|
Name |
Accession |
Description |
Interval |
E-value |
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1132-4204 |
0e+00 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 1267.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1132 LIVLIDSYLKNKQLFNEWEEQIKLFNQIQNFLFRQRYKFPSGWLYVEQLESHLSMVLTLIQRKQKLidDNYEIIVSKIKA 1211
Cdd:COG5245 285 ILVQMDSLARLIVDRICEYVSIEWLGCCEELLTCSMESMSSLVNSFDGEESEAMSLESSLFYEFRG--GEHLAGFYSAFG 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1212 EAIKLNDSVHALYRKWsTHKPITGNLSPAFAMVELENFQKQFANLELNTKAILNVAVLLDIAIIHIDDLSLGVQEVKDLK 1291
Cdd:COG5245 363 DIKRILLFTWSFKKLG-TLLPSLPGYSSGGMDYGEEYRSLLWELGSEVGDPDSGPVRKWMRKDLFDAKVRSGVSFGKQEE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1292 IVWSSVNGLWEDLERLKHWKWS---ELQPRQLHVQLAELLNSSRSLPTNVRQYAAVDEIQNLVKDHLKNhnKVAELKnec 1368
Cdd:COG5245 442 FVSDIFNITFERIHGMDPTTLEddeEDTPALAILLGQEEAGRFVKLCKIMRMFSFFNSLEMFSRRTLAN--RMAIVK--- 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1369 mkerHWKILL--SQLGVEKVLFEEMT--VGDVWNLNISLNLQVINEMLEQANnerTIEENLTKINTEWSTITFElfnyen 1444
Cdd:COG5245 517 ----YLSSVVrtGPLFLQRDFFGRMSelLMARDMFMEVDGVLRLFFGGEWSG---IVQLSGIRRAKRCVERQID------ 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1445 kcRLVKNWdklfdqCNNDINALSSMKNSPYFgsfEREIsELEKKLNNLfmildTWIDVQRqWVYLDGVFGnSNNDIKSLL 1524
Cdd:COG5245 584 --DEIREW------CSSVLSDDFLEERAVRV---ERGA-DGARRLRAS-----SGSPVLR-RLDEYLMMM-SLEDLMPLI 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1525 PIETTRFTNITYELQNLMKRIYKFNLVIDIVLIgDIQTIMNKFLESLTKVRRLLTDYLEKQRELFPRFyfVGNEDLLEII 1604
Cdd:COG5245 645 PHAVHRKMSLVSGVRGIYKRVVSGCEAINTILE-DVGDDLDLFYKEMDQVFMSIEKVLGLRWREVERA--SEVEELMDRV 721
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1605 GGSNDITRINRHFKKMFAGIECVEYAneSSSIVSVQSEEGEKLELNKPVSLIKFPRLNEWLNELELEtrltlaqlvkdkl 1684
Cdd:COG5245 722 RELENRVYSYRFFVKKIAKEEMKTVF--SSRIQKKEPFSLDSEAYVGFFRLYEKSIVIRGINRSMGR------------- 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1685 glchmLLSQFGDSSRYLDFVTSAPGQVALLAVQitfTTLTEESMKTGSL-NDQQINVNSGINALTQLISYEI---SDIER 1760
Cdd:COG5245 787 -----VLSQYLESVQEALEIEDGSFFVSRHRVR---DGGLEKGRGCDAWeNCFDPPLSEYFRILEKIFPSEEgyfFDEVL 858
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1761 KKIQNLIIEMIHHRDIITSLLNAKSESERDSIWHISQKFYfdtkcSDLLSSLKVKQVNAEFNYAFEYLGVVERLAYTPLI 1840
Cdd:COG5245 859 KRLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELP-----QGLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMD 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1841 DNCFLTMTQALARKQggSPFgpAGTGKTESIKALGHNLGKMVlvfccdESFDFQSmgRIFLGLCRVGIWGcFDEFNRLDD 1920
Cdd:COG5245 934 TSQHQKLFEAVCDEV--CRF--VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDE 1000
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1921 GSLsAISSQIETIEHGLKNPGSQISISNRSINVDPETGLFVTMNPgyvgRQELPENLKKLFRSFSMEKPDSTIIveilla 2000
Cdd:COG5245 1001 ISR-TILVDEYLNSDEFRMLEELNSAVVEHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSNIPFGAIK------ 1069
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2001 sqafENSRDLANVIVPFYLELAEKVSRQSHYDFglRALKSMLircgQSKRNSRNQLGKDQKLWETELVLRSIIETILPKl 2080
Cdd:COG5245 1070 ----SRRESLDREIGAFNNEVDGIAREEDELMF--YPMFKSL----KAKHRMLEEKTEYLNKILSITGLPLISDTLRER- 1138
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2081 vredeilfnilkdkffagvsSDTVDnaklvAELHKYCSSIGIQC----DDRWITKASQVVD---IQNTHHGIMLVGESGS 2153
Cdd:COG5245 1139 --------------------IDTLD-----AEWDSFCRISESLKkyesQQVSGLDVAQFVSflrSVDTGAFHAEYFRVFL 1193
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2154 GKSTILNSVLHALSEVENVehtsIVIDAkvlskeqiYGKLDLVTRdwtdGLFTSVLRrirENLRGELS-KRIWIVFDcdi 2232
Cdd:COG5245 1194 CKIKHYTDACDYLWHVKSP----YVKKK--------YFDADMELR----QFFLMFNR---EDMEARLAdSKMEYEVE--- 1251
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2233 dpQWAENLNSVLDDNRILTLPNGERLALPDNLRivfevdslkcTTPATVSRCGMVWFDSSLISIDAlchKLVHNLNSETV 2312
Cdd:COG5245 1252 --RYVEKTKAEVSSLKLELSSVGEGQVVVSNLG----------SIGDKVGRCLVEYDSISRLSTKG---VFLDELGDTKR 1316
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2313 HLGEEgIAELNNGKklqtlFVQQVAEILNPQLLSKICDLAKNIDHIMDfsiQRAVTSFETTLRSYLRRFIKHS-YTHNSD 2391
Cdd:COG5245 1317 YLDEC-LDFFSCFE-----EVQKEIDELSMVFCADALRFSADLYHIVK---ERRFSGVLAGSDASESLGGKSIeLAAILE 1387
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2392 IIDIKKYVDKAVLLSFIWTFAGDASYEEKEKF--------GREVALLDTFGHIepvegVHLDYDISLPECEWlnwnNSVF 2463
Cdd:COG5245 1388 HKDLIVEMKRGINDVLKLRIFGDKCRESTPRFylisdgdlIKDLNERSDYEEM-----LIMMFNISAVITNN----GSIA 1458
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2464 AIELEPYQVASP-NTVVPTLDTVRHEYLVYSILNEHRPLLLCGPPGSGKTMTLLEALRKSPQLDVLSLNFSKDTSPISLL 2542
Cdd:COG5245 1459 GFELRGERVMLRkEVVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSLRSELITEVKYFNFSTCTMTPSKL 1538
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2543 KSLEQFCEYKKSNRGIQLAPKVSGKWVVVFCDEINLPKMDKYGTQQVISLIRLMVEHKGFWRTGDQQWVSLENIQFVGAC 2622
Cdd:COG5245 1539 SVLERETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSSIAVSWVTICGIILYGAC 1618
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2623 NSPKDPGRNALSERFLRHVSLIMVDYPGTTSLKQIYHTFSYAILKCAPVLRGFSQAITDASIEIYQQSKRHFTKSEQPHY 2702
Cdd:COG5245 1619 NPGTDEGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASVELYLSSKDKTKFFLQMNY 1698
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2703 IYSPRELTRWSRGLLEALKSMEYTDLMQLIRVWYHEGLRLFYDRLVSEKDRNWTMSLFRQISGIHFLNVDLESCFKAPVL 2782
Cdd:COG5245 1699 GYKPRELTRSLRAIFGYAETRIDTPDVSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREMIAGHIGEAEIT 1778
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2783 FSNWLTLNYRSVNENELKSFLSERLRVFSEEETEVDLVLHEDMLDHALRIDRVLRQPQGHMILVGPSTSGKSTLAKFVAW 2862
