHPSKF 609
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGG----------------------PPGRPELVGDGVRVHRLPV----PPRPSPL 54
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1847837041 610 FWRgtvygehddfrrfsYFSRAALELLlqAGKKPDIIHCHDWQTAFVAPL 659
Cdd:pfam13579 55 ADL--------------AALRRLRRLL--RAERPDVVHAHSPTAGLAARL 88
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
767-927 |
8.35e-04 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 43.16 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 767 GIDTDAWDPAtdvyLKSqfnandlqgkaenkEALRKHLglSYADTRRPLVGCIARLVPQKGIHLIRHAIYRTLELGGQFV 846
Cdd:PLN02871 237 GVDSESFHPR----FRS--------------EEMRARL--SGGEPEKPLIVYVGRLGAEKNLDFLKRVMERLPGARLAFV 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 847 llGSSPV-PHIQVEFEGIANHFKGddhirlILKYDEsLShSIYAASDMFLIPSMFEPCGLTQMIAMRYGSIPIARKTGGL 925
Cdd:PLN02871 297 --GDGPYrEELEKMFAGTPTVFTG------MLQGDE-LS-QAYASGDVFVMPSESETLGFVVLEAMASGVPVVAARAGGI 366
|
..
gi 1847837041 926 ND 927
Cdd:PLN02871 367 PD 368
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
262-443 |
8.45e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.07 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 262 VSLKDDILAlkEELSHVQKT---DKRVV--MLEKERSFLESALKELEFKLVASQEDVSKLSTLKFECKNLWDRVENLQVL 336
Cdd:pfam05262 158 IPLKKNILS--GNVSDVDTDsisDKKVVeaLREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQK 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 337 LDRATDQADKAILVLEQNQELRKKVDMLEESLEEANVYKLSSEKMQQYNDLMQKKIKLLEERLDRSDEEILSYVKLYQES 416
Cdd:pfam05262 236 ADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKAS 315
|
170 180
....*....|....*....|....*..
gi 1847837041 417 IKEFQDtlnnlKEESKRRALNEPVDDM 443
Cdd:pfam05262 316 EKEAED-----KELEAQKKREPVAEDL 337
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
280-433 |
9.21e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 280 KTDKRVVMLEKERSFLESALKELEFKLVASQEDVSKLSTLKFECKNLWDRVENLQVLLDRAtDQADKAILVLEQNQELRK 359
Cdd:COG4717 61 PQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 360 KVDMLEESLEEAnvyklsSEKMQQYNDLMQKKIKL----------LEERLDRSDEEILSYVKLYQESIKEFQDTLNNLKE 429
Cdd:COG4717 140 ELAELPERLEEL------EERLEELRELEEELEELeaelaelqeeLEELLEQLSLATEEELQDLAEELEELQQRLAELEE 213
|
....
gi 1847837041 430 ESKR 433
Cdd:COG4717 214 ELEE 217
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
272-487 |
9.81e-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: 43.29 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 272 KEELSHVQKTDKRVVMLEKERSflESALKELEFKLVASQEdvSKLSTLKFECKNLWDRVENLQVllDRATDQADKailvl 351
Cdd:pfam12128 220 RQQVEHWIRDIQAIAGIMKIRP--EFTKLQQEFNTLESAE--LRLSHLHFGYKSDETLIASRQE--ERQETSAEL----- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 352 eqNQELRKKVDMLEESLEEANVyKLSSEKMQQYNDlmQKKIKLLEERLDRSDEEILSYVKLYQESIKEFQDTLNNLKEES 431
Cdd:pfam12128 289 --NQLLRTLDDQWKEKRDELNG-ELSAADAAVAKD--RSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERL 363
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1847837041 432 KrrALNEPVDDMPWDFWSRLLLIVDGwlLEKKISANDAKL--LREMVWKRDGRIRDAY 487
Cdd:pfam12128 364 K--ALTGKHQDVTAKYNRRRSKIKEQ--NNRDIAGIKDKLakIREARDRQLAVAEDDL 417
|
|
| KBP_C |
pfam12309 |
KIF-1 binding protein C terminal; This family of proteins is found in bacteria and eukaryotes. ... |
254-429 |
1.25e-03 |
|
KIF-1 binding protein C terminal; This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 365 and 621 amino acids in length. There is a conserved LLP sequence motif. KBP is a binding partner for KIF1Balpha that is a regulator of its transport function and thus represents a type of kinesin interacting protein.