Cdd:COG5245 1779 FSMILFFGMACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCW 1858
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2863 INGLKIVQLNVRRNYSIDDFDNTLRKLLLRC-VGGERVCFIIDESSILETSFIERMNTLLANAEIPGLFEGEEYTSLMSL 2941
Cdd:COG5245 1859 LNPRNMREIFGHRDELTGDFRDSLKVQDLRRnIHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPEN 1938
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2942 CLEISNSQGLLLDNDDELYNWFRGQVSQNLHVIFTISETNVGSSAAVISSPALFNRCVLSWMGDWSNKCLYEIAASRIeq 3021
Cdd:COG5245 1939 LRFVFESTSLEKDTEATLTRVFLVYMEENLPVVFSACCSQDTSVLAGIRSPALKNRCFIDFKKLWDTEEMSQYANSVE-- 2016
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3022 vPLDISNYSIPTSFEPFLEINISNFRDVLVDAIAFIHR---YEPNYQATLAyrRAPSDFLNFISGFVTLFNKKQFELEES 3098
Cdd:COG5245 2017 -TLSRDGGRVFFINGELGVGKGALISEVFGDDAVVIEGrgfEISMIEGSLG--ESKIKFIGGLKVYDARCVIYIEELDCT 2093
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3099 QRHISGGLDKLRETVIKVDKLKTELARKQEVLKLKDKDAKVMLNKMLTDQNEAERKQEFSVATQAELEKQEIEIERRRNI 3178
Cdd:COG5245 2094 NVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGS 2173
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3179 VMKDLALVEPAVLEAQRGVQNIKKQYLTEIRSMSNPPAAVKMTMESVCALLGYEVSTWRDVQLVIRKDDFIPNIVSFDNE 3258
Cdd:COG5245 2174 VMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLLGFEAKIWFGEQQSLRRDDFIRIIGKYPDE 2253
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3259 TQITPELRKYMEEMYVSREDFTYEVAYRASKACGPLLQWVLAQLTYSRILQTIAPLREEVQRLETQTKKTKTQLIVIDEM 3338
Cdd:COG5245 2254 IEFDLEARRFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGL 2333
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3339 IHELEESIEKYKDDYSELIRETENIKTEMKTVEKKVERSLSLLNSLTNERERWKGSIKRFADQRERLIGNSLLVAGFLAY 3418
Cdd:COG5245 2334 SSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPY 2413
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3419 CGIYDQKGRQLLVQAWKNKLNKS-GIVYDEELTVSQYLTNANESLKWVNSglLNDeLNIDNFSLLKWSQ--TPLIIDPTS 3495
Cdd:COG5245 2414 IGTLGFLCRAIEFGMSFIRISKEfRDKEIRRRQFITEGVQKIEDFKEEAC--STD-YGLENSRIRKDLQdlTAVLNDPSS 2490
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3496 SIVEILVRSYSPKTVTVTSFLHDGLIHQLENALRFGGLIVIEECQYYDPILDPILRGEIHKQGGRLMARLGEQMVDFSPN 3575
Cdd:COG5245 2491 KIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSDKIIGDAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTV 2570
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3576 FRMILSTKDGHIKLPAFVSSRTNIVNFTVTIGSLETRALDIALRVAKPDIEKQREELISLNGEYHARLQTLEEELLNSLS 3655
Cdd:COG5245 2571 EAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLM 2650
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3656 DSIGNILDNDKLVETLETLKAESSLISEKLSHAKEIILNVEEARNQYQEVAKHASIIYSVLELLGGISSFYNVSLSRFIS 3735
Cdd:COG5245 2651 LSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSS 2730
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3736 LFAELLGNN-------HDVNLSGFVLkLYEESFAKVAPSLKLKDKIILALMLSIVYysedigtIFKGVFLSVLKSIYsnT 3808
Cdd:COG5245 2731 EFEKWRRMKskylcaiRYMLMSSEWI-LDHEDRSGFIHRLDVSFLLRTKRFVSTLL-------EDKNYRQVLSSCSL--Y 2800
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3809 FPDTIKHafglclarvesGSDNVGKI-------LENNQDNSTLKVLSSlilAGDGNKKAEIINTFSSITSFLYSGDRppy 3881
Cdd:COG5245 2801 GNDVISH-----------SCDRFDRDvyralkhQMDNRTHSTILTSNS---KTNPYKEYTYNDSWAEAFEVEDSGDL--- 2863
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3882 sspYELNYWISREgittfiltcpdgFDATYKVEKLAMDMKKKLTIV-SMGSKEGVDAANSEIQKAANNGDWLVVQNIQMS 3960
Cdd:COG5245 2864 ---YKFEEGLLEL------------IVGHAPLIYAHKKSLENERNVdRLGSKENEVYAVLNSLFSRKEKSWFEVYNISLS 2928
|
2890 2900 2910 2920 2930 2940 2950 2960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3961 PAWL-----SHLEMRLNSINFHKDTRLLLTCGTSSHVPSGLISQSRVLHFDTelgltgivQDTFKSIPVNLLEQQPVEMK 4035
Cdd:COG5245 2929 FGWFkryveDVVYPIKASRVCGKVKNMWTSMVDADMLPIQLLIAIDSFVSST--------YPETGCGYADLVEIDRYPFD 3000
|
2970 2980 2990 3000 3010 3020 3030 3040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 4036 SVLL-------LLVWYHSIIIKRLRYCPASFKKSYDINDSDFATGLYVIQEAFAPLSKRTnvdpklIPWDTICYLIGTIT 4108
Cdd:COG5245 3001 YTLViacddafYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNILFLNHLNA------RKWGNNRDLIFTIV 3074
|
3050 3060 3070 3080 3090 3100 3110 3120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 4109 YGGKVDDKDDFAYFESLASRLFsekAFEIDFNIIENEYTIQSNSILRMPEGNSISAYTEWIAKLPNNTPLSWIGLDENdg 4188
Cdd:COG5245 3075 YGKKHSLMEDSKVVDKYCRGYG---AHETSSQILASVPGGDPELVKFHMEEMCRSSAFGVIGQLPDLALCAWLMGPCD-- 3149
|
3130
....*....|....*.
gi 598070671 4189 nlvQEKLGEDIASKVV 4204
Cdd:COG5245 3150 ---SEYLKAIVYSSRI 3162
|
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1823-2156 |
2.73e-139 |
|
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities: AAA1-AAA6). This is the first site (out of four nucleotide binding sites in the dynein motor) where the movement depends on ATP hydrolysis. When this site is nucleotide free or bound to ADP, the microtubule binding domain (MTBD) binds to the microtubule and the linker adopts the straight post-power-stroke conformation. Upon ATP binding and hydrolysis, the MTBD detaches from the microtubule and the linker is primed into the pre-power-stroke conformation. Dynein's AAA+ domains are each divided into an alpha/beta large subdomain designated with an L and and alpha small subdomains designated with an S. This is the AAA1 large (AAA1L) subdomain with the accompanying small subdomain (AAA1S). AAA1L, AAA1S and AAA2L enclose ADP.vanadate (ADP.Vi, ATP-hydrolysis transition state analogue). The AAA1L sensor-I loop, which varies in position depending on dynein's nucleotide state, swings in to contact AAA2L forming the important AAA1 nucleotide-binding site.
Pssm-ID: 463697 [Multi-domain] Cd Length: 327 Bit Score: 438.84 E-value: 2.73e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1823 YAFEYLGVVERLAYTPLIDNCFLTMTQALARKQGGSPFGPAGTGKTESIKALGHNLGKMVLVFCCDESFDFQSMGRIFLG 1902
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1903 LCRVGIWGCFDEFNRLDDGSLSAISSQIETIEHGLKNPGSQISISNRSINVDPETGLFVTMNPGYVGRQELPENLKKLFR 1982
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1983 SFSMEKPDSTIIVEILLASQAFENSRDLANVIVPFYLELAEKVSRQSHYDFGLRALKSMLIRCGQSKRNSRNQLgkdqkl 2062
Cdd:pfam12774 161 PVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLN------ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2063 wETELVLRSIIETILPKLVREDEILFN-ILKDkFFAGVSSDTVDNAKLVAELHKYCSSIGIQCDDRWITKASQVVDIQNT 2141
Cdd:pfam12774 235 -EDVLLLRALRDMNLPKLVADDVPLFLgLISD-LFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLV 312
|
330
....*....|....*
gi 598070671 2142 HHGIMLVGESGSGKS 2156
Cdd:pfam12774 313 RHGVMLVGPTGSGKT 327
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
225-770 |
2.73e-30 |
|
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains to form dimers, and with intermediate chain-light chain complexes to form a basal cargo binding unit. The region featured in this family includes the sequences implicated in mediating these interactions. It is thought to be flexible and not to adopt a rigid conformation.
Pssm-ID: 462457 Cd Length: 560 Bit Score: 129.62 E-value: 2.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 225 LNEVTTIVNNWARQIQGLIRLNHDpMDSESIMEEIQFWKSMEAALLSLNQQVSSFEIKKSVEILNKAKRFHITlGFQNDV 304
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQ-GRNPGPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLP-AFKALD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 305 SSISDKLTQARLYNSLLKEL--PMNDLitisgEDEQDFSKFELAIVNIFNHLKLKL-NS--YP-LTRSVETIEVILNDII 378
Cdd:pfam08385 79 TELTDALNEAKDNVKYLKTLerPFEDL-----EELTDPPEIIEAIPPLMNTIRLIWsISryYNtSERMTVLLEKISNQLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 379 SKFQGLLTKKSIMSLSFSKF-SQLYDSH-INKLFDIIENNIKYMINLLRELLRRRQEKFKIikinQTRFDQIKSRLEHLY 456
Cdd:pfam08385 154 EQCKKYLSPEGIFDGDVEEAlEKLQECIeLLEAWKEEYKKTREKLEESPRERPWDFSERYI----FGRFDAFLERLEKIL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 457 QFRLNHLDLLQ------SIENVLSNS-DKIEASMKlsDAYNK-EIISINSVDISYQGslvWKMREESYLEVFNQLNTLIV 528
Cdd:pfam08385 230 ELFETIEQFSKlekiggTKGPELEGViEEILEEFQ--EAYKVfKSKTYDILDVSNEG---FDDDYEEFKERIKDLERRLQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 529 KRINLFFAKASTFVDAMAIYTKFffthsSSLLV--SIN---DEYKLKILSI--ADVE-IQKLIDFNSDRKSSDD-----I 595
Cdd:pfam08385 305 AFIDQAFDDARSTESAFKLLRIF-----EFLLErpIIRgalEEKYTDLLQMfkKELDaVKKIFDKQKYNPSPIAknmppV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 596 VGQIMWNSSLVSKLSFYRNNLKTLLGInwNNYSTGTKIDATTNKIIVSLN--PQLVYNRWIVAIGQkhAMVENLGK-IID 672
Cdd:pfam08385 380 AGAIIWARQLFRRIQEPMKRFKEELGL--LKHAEGKKVIKKYNELAKKLDeyERLIYEAWLKEVEE--ASEGNLKRpLLV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 673 IVEKSSGNdfdLIVNFNYSLLQIYEQLIQLSNLGLDVPSTTLMQYGKIYQLHPlaigLRDHVNLLCQLFENMQNSKYGQT 752
Cdd:pfam08385 456 RHPETGKL---LSVNFDPQLLALLREVKYLQKLGFEIPESALNIALKEERLRP----YAESLELLVRWYNKIRSTLLPVE 528
|
570
....*....|....*...
gi 598070671 753 FGfLLSGQIGKVKESLKP 770
Cdd:pfam08385 529 RP-LLAPHLKDIDEKLEP 545
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2480-2643 |
3.72e-10 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 61.39 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2480 PTLDTVRHEYLVYSILNEHRPLLLCGPPGSGKTMTLLEALRKS--PQLDVLSLNFSKDTSPISLLKSLEQFceykksNRG 2557
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELfrPGAPFLYLNASDLLEGLVVAELFGHF------LVR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2558 IQLAPKVSGKWVVVFCDEIN-LPKMDKYGTQQVISLIRLMVEhkgfwrtgdqqwvSLENIQFVGACNSP-KDPGRNALSE 2635
Cdd:cd00009 75 LLFELAEKAKPGVLFIDEIDsLSRGAQNALLRVLETLNDLRI-------------DRENVRVIGATNRPlLGDLDRALYD 141
|
....*...
gi 598070671 2636 RFLRHVSL 2643
Cdd:cd00009 142 RLDIRIVI 149
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2498-2641 |
5.88e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.69 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2498 HRPLLLCGPPGSGKTMTLLEALR--KSPQLDVLSLNFSKDTSPISLLKSLEQFCEYKKSNRGIQ-------LAPKVSGKw 2568
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARelGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlalaLARKLKPD- 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 598070671 2569 vVVFCDEINlpKMDKYGTQQVISLIRLMVEHKGFWRTgdqqwvslENIQFVGACNSPKDPGRNALSERFLRHV 2641
Cdd:smart00382 81 -VLILDEIT--SLLDAEQEALLLLLEELRLLLLLKSE--------KNLTVILTTNDEKDLGPALLRRRFDRRI 142
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
3309-3405 |
2.75e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3309 QTIAPLREEVQRLETQTKKTKTQLIVIDEMI--HE--------LEESIEKYKDDYSELIRETENIKTEMKTVEKKVERSL 3378
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRDEADEVLeeHEerreeletLEAEIEDLRETIAETEREREELAEEVRDLRERLEELE 292
|
90 100
....*....|....*....|....*..