Pssm-ID: 463528 Cd Length: 362 Bit Score: 42.27 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 254 LSLLRTENVSLKDDIlalkEELsHVQKTDKRVVMLEKERSFLESALKELEFKLVASQEDVSKLSTLKFE--------CKN 325
Cdd:pfam12309 73 LTLLQASKERLLDDG----EEL-DGSSGDELTAEREDEEEELEEGFKDGDLELTAYENQITDDYVLDFDdaravflnGQR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 326 LWDRVENLQVLLDRATD---------QADKAILVLEQNQELRKK-----VDMLEESLEEAN------VYK-LSSEKMQQY 384
Cdd:pfam12309 148 WLNKAKEYYTLDGHATDyveivqdhsALYKHLAFFEEDLERQCKmhkrrIDMLEPLLKELNpqyyllICRqLWFELGETY 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1847837041 385 NDLMQKKIKLLEERLDRSD-EEILSYVKLYQESIKEFQDTLNNLKE 429
Cdd:pfam12309 228 SEILDLKLDKLKASGDSPTpHAIKKINHLAKKAIKHYQSFLDSFKE 273
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
31-462 |
1.34e-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: 42.65 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 31 QRLLPASCKMRQRNFSSQHKRQQTKKVSPDRRPTNSHFQSNGDEDTEPENALADGVSSLNQGTIPDGEDADVDSHIAIEH 110
Cdd:TIGR00618 497 LELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILT 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 111 INDNPLKhltvsEEMTplgiNVKSGEQLssfqLEDLVGMLKNAEKNILLLNQArvralqdlekiltEKDALQGEINILEM 190
Cdd:TIGR00618 577 QCDNRSK-----EDIP----NLQNITVR----LQDLTEKLSEAEDMLACEQHA-------------LLRKLQPEQDLQDV 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 191 RLAETNARiKVAAQEKIHVEILEEQLVNLRNELSHRGVTEGSGADMHENWNKaFDGVHSLGKELSLLRTEnvsLKDDILA 270
Cdd:TIGR00618 631 RLHLQQCS-QELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLA-LQKMQSEKEQLTYWKEM---LAQCQTL 705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 271 LKEELSHVQKTDKRVvmlEKERSFLESALKELEFKLVASQEDVSKLSTL-KFECKNLW--DRVENLQVLLDRATDQ--AD 345
Cdd:TIGR00618 706 LRELETHIEEYDREF---NEIENASSSLGSDLAAREDALNQSLKELMHQaRTVLKARTeaHFNNNEEVTAALQTGAelSH 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 346 KAILVLEQNQELRKKVDMLEESLEEANVYK--------LSSEKMQQynDLMQKKIKLleERLDRSDEEILSYVKLYQESI 417
Cdd:TIGR00618 783 LAAEIQFFNRLREEDTHLLKTLEAEIGQEIpsdedilnLQCETLVQ--EEEQFLSRL--EEKSATLGEITHQLLKYEECS 858
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1847837041 418 KEFQDtlnnLKEESKRraLNEPVDDmpWDFWSRLLLIVDGWLLEK 462
Cdd:TIGR00618 859 KQLAQ----LTQEQAK--IIQLSDK--LNGINQIKIQFDGDALIK 895
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
249-428 |
2.05e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.37 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 249 SLGKELSLLRTENVSLKDDILALKEELSHVQKTDKRVVMLEKERSFLESA--LKELEFKLVASQEDVSKLSTLKFECKNL 326
Cdd:COG5022 825 TIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAqrVELAERQLQELKIDVKSISSLKLVNLEL 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 327 wdrvenLQVLLDRATDQADkaiLVLEQNQELRKKVDMLEESLEEANVyKLSSEKMQQYNDlmqKKIKLLEE--RLDRSDE 404
Cdd:COG5022 905 ------ESEIIELKKSLSS---DLIENLEFKTELIARLKKLLNNIDL-EEGPSIEYVKLP---ELNKLHEVesKLKETSE 971
|
170 180
....*....|....*....|....