gi 598070671 3379 SLLNSLTNERERWKGSIKRFADQRERL 3405
Cdd:PRK02224 293 EERDDLLAEAGLDDADAEAVEARREEL 319
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3311-3405 |
5.81e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3311 IAPLREEVQRLETQTKKTKTQLIVIDEMIHELEESIEKYKDDYSELIRETENIKTEMKTVEKKVERSLSLLNSLTNERER 3390
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90
....*....|....*
gi 598070671 3391 WKGSIKRFADQRERL 3405
Cdd:TIGR02168 759 LEAEIEELEERLEEA 773
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1132-4204 |
0e+00 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 1267.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1132 LIVLIDSYLKNKQLFNEWEEQIKLFNQIQNFLFRQRYKFPSGWLYVEQLESHLSMVLTLIQRKQKLidDNYEIIVSKIKA 1211
Cdd:COG5245 285 ILVQMDSLARLIVDRICEYVSIEWLGCCEELLTCSMESMSSLVNSFDGEESEAMSLESSLFYEFRG--GEHLAGFYSAFG 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1212 EAIKLNDSVHALYRKWsTHKPITGNLSPAFAMVELENFQKQFANLELNTKAILNVAVLLDIAIIHIDDLSLGVQEVKDLK 1291
Cdd:COG5245 363 DIKRILLFTWSFKKLG-TLLPSLPGYSSGGMDYGEEYRSLLWELGSEVGDPDSGPVRKWMRKDLFDAKVRSGVSFGKQEE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1292 IVWSSVNGLWEDLERLKHWKWS---ELQPRQLHVQLAELLNSSRSLPTNVRQYAAVDEIQNLVKDHLKNhnKVAELKnec 1368
Cdd:COG5245 442 FVSDIFNITFERIHGMDPTTLEddeEDTPALAILLGQEEAGRFVKLCKIMRMFSFFNSLEMFSRRTLAN--RMAIVK--- 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1369 mkerHWKILL--SQLGVEKVLFEEMT--VGDVWNLNISLNLQVINEMLEQANnerTIEENLTKINTEWSTITFElfnyen 1444
Cdd:COG5245 517 ----YLSSVVrtGPLFLQRDFFGRMSelLMARDMFMEVDGVLRLFFGGEWSG---IVQLSGIRRAKRCVERQID------ 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1445 kcRLVKNWdklfdqCNNDINALSSMKNSPYFgsfEREIsELEKKLNNLfmildTWIDVQRqWVYLDGVFGnSNNDIKSLL 1524
Cdd:COG5245 584 --DEIREW------CSSVLSDDFLEERAVRV---ERGA-DGARRLRAS-----SGSPVLR-RLDEYLMMM-SLEDLMPLI 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1525 PIETTRFTNITYELQNLMKRIYKFNLVIDIVLIgDIQTIMNKFLESLTKVRRLLTDYLEKQRELFPRFyfVGNEDLLEII 1604
Cdd:COG5245 645 PHAVHRKMSLVSGVRGIYKRVVSGCEAINTILE-DVGDDLDLFYKEMDQVFMSIEKVLGLRWREVERA--SEVEELMDRV 721
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1605 GGSNDITRINRHFKKMFAGIECVEYAneSSSIVSVQSEEGEKLELNKPVSLIKFPRLNEWLNELELEtrltlaqlvkdkl 1684
Cdd:COG5245 722 RELENRVYSYRFFVKKIAKEEMKTVF--SSRIQKKEPFSLDSEAYVGFFRLYEKSIVIRGINRSMGR------------- 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1685 glchmLLSQFGDSSRYLDFVTSAPGQVALLAVQitfTTLTEESMKTGSL-NDQQINVNSGINALTQLISYEI---SDIER 1760
Cdd:COG5245 787 -----VLSQYLESVQEALEIEDGSFFVSRHRVR---DGGLEKGRGCDAWeNCFDPPLSEYFRILEKIFPSEEgyfFDEVL 858
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1761 KKIQNLIIEMIHHRDIITSLLNAKSESERDSIWHISQKFYfdtkcSDLLSSLKVKQVNAEFNYAFEYLGVVERLAYTPLI 1840
Cdd:COG5245 859 KRLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELP-----QGLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMD 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1841 DNCFLTMTQALARKQggSPFgpAGTGKTESIKALGHNLGKMVlvfccdESFDFQSmgRIFLGLCRVGIWGcFDEFNRLDD 1920
Cdd:COG5245 934 TSQHQKLFEAVCDEV--CRF--VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDE 1000
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1921 GSLsAISSQIETIEHGLKNPGSQISISNRSINVDPETGLFVTMNPgyvgRQELPENLKKLFRSFSMEKPDSTIIveilla 2000
Cdd:COG5245 1001 ISR-TILVDEYLNSDEFRMLEELNSAVVEHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSNIPFGAIK------ 1069
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2001 sqafENSRDLANVIVPFYLELAEKVSRQSHYDFglRALKSMLircgQSKRNSRNQLGKDQKLWETELVLRSIIETILPKl 2080
Cdd:COG5245 1070 ----SRRESLDREIGAFNNEVDGIAREEDELMF--YPMFKSL----KAKHRMLEEKTEYLNKILSITGLPLISDTLRER- 1138
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2081 vredeilfnilkdkffagvsSDTVDnaklvAELHKYCSSIGIQC----DDRWITKASQVVD---IQNTHHGIMLVGESGS 2153
Cdd:COG5245 1139 --------------------IDTLD-----AEWDSFCRISESLKkyesQQVSGLDVAQFVSflrSVDTGAFHAEYFRVFL 1193
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2154 GKSTILNSVLHALSEVENVehtsIVIDAkvlskeqiYGKLDLVTRdwtdGLFTSVLRrirENLRGELS-KRIWIVFDcdi 2232
Cdd:COG5245 1194 CKIKHYTDACDYLWHVKSP----YVKKK--------YFDADMELR----QFFLMFNR---EDMEARLAdSKMEYEVE--- 1251
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2233 dpQWAENLNSVLDDNRILTLPNGERLALPDNLRivfevdslkcTTPATVSRCGMVWFDSSLISIDAlchKLVHNLNSETV 2312
Cdd:COG5245 1252 --RYVEKTKAEVSSLKLELSSVGEGQVVVSNLG----------SIGDKVGRCLVEYDSISRLSTKG---VFLDELGDTKR 1316
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2313 HLGEEgIAELNNGKklqtlFVQQVAEILNPQLLSKICDLAKNIDHIMDfsiQRAVTSFETTLRSYLRRFIKHS-YTHNSD 2391
Cdd:COG5245 1317 YLDEC-LDFFSCFE-----EVQKEIDELSMVFCADALRFSADLYHIVK---ERRFSGVLAGSDASESLGGKSIeLAAILE 1387
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2392 IIDIKKYVDKAVLLSFIWTFAGDASYEEKEKF--------GREVALLDTFGHIepvegVHLDYDISLPECEWlnwnNSVF 2463
Cdd:COG5245 1388 HKDLIVEMKRGINDVLKLRIFGDKCRESTPRFylisdgdlIKDLNERSDYEEM-----LIMMFNISAVITNN----GSIA 1458
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2464 AIELEPYQVASP-NTVVPTLDTVRHEYLVYSILNEHRPLLLCGPPGSGKTMTLLEALRKSPQLDVLSLNFSKDTSPISLL 2542
Cdd:COG5245 1459 GFELRGERVMLRkEVVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSLRSELITEVKYFNFSTCTMTPSKL 1538
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2543 KSLEQFCEYKKSNRGIQLAPKVSGKWVVVFCDEINLPKMDKYGTQQVISLIRLMVEHKGFWRTGDQQWVSLENIQFVGAC 2622
Cdd:COG5245 1539 SVLERETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSSIAVSWVTICGIILYGAC 1618
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2623 NSPKDPGRNALSERFLRHVSLIMVDYPGTTSLKQIYHTFSYAILKCAPVLRGFSQAITDASIEIYQQSKRHFTKSEQPHY 2702
Cdd:COG5245 1619 NPGTDEGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASVELYLSSKDKTKFFLQMNY 1698
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2703 IYSPRELTRWSRGLLEALKSMEYTDLMQLIRVWYHEGLRLFYDRLVSEKDRNWTMSLFRQISGIHFLNVDLESCFKAPVL 2782
Cdd:COG5245 1699 GYKPRELTRSLRAIFGYAETRIDTPDVSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREMIAGHIGEAEIT 1778
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2783 FSNWLTLNYRSVNENELKSFLSERLRVFSEEETEVDLVLHEDMLDHALRIDRVLRQPQGHMILVGPSTSGKSTLAKFVAW 2862
Cdd:COG5245 1779 FSMILFFGMACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCW 1858
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2863 INGLKIVQLNVRRNYSIDDFDNTLRKLLLRC-VGGERVCFIIDESSILETSFIERMNTLLANAEIPGLFEGEEYTSLMSL 2941
Cdd:COG5245 1859 LNPRNMREIFGHRDELTGDFRDSLKVQDLRRnIHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPEN 1938
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2942 CLEISNSQGLLLDNDDELYNWFRGQVSQNLHVIFTISETNVGSSAAVISSPALFNRCVLSWMGDWSNKCLYEIAASRIeq 3021
Cdd:COG5245 1939 LRFVFESTSLEKDTEATLTRVFLVYMEENLPVVFSACCSQDTSVLAGIRSPALKNRCFIDFKKLWDTEEMSQYANSVE-- 2016
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3022 vPLDISNYSIPTSFEPFLEINISNFRDVLVDAIAFIHR---YEPNYQATLAyrRAPSDFLNFISGFVTLFNKKQFELEES 3098
Cdd:COG5245 2017 -TLSRDGGRVFFINGELGVGKGALISEVFGDDAVVIEGrgfEISMIEGSLG--ESKIKFIGGLKVYDARCVIYIEELDCT 2093
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3099 QRHISGGLDKLRETVIKVDKLKTELARKQEVLKLKDKDAKVMLNKMLTDQNEAERKQEFSVATQAELEKQEIEIERRRNI 3178
Cdd:COG5245 2094 NVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGS 2173
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3179 VMKDLALVEPAVLEAQRGVQNIKKQYLTEIRSMSNPPAAVKMTMESVCALLGYEVSTWRDVQLVIRKDDFIPNIVSFDNE 3258
Cdd:COG5245 2174 VMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLLGFEAKIWFGEQQSLRRDDFIRIIGKYPDE 2253
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3259 TQITPELRKYMEEMYVSREDFTYEVAYRASKACGPLLQWVLAQLTYSRILQTIAPLREEVQRLETQTKKTKTQLIVIDEM 3338
Cdd:COG5245 2254 IEFDLEARRFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGL 2333
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3339 IHELEESIEKYKDDYSELIRETENIKTEMKTVEKKVERSLSLLNSLTNERERWKGSIKRFADQRERLIGNSLLVAGFLAY 3418
Cdd:COG5245 2334 SSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPY 2413
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3419 CGIYDQKGRQLLVQAWKNKLNKS-GIVYDEELTVSQYLTNANESLKWVNSglLNDeLNIDNFSLLKWSQ--TPLIIDPTS 3495
Cdd:COG5245 2414 IGTLGFLCRAIEFGMSFIRISKEfRDKEIRRRQFITEGVQKIEDFKEEAC--STD-YGLENSRIRKDLQdlTAVLNDPSS 2490
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3496 SIVEILVRSYSPKTVTVTSFLHDGLIHQLENALRFGGLIVIEECQYYDPILDPILRGEIHKQGGRLMARLGEQMVDFSPN 3575
Cdd:COG5245 2491 KIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSDKIIGDAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTV 2570
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3576 FRMILSTKDGHIKLPAFVSSRTNIVNFTVTIGSLETRALDIALRVAKPDIEKQREELISLNGEYHARLQTLEEELLNSLS 3655
Cdd:COG5245 2571 EAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLM 2650
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3656 DSIGNILDNDKLVETLETLKAESSLISEKLSHAKEIILNVEEARNQYQEVAKHASIIYSVLELLGGISSFYNVSLSRFIS 3735
Cdd:COG5245 2651 LSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSS 2730
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3736 LFAELLGNN-------HDVNLSGFVLkLYEESFAKVAPSLKLKDKIILALMLSIVYysedigtIFKGVFLSVLKSIYsnT 3808
Cdd:COG5245 2731 EFEKWRRMKskylcaiRYMLMSSEWI-LDHEDRSGFIHRLDVSFLLRTKRFVSTLL-------EDKNYRQVLSSCSL--Y 2800
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3809 FPDTIKHafglclarvesGSDNVGKI-------LENNQDNSTLKVLSSlilAGDGNKKAEIINTFSSITSFLYSGDRppy 3881
Cdd:COG5245 2801 GNDVISH-----------SCDRFDRDvyralkhQMDNRTHSTILTSNS---KTNPYKEYTYNDSWAEAFEVEDSGDL--- 2863
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3882 sspYELNYWISREgittfiltcpdgFDATYKVEKLAMDMKKKLTIV-SMGSKEGVDAANSEIQKAANNGDWLVVQNIQMS 3960
Cdd:COG5245 2864 ---YKFEEGLLEL------------IVGHAPLIYAHKKSLENERNVdRLGSKENEVYAVLNSLFSRKEKSWFEVYNISLS 2928
|
2890 2900 2910 2920 2930 2940 2950 2960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3961 PAWL-----SHLEMRLNSINFHKDTRLLLTCGTSSHVPSGLISQSRVLHFDTelgltgivQDTFKSIPVNLLEQQPVEMK 4035
Cdd:COG5245 2929 FGWFkryveDVVYPIKASRVCGKVKNMWTSMVDADMLPIQLLIAIDSFVSST--------YPETGCGYADLVEIDRYPFD 3000
|
2970 2980 2990 3000 3010 3020 3030 3040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 4036 SVLL-------LLVWYHSIIIKRLRYCPASFKKSYDINDSDFATGLYVIQEAFAPLSKRTnvdpklIPWDTICYLIGTIT 4108
Cdd:COG5245 3001 YTLViacddafYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNILFLNHLNA------RKWGNNRDLIFTIV 3074
|
3050 3060 3070 3080 3090 3100 3110 3120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 4109 YGGKVDDKDDFAYFESLASRLFsekAFEIDFNIIENEYTIQSNSILRMPEGNSISAYTEWIAKLPNNTPLSWIGLDENdg 4188
Cdd:COG5245 3075 YGKKHSLMEDSKVVDKYCRGYG---AHETSSQILASVPGGDPELVKFHMEEMCRSSAFGVIGQLPDLALCAWLMGPCD-- 3149
|
3130
....*....|....*.
gi 598070671 4189 nlvQEKLGEDIASKVV 4204
Cdd:COG5245 3150 ---SEYLKAIVYSSRI 3162
|
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1823-2156 |
2.73e-139 |
|
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities: AAA1-AAA6). This is the first site (out of four nucleotide binding sites in the dynein motor) where the movement depends on ATP hydrolysis. When this site is nucleotide free or bound to ADP, the microtubule binding domain (MTBD) binds to the microtubule and the linker adopts the straight post-power-stroke conformation. Upon ATP binding and hydrolysis, the MTBD detaches from the microtubule and the linker is primed into the pre-power-stroke conformation. Dynein's AAA+ domains are each divided into an alpha/beta large subdomain designated with an L and and alpha small subdomains designated with an S. This is the AAA1 large (AAA1L) subdomain with the accompanying small subdomain (AAA1S). AAA1L, AAA1S and AAA2L enclose ADP.vanadate (ADP.Vi, ATP-hydrolysis transition state analogue). The AAA1L sensor-I loop, which varies in position depending on dynein's nucleotide state, swings in to contact AAA2L forming the important AAA1 nucleotide-binding site.