gi 1847837041 405 EILSYVKLYQESIKEFQDTLNNLK 428
Cdd:COG5022 972 EYEDLLKKSTILVREGNKANSELK 995
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
247-432 |
2.66e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 41.34 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 247 VHSLGKELSLLRTENVSLKDDILALKEELshvQKTDKRVVMLEKERSFLESALKELE------------FKLVASQEDVS 314
Cdd:pfam15905 75 QKELEKEIRALVQERGEQDKRLQALEEEL---EKVEAKLNAAVREKTSLSASVASLEkqlleltrvnelLKAKFSEDGTQ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 315 K-LSTLKFECKNLWDRVENLQVLLDRATDQADKAILVLEQN-QELRKKVDMLEESL----EEANVYKLSSEKMQQYN--- 385
Cdd:pfam15905 152 KkMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNlEHSKGKVAQLEEKLvsteKEKIEEKSETEKLLEYItel 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1847837041 386 -------DLMQKKIKLLEERLDRSDEEILSYVKLYQESIKEFQDTLNNLKEESK 432
Cdd:pfam15905 232 scvseqvEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCK 285
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
247-440 |
2.80e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 247 VHSLGKELSLLRTENVSLKDDILALKEELshvQKTDKRVVMLEKERSFLESALKELefkLVASQE---DVSKLSTLkFEC 323
Cdd:COG3883 39 LDALQAELEELNEEYNELQAELEALQAEI---DKLQAEIAEAEAEIEERREELGER---ARALYRsggSVSYLDVL-LGS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 324 KNLWDRVENLQvLLDRATDQADKAI-LVLEQNQELRKKVDMLEESLEEANVYKLSSEKMQQyndLMQKKIKLLEERLDRS 402
Cdd:COG3883 112 ESFSDFLDRLS-ALSKIADADADLLeELKADKAELEAKKAELEAKLAELEALKAELEAAKA---ELEAQQAEQEALLAQL 187
|
170 180 190
....*....|....*....|....*....|....*...
gi 1847837041 403 DEEILSYVKLYQESIKEFQDTLNNLKEESKRRALNEPV 440
Cdd:COG3883 188 SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
150-438 |
3.13e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.38 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 150 LKNAEKNILLLNQARVRALQDLEKILTEKDAL-------QGEINILEMRLAEtnARIKVAAQEkiH-----VEILEEQLV 217
Cdd:pfam06160 81 FKKAKKALDEIEELLDDIEEDIKQILEELDELleseeknREEVEELKDKYRE--LRKTLLANR--FsygpaIDELEKQLA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 218 NLRNELSHRGVTEGSGadmheNWNKAFDGVHSLGKEL-----------SLLRTENVSLKDDILALKE----------ELS 276
Cdd:pfam06160 157 EIEEEFSQFEELTESG-----DYLEAREVLEKLEEETdaleelmedipPLYEELKTELPDQLEELKEgyremeeegyALE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 277 HVQkTDKRVVMLEKERSFLESALKELEFKLVasQEDVSKLStlkfecknlwDRVENLQVLLDR---ATDQADKAILVL-- 351
Cdd:pfam06160 232 HLN-VDKEIQQLEEQLEENLALLENLELDEA--EEALEEIE----------ERIDQLYDLLEKevdAKKYVEKNLPEIed 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 352 ------EQNQELRKKVDMLEESleeanvYKLSSEKMQQYNDLmQKKIKLLEERLDRSD-----------------EEILS 408
Cdd:pfam06160 299 ylehaeEQNKELKEELERVQQS------YTLNENELERVRGL-EKQLEELEKRYDEIVerleekevayselqeelEEILE 371
|
330 340 350
....*....|....*....|....*....|..