Pssm-ID: 463697 [Multi-domain] Cd Length: 327 Bit Score: 438.84 E-value: 2.73e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1823 YAFEYLGVVERLAYTPLIDNCFLTMTQALARKQGGSPFGPAGTGKTESIKALGHNLGKMVLVFCCDESFDFQSMGRIFLG 1902
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1903 LCRVGIWGCFDEFNRLDDGSLSAISSQIETIEHGLKNPGSQISISNRSINVDPETGLFVTMNPGYVGRQELPENLKKLFR 1982
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1983 SFSMEKPDSTIIVEILLASQAFENSRDLANVIVPFYLELAEKVSRQSHYDFGLRALKSMLIRCGQSKRNSRNQLgkdqkl 2062
Cdd:pfam12774 161 PVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLN------ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2063 wETELVLRSIIETILPKLVREDEILFN-ILKDkFFAGVSSDTVDNAKLVAELHKYCSSIGIQCDDRWITKASQVVDIQNT 2141
Cdd:pfam12774 235 -EDVLLLRALRDMNLPKLVADDVPLFLgLISD-LFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLV 312
|
330
....*....|....*
gi 598070671 2142 HHGIMLVGESGSGKS 2156
Cdd:pfam12774 313 RHGVMLVGPTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1285-1682 |
4.28e-117 |
|
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic cells, as they can convert energy derived from the hydrolysis of ATP to force and movement along cytoskeletal polymers, such as microtubules. This region is found C-terminal to the dynein heavy chain N-terminal region 1 (pfam08385) in many members of this family. No functions seem to have been attributed specifically to this region.
Pssm-ID: 462462 [Multi-domain] Cd Length: 402 Bit Score: 378.53 E-value: 4.28e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1285 QEVKDLKIVWSSVNGLWEDLERLKHWKWSELQPRQLHVQLAELLNSSRSLPTNVRQYAAVDEIQNLVKDHLKNHNKVAEL 1364
Cdd:pfam08393 6 KELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLPLIEDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1365 KNECMKERHWKILLSQLGVE-KVLFEEMTVGDVWNLNISLNLQVINEMLEQANNERTIEENLTKINTEWSTITFELFNYE 1443
Cdd:pfam08393 86 RNPALRERHWKQLSEILGFDfDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFELVPYK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1444 N-KCRLVKNWDKLFDQCNNDINALSSMKNSPYFGSFEREISELEKKLNNLFMILDTWIDVQRQWVYLDGVFGNSnnDIKS 1522
Cdd:pfam08393 166 DtGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSSE--DIRK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1523 LLPIETTRFTNITYELQNLMKRIYKFNLVIDIVLIGDIQTIMNKFLESLTKVRRLLTDYLEKQRELFPRFYFVGNEDLLE 1602
Cdd:pfam08393 244 QLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLSNDELLE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 1603 IIGGSNDITRINRHFKKMFAGIECVEYaNESSSIVSVQSEEGEKLELNKPVSLIKfPRLNEWLNELELETRLTLAQLVKD 1682
Cdd:pfam08393 324 ILSQTKDPTRVQPHLKKCFEGIASLEF-DENKEITGMISKEGEVVPFSKPPVEAK-GNVEEWLNELEEEMRETLRDLLKE 401
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3462-3681 |
1.48e-76 |
|
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the fifth AAA+ domain subdomain AAA5S. Structural analysis reveal that it is the coiled-coil buttress interface. The relative movement of AAA5S together with the stalk (AAA4S), is coupled to rearrangements in the AAA+ ring. Closure of the AAA1 site and the rigid body movement of AAA2-AAA4 force the AAA4/AAA5 interface to close and the AAA6L subdomain to rotate towards the ring centre. The AAA5S subdomain rotates as a unit together with AAA6L, and this movement pulls the buttress relative to the stalk.
Pssm-ID: 463702 [Multi-domain] Cd Length: 222 Bit Score: 254.29 E-value: 1.48e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3462 LKWVNSGLLNDELNIDNFSLLK-WSQTPLIIDPTSSIVEILVRSYSPKTVTVTSFLHDGLIHQLENALRFGGLIVIEEC- 3539
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTnSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3540 QYYDPILDPILRGEIHKQGGRLMARLGEQMVDFSPNFRMILSTKDGHIKLPAFVSSRTNIVNFTVTIGSLETRALDIALR 3619
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 598070671 3620 VAKPDIEKQREELISLNGEYHARLQTLEEELLNSLSDSIGNILDNDKLVETLETLKAESSLI 3681
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2476-2649 |
5.03e-44 |
|
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).
Pssm-ID: 463698 [Multi-domain] Cd Length: 179 Bit Score: 159.48 E-value: 5.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2476 NTVVPTLDTVRHEYLVYSILNEHRPLLLCGPPGSGKTMTLLEALRKSP--QLDVLSLNFSKDTSPISLLKSLEQFCEyKK 2553
Cdd:pfam12775 9 EILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDkeKYLPLFINFSAQTTSNQTQDIIESKLE-KR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2554 snRGIQLAPKVsGKWVVVFCDEINLPKMDKYGTQQVISLIRLMVEHKGFWRTGDQQWVSLENIQFVGACNSPKdPGRNAL 2633
Cdd:pfam12775 88 --RKGVYGPPG-GKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKLTFKEIVDVQFVAAMGPPG-GGRNDI 163
|
170
....*....|....*.
gi 598070671 2634 SERFLRHVSLIMVDYP 2649
Cdd:pfam12775 164 TPRLLRHFNVFNITFP 179
|
|
| AAA_8 |
pfam12780 |
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
2818-3087 |
1.75e-40 |
|
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This particular family is the D4 ATP-binding region of the motor.
Pssm-ID: 463701 [Multi-domain] Cd Length: 259 Bit Score: 151.99 E-value: 1.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2818 DLVLHEDMLDHALRIDRVLRQPQGHMILVGPSTSGKSTLAKFVAWINGLKIVQLNVRRNYSIDDFDNTLRKLLLRC-VGG 2896
Cdd:pfam12780 2 DLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAgIKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2897 ERVCFIIDESSILETSFIERMNTLLANAEIPGLFEGEEYTSLMSLCLEISNSQGlLLDNDDELYNWFRGQVSQNLHVIFT 2976
Cdd:pfam12780 82 KPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQN-IEDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2977 ISETNVGSSAAVISSPALFNRCVLSWMGDWSNKCLYEIAASRIEQVPLDisnysiptsfepfleiniSNFRDVLVDAIAF 3056
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFLEDIEIP------------------EELKSNVVKVFVY 222
|
250 260 270
....*....|....*....|....*....|....*....
gi 598070671 3057 IH----RYEPNYQATLayRRA----PSDFLNFISGFVTL 3087
Cdd:pfam12780 223 VHssveDMSKKFYEEL--KRKnyvtPKSYLELLRLYKNL 259
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
3102-3435 |
9.95e-32 |
|
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This family is the region between D4 and D5 and is the two predicted alpha-helical coiled coil segments that form the stalk supporting the ATP-sensitive microtubule binding component.
Pssm-ID: 463699 [Multi-domain] Cd Length: 344 Bit Score: 129.42 E-value: 9.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3102 ISGGLDKLRETVIKVDKLKTELARKQEVLKLKDKDAKVMLNKMLTDQNEAERKQEFSVATQAELEKQEIEIERRRNIVMK 3181
Cdd:pfam12777 3 LENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKACEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3182 DLALVEPAVLEAQRGVQNIKKQYLTEIRSMSNPPAAVKMTMESVCALL--GYEV---STWRDVQLVIRK-DDFIPNIVSF 3255
Cdd:pfam12777 83 DLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMapGGKIpkdKSWKAAKIMMAKvDGFLDSLIKF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3256 DNETqiTPELRKYMEEMYVSREDFTYEVAYRASKACGPLLQWVLAQLTYSRILQTIAPLREEVQRLETQTKKTKTQLIVI 3335
Cdd:pfam12777 163 DKEH--IHEACLKAFKPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQEKLAAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3336 DEMIHELEESIEKYKDDYSELIRETENIKTEMKTVEKKVERSLSLLNSLTNERERWKGSIKRFADQRERLIGNSLLVAGF 3415
Cdd:pfam12777 241 KAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDILLISAF 320
|
330 340
....*....|....*....|.
gi 598070671 3416 LAYCGIYDQKGRQ-LLVQAWK 3435
Cdd:pfam12777 321 ISYLGFFTKKYRNeLLDKFWI 341
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
225-770 |
2.73e-30 |
|
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains to form dimers, and with intermediate chain-light chain complexes to form a basal cargo binding unit. The region featured in this family includes the sequences implicated in mediating these interactions. It is thought to be flexible and not to adopt a rigid conformation.
Pssm-ID: 462457 Cd Length: 560 Bit Score: 129.62 E-value: 2.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 225 LNEVTTIVNNWARQIQGLIRLNHDpMDSESIMEEIQFWKSMEAALLSLNQQVSSFEIKKSVEILNKAKRFHITlGFQNDV 304
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQ-GRNPGPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLP-AFKALD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 305 SSISDKLTQARLYNSLLKEL--PMNDLitisgEDEQDFSKFELAIVNIFNHLKLKL-NS--YP-LTRSVETIEVILNDII 378
Cdd:pfam08385 79 TELTDALNEAKDNVKYLKTLerPFEDL-----EELTDPPEIIEAIPPLMNTIRLIWsISryYNtSERMTVLLEKISNQLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 379 SKFQGLLTKKSIMSLSFSKF-SQLYDSH-INKLFDIIENNIKYMINLLRELLRRRQEKFKIikinQTRFDQIKSRLEHLY 456
Cdd:pfam08385 154 EQCKKYLSPEGIFDGDVEEAlEKLQECIeLLEAWKEEYKKTREKLEESPRERPWDFSERYI----FGRFDAFLERLEKIL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 457 QFRLNHLDLLQ------SIENVLSNS-DKIEASMKlsDAYNK-EIISINSVDISYQGslvWKMREESYLEVFNQLNTLIV 528
Cdd:pfam08385 230 ELFETIEQFSKlekiggTKGPELEGViEEILEEFQ--EAYKVfKSKTYDILDVSNEG---FDDDYEEFKERIKDLERRLQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 529 KRINLFFAKASTFVDAMAIYTKFffthsSSLLV--SIN---DEYKLKILSI--ADVE-IQKLIDFNSDRKSSDD-----I 595
Cdd:pfam08385 305 AFIDQAFDDARSTESAFKLLRIF-----EFLLErpIIRgalEEKYTDLLQMfkKELDaVKKIFDKQKYNPSPIAknmppV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 596 VGQIMWNSSLVSKLSFYRNNLKTLLGInwNNYSTGTKIDATTNKIIVSLN--PQLVYNRWIVAIGQkhAMVENLGK-IID 672
Cdd:pfam08385 380 AGAIIWARQLFRRIQEPMKRFKEELGL--LKHAEGKKVIKKYNELAKKLDeyERLIYEAWLKEVEE--ASEGNLKRpLLV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 673 IVEKSSGNdfdLIVNFNYSLLQIYEQLIQLSNLGLDVPSTTLMQYGKIYQLHPlaigLRDHVNLLCQLFENMQNSKYGQT 752
Cdd:pfam08385 456 RHPETGKL---LSVNFDPQLLALLREVKYLQKLGFEIPESALNIALKEERLRP----YAESLELLVRWYNKIRSTLLPVE 528
|
570
....*....|....*...
gi 598070671 753 FGfLLSGQIGKVKESLKP 770
Cdd:pfam08385 529 RP-LLAPHLKDIDEKLEP 545
|
|
| AAA_lid_11 |
pfam18198 |
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the ... |
4035-4186 |
1.45e-27 |
|
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the C-terminal region of dynein heavy chain.
Pssm-ID: 465676 Cd Length: 139 Bit Score: 110.62 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 4035 KSVLLLLVWYHSIIIKRLRYCPASFKKSYDINDSDFATGLYVIQEAFaplskrTNVDPKlIPWDTICYLIGTITYGGKVD 4114
Cdd:pfam18198 2 KKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYL------DEYDEK-IPWDALRYLIGEINYGGRVT 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 598070671 4115 DKDDFAYFESLASRLFSEKAFEIDFNIIENEYTIqsnsilrmPEGNSISAYTEWIAKLPNNTPLSWIGLDEN 4186
Cdd:pfam18198 75 DDWDRRLLNTYLEEFFNPEVLEEDFKFSPSLYYI--------PPDGDLEDYLEYIESLPLVDSPEVFGLHPN 138
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
3899-4001 |
1.70e-15 |
|
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of dynein heavy chain. The chain also contains ATPase activity and microtubule binding ability and acts as a motor for the movement of organelles and vesicles along microtubules. Dynein is also involved in cilia and flagella movement. The dynein subunit consists of at least two heavy chains and a number of intermediate and light chains. The 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This C-terminal domain carries the D6 region of the dynein motor where the P-loop has been lost in evolution but the general structure of a potential ATP binding site appears to be retained.
Pssm-ID: 460782 Cd Length: 115 Bit Score: 75.17 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3899 FILTcPdGFDATYKVEKLA--MDMKKKLTIVSMGSKEGVDAANSeIQKAANNGDWLVVQNIQMSPAWLSHLE---MRLNS 3973
Cdd:pfam03028 8 FILS-P-GSDPTADLEKLAkkLGFGGKLHSISLGQGQGPIAEKL-IEEAAKEGGWVLLQNCHLALSWMPELEkilEELPE 84
|
90 100
....*....|....*....|....*...
gi 598070671 3974 INFHKDTRLLLTCGTSSHVPSGLISQSR 4001
Cdd:pfam03028 85 ETLHPDFRLWLTSEPSPKFPISILQNSI 112
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
2343-2460 |
1.97e-13 |
|
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA domain 5 in the dynein heavy chain. This domain is composed of 8 alpha helices.
Pssm-ID: 465532 [Multi-domain] Cd Length: 126 Bit Score: 69.62 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2343 QLLSKICD-----LAKNIDHIMDFSIQRAVTSFETTLRSYLRRFIKHSYTHNSDIIDIKKYVDKAVLLSFIWTFAGDASY 2417
Cdd:pfam17852 3 PLFEWLVPpalefVRKNCKEIVPTSDLNLVQSLCRLLESLLDEVLEYNGVHPLSPDKLKEYLEKLFLFALVWSIGGTLDE 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 598070671 2418 EEKEKFGREVALLDTFGHIEPVEGVHL-DYDISLPECEWLNWNN 2460
Cdd:pfam17852 83 DSRKKFDEFLRELFSGLDLPPPEKGTVyDYFVDLEKGEWVPWSD 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2144-2284 |
9.64e-12 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 65.39 E-value: 9.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2144 GIMLVGESGSGKSTILNSVLHALSeveNVEHTSIVIDAKvLSKEQIYGKLDLVTRD--WTDGlftSVLRRIRENlrgels 2221
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALS---NRPVFYVQLTRD-TTEEDLFGRRNIDPGGasWVDG---PLVRAAREG------ 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 598070671 2222 kriWIVFDCDID---PQWAENLNSVLDDNRILTLPNGERL-ALPDNLRIVF---EVD-SLKCTTPATVSRC 2284
Cdd:pfam07728 68 ---EIAVLDEINranPDVLNSLLSLLDERRLLLPDGGELVkAAPDGFRLIAtmnPLDrGLNELSPALRSRF 135
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2480-2643 |
3.72e-10 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 61.39 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2480 PTLDTVRHEYLVYSILNEHRPLLLCGPPGSGKTMTLLEALRKS--PQLDVLSLNFSKDTSPISLLKSLEQFceykksNRG 2557
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELfrPGAPFLYLNASDLLEGLVVAELFGHF------LVR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2558 IQLAPKVSGKWVVVFCDEIN-LPKMDKYGTQQVISLIRLMVEhkgfwrtgdqqwvSLENIQFVGACNSP-KDPGRNALSE 2635
Cdd:cd00009 75 LLFELAEKAKPGVLFIDEIDsLSRGAQNALLRVLETLNDLRI-------------DRENVRVIGATNRPlLGDLDRALYD 141
|
....*...