gi 1847837041 409 YVKLYQESIKEFQDTLNNL-KEESK-RRALNE 438
Cdd:pfam06160 372 QLEEIEEEQEEFKESLQSLrKDELEaREKLDE 403
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
273-442 |
3.23e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 273 EELSHVQKTDKRVVMLEKERSFLESALKELEFKLVASQEDVSKLST----LKFECKNLWDRVENLQVLLDRATDQADKAI 348
Cdd:COG1579 7 RALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTeledLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 349 LVLEQnQELRKKVDMLEESLEEANvyKLSSEKMQQYNDLmQKKIKLLEERLDRSDEEILSYVKLYQESIKEFQDTLNNLK 428
Cdd:COG1579 87 NNKEY-EALQKEIESLKRRISDLE--DEILELMERIEEL-EEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|....
gi 1847837041 429 EEskRRALNEPVDD 442
Cdd:COG1579 163 AE--REELAAKIPP 174
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
151-375 |
6.02e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 151 KNAEKNILLLNQarvraLQDLEKILTEKDALQGEINILEMRLAETNARIkvaaqekihvEILEEQLVNLRNELshrgvte 230
Cdd:COG4717 61 PQGRKPELNLKE-----LKELEEELKEAEEKEEEYAELQEELEELEEEL----------EELEAELEELREEL------- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 231 gsgaDMHENWNKAFDgvhslgkelslLRTENVSLKDDILALKEELSHVQKTDKRVVMLEKERSFLESALKELEFKLVASQ 310
Cdd:COG4717 119 ----EKLEKLLQLLP-----------LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1847837041 311 EDVSkLSTLKfECKNLWDRVENLQVLLDRATDQADKAIlvlEQNQELRKKVDMLEESLEEANVYK 375
Cdd:COG4717 184 EQLS-LATEE-ELQDLAEELEELQQRLAELEEELEEAQ---EELEELEEELEQLENELEAAALEE 243
|
|
| MAP65_ASE1 |
pfam03999 |
Microtubule associated protein (MAP65/ASE1 family); |
247-436 |
6.35e-03 |
|
Microtubule associated protein (MAP65/ASE1 family);
Pssm-ID: 427641 [Multi-domain] Cd Length: 477 Bit Score: 40.37 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 247 VHSLGKELSLLRTENVSLKDDILALKEELSHVQKTD-KRVVMLEKERSF---------LESALKELEFKLVASQEdvsKL 316
Cdd:pfam03999 152 LENLRNEKERRLEEVNELKKQIKLLMEELDLVPGTDfEEDLLCESEDNFclsrenidkLRKLIKQLEEQKAEREE---KI 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 317 STLKFECKNLWDRvenLQVLLDRATDQADKA-ILVLEQNQELRKKVDMLEEsLEEANVYKL---SSEKMQQYNDLMQK-- 390
Cdd:pfam03999 229 DDLREKILELWNR---LQVPQEEQESFVRENnSLSQDTIDALREELQRLEE-LKKKNIKKLiedLRVEIEELWDKLFYst 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 391 ------------------------KIKLLEERLdRSDEEILSYVKLYQESIKEFQ---------DTLNN------LKEES 431
Cdd:pfam03999 305 eqrkrfipffeelytedllelhelELKRLKEEY-ESNKEILELVEKWEELWEDMEeleakandpSRFNNrggkllLKEEK 383
|
....*
gi 1847837041 432 KRRAL 436
Cdd:pfam03999 384 ERKRL 388
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
252-426 |
8.78e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 39.55 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 252 KELSLLRTENVSLKDDILALKEELSHVQKTDKRVVMLekeRSFLES----------ALKELEFKLVASQEDVSKLSTLKF 321
Cdd:pfam09728 32 EEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILA---KSKLEKlcrelqkqnkKLKEESKKLAKEEEEKRKELSEKF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847837041 322 EcKNLWDrvenLQVLLDratDQADKAILVLEQNQELRKKVDMLEESLE--EANVYKLSSEKM--QQYNDLMQKKIKLLEE 397
Cdd:pfam09728 109 Q-STLKD----IQDKME---EKSEKNNKLREENEELREKLKSLIEQYElrELHFEKLLKTKEleVQLAEAKLQQATEEEE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1847837041 398 RLDRSDE--EILSY-----------------VKLYQESIKEFQDTLNN 426
Cdd:pfam09728 181 KKAQEKEvaKARELkaqvqtlsetekelreqLNLYVEKFEEFQDTLNK 228
|
|
| |