gi 598070671 2636 RFLRHVSL 2643
Cdd:cd00009 142 RLDIRIVI 149
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2498-2641 |
5.88e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.69 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2498 HRPLLLCGPPGSGKTMTLLEALR--KSPQLDVLSLNFSKDTSPISLLKSLEQFCEYKKSNRGIQ-------LAPKVSGKw 2568
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARelGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlalaLARKLKPD- 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 598070671 2569 vVVFCDEINlpKMDKYGTQQVISLIRLMVEHKGFWRTgdqqwvslENIQFVGACNSPKDPGRNALSERFLRHV 2641
Cdd:smart00382 81 -VLILDEIT--SLLDAEQEALLLLLEELRLLLLLKSE--------KNLTVILTTNDEKDLGPALLRRRFDRRI 142
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2500-2639 |
1.31e-05 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 47.67 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2500 PLLLCGPPGSGKT---MTLLEALRKSPqldVLSLNFSKDTSPISLLKSLEQFCEYKKSNRGIqLAPKVSGKWVVVFcDEI 2576
Cdd:pfam07728 1 GVLLVGPPGTGKTelaERLAAALSNRP---VFYVQLTRDTTEEDLFGRRNIDPGGASWVDGP-LVRAAREGEIAVL-DEI 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 598070671 2577 NLPKMDKYGTQ-QVISLIRLMVEhKGFWRTGdqqwVSLENIQFVGACNSPkDPGRNALSERFLR 2639
Cdd:pfam07728 76 NRANPDVLNSLlSLLDERRLLLP-DGGELVK----AAPDGFRLIATMNPL-DRGLNELSPALRS 133
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2828-2905 |
1.41e-04 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 45.21 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2828 HALRIDRVLRQPQGHMILVGPSTSGKSTLAKFVAWI---NGLKIVQLNVRRNYSIDDFD-----NTLRKLLLRCVGGERV 2899
Cdd:cd00009 7 IEALREALELPPPKNLLLYGPPGTGKTTLARAIANElfrPGAPFLYLNASDLLEGLVVAelfghFLVRLLFELAEKAKPG 86
|
....*.
gi 598070671 2900 CFIIDE 2905
Cdd:cd00009 87 VLFIDE 92
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
2147-2234 |
5.76e-04 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 43.60 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2147 LVGESGSGKSTILNSVLHA-LSEVENVEHTSIVIDAKVLSKEQIYGKLDLVTrdwTDGLFTSVLRRIRENLRGELSKR-- 2223
Cdd:cd00882 2 VVGRGGVGKSSLLNALLGGeVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVD---TPGLDEFGGLGREELARLLLRGAdl 78
|
90
....*....|.
gi 598070671 2224 IWIVFDCDIDP 2234
Cdd:cd00882 79 ILLVVDSTDRE 89
|
|
| AAA_lid_1 |
pfam17857 |
AAA+ lid domain; This domain represents the AAA lid domain from dynein heavy chain D3. |
2701-2752 |
1.98e-03 |
|
AAA+ lid domain; This domain represents the AAA lid domain from dynein heavy chain D3.
Pssm-ID: 465535 [Multi-domain] Cd Length: 100 Bit Score: 40.30 E-value: 1.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 598070671 2701 HYIYSPRELTRWSRGLL----EALKSMeytdlMQLIRVWYHEGLRLFYDRLVSEKD 2752
Cdd:pfam17857 24 HYIFNLRDFANIFQGILfssaECLKSP-----LDLIRLWLHESERVYGDKMVDEKD 74
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
3309-3405 |
2.75e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3309 QTIAPLREEVQRLETQTKKTKTQLIVIDEMI--HE--------LEESIEKYKDDYSELIRETENIKTEMKTVEKKVERSL 3378
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRDEADEVLeeHEerreeletLEAEIEDLRETIAETEREREELAEEVRDLRERLEELE 292
|
90 100
....*....|....*....|....*..
gi 598070671 3379 SLLNSLTNERERWKGSIKRFADQRERL 3405
Cdd:PRK02224 293 EERDDLLAEAGLDDADAEAVEARREEL 319
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3311-3405 |
5.81e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3311 IAPLREEVQRLETQTKKTKTQLIVIDEMIHELEESIEKYKDDYSELIRETENIKTEMKTVEKKVERSLSLLNSLTNERER 3390
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90
....*....|....*
gi 598070671 3391 WKGSIKRFADQRERL 3405
Cdd:TIGR02168 759 LEAEIEELEERLEEA 773
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
3309-3397 |
6.71e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 3309 QTIAPLREEVQRLETQTKKTKTQLIVIDEMIHELEESIEKYKDDYSELIRETEN---IKTEMKTVEKKVERSLSLLNSLT 3385
Cdd:COG2433 406 RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERReirKDREISRLDREIERLERELEEER 485
|
90
....*....|..
gi 598070671 3386 NERERWKGSIKR 3397
Cdd:COG2433 486 ERIEELKRKLER 497
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
2486-2630 |
7.10e-03 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 40.34 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2486 RHEYLVYSILNEHRPLLLCGPPGSGKTMtLLEALRKSpqldvLSLNFSKdtspISLLKSLEQFCEY--KKSNRGIQLAPK 2563
Cdd:cd19481 14 RGSRLRRYGLGLPKGILLYGPPGTGKTL-LAKALAGE-----LGLPLIV----VKLSSLLSKYVGEseKNLRKIFERARR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2564 VSGkwVVVFCDEINL-------PKMDKYGTQQVISLIRLMVEhkgfwrtgdqqWVSLENIQFVGACNSP-------KDPG 2629
Cdd:cd19481 84 LAP--CILFIDEIDAigrkrdsSGESGELRRVLNQLLTELDG-----------VNSRSKVLVIAATNRPdlldpalLRPG 150
|
.
gi 598070671 2630 R 2630
Cdd:cd19481 151 R 151
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
2145-2251 |
9.93e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 39.25 E-value: 9.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 598070671 2145 IMLVGESGSGKSTILNSVLHALsevENVEHTSIVIDAKVLSK-----EQIYGKLDLVTRDWTDGLftSVLRRIRENLRGE 2219
Cdd:pfam13401 8 LVLTGESGTGKTTLLRRLLEQL---PEVRDSVVFVDLPSGTSpkdllRALLRALGLPLSGRLSKE--ELLAALQQLLLAL 82
|
90 100 110
....*....|....*....|....*....|...
gi 598070671 2220 LSKRIWIVFDCD-IDPQWAENLNSVLDDNRILT 2251
Cdd:pfam13401 83 AVAVVLIIDEAQhLSLEALEELRDLLNLSSKLL 115
|
|
| |
