|
Name |
Accession |
Description |
Interval |
E-value |
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1253-4563 |
0e+00 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 803.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1253 IEKINeINKKEELEWSKKCDLLKQSEVLLEKQRYTFPTNWLYIDNIIGKLETVKQICKYQIKLiKDYLPYIQSMVLDFDR 1332
Cdd:COG5245 289 MDSLA-RLIVDRICEYVSIEWLGCCEELLTCSMESMSSLVNSFDGEESEAMSLESSLFYEFRG-GEHLAGFYSAFGDIKR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1333 KvqNNIKELFEEWNKNKPSHGNANSTKALQIITTFEERIDIINEQ-YEISEKIRKLLELENSESEIGfHVSPNILKEEIn 1411
Cdd:COG5245 367 I--LLFTWSFKKLGTLLPSLPGYSSGGMDYGEEYRSLLWELGSEVgDPDSGPVRKWMRKDLFDAKVR-SGVSFGKQEEF- 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1412 cvkgIWDELKIIYSNICDMKKMLWSNVDpkDVKHRLNNLLESiKKIPaKYRQYEIFDNVQNEIQQYLKTYSLLLDLKSES 1491
Cdd:COG5245 443 ----VSDIFNITFERIHGMDPTTLEDDE--EDTPALAILLGQ-EEAG-RFVKLCKIMRMFSFFNSLEMFSRRTLANRMAI 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1492 LKerHWKLILQKLNIKIYYNKLTLGNLWSLHLCIHENVLSEILNQAQGEMA--LEQFLRGLKDTWNEYELElvqyqnkcK 1569
Cdd:COG5245 515 VK--YLSSVVRTGPLFLQRDFFGRMSELLMARDMFMEVDGVLRLFFGGEWSgiVQLSGIRRAKRCVERQID--------D 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1570 LIKGWndifstIDDHLNAIQSMKISSYikiFEEETftwdDKLNRLRNLLDVWMnvqRKWVYLEGVLKGSSDIKSLLPQEY 1649
Cdd:COG5245 585 EIREW------CSSVLSDDFLEERAVR---VERGA----DGARRLRASSGSPV---LRRLDEYLMMMSLEDLMPLIPHAV 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1650 NRFKIIDSDFINIMKKTSDKPKLLELFQMEGFQkQLDRLSDSLSKIQKALGEYLEKQRNKFPRFyfVGDEDLLEMIGNSK 1729
Cdd:COG5245 649 HRKMSLVSGVRGIYKRVVSGCEAINTILEDVGD-DLDLFYKEMDQVFMSIEKVLGLRWREVERA--SEVEELMDRVRELE 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1730 DAKIIQRNVNKMFAGINSFILKEntnDIILGMSSREGEevlfleALNISSFNTLKEWLIVLE---KSMKSSLEFYLDeAA 1806
Cdd:COG5245 726 NRVYSYRFFVKKIAKEEMKTVFS---SRIQKKEPFSLD------SEAYVGFFRLYEKSIVIRginRSMGRVLSQYLE-SV 795
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1807 KEILEMDMIEctkiennkilLWSEKYPNQIILLCLQiLWTTNIENELinfskNPPdeSNTLFHKSEKICLNLLEFLAVNV 1886
Cdd:COG5245 796 QEALEIEDGS----------FFVSRHRVRDGGLEKG-RGCDAWENCF-----DPP--LSEYFRILEKIFPSEEGYFFDEV 857
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1887 VKQKDhrtrqkfvQMITELVHQRDVIRILIDKNVNNVNSFIWLQYMRYYWDSKKKenkinLIIKMADATFEYGYEYLGMC 1966
Cdd:COG5245 858 LKRLD--------PGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLYKR-----FIKVRSSYRSAEMFAKNTIP 924
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1967 EKLVQTELTDACFLTLTQALKMKLGGNpfgpAGTGKTESVKALGAQLGRYVlvfncdESFDFTAmgRIFVGLCQVGAWGc 2046
Cdd:COG5245 925 FFVFEHSMDTSQHQKLFEAVCDEVCRF----VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG- 991
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2047 FDEFNRLEERILsAVSEQILTIQTSLVQRKNEIEILNKKIGLNKNVGIFVTMNPgyagRSNLPDNLKQLFRSFAMIEPNk 2126
Cdd:COG5245 992 TEESALLDEISR-TILVDEYLNSDEFRMLEELNSAVVEHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSNIPF- 1065
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2127 qlivevtlfsqGFISA--EHLSSKIVSLFDLCSEQLSKQPHYDFglRSLKSVLnsagnlkrltllKDESKYVQNNQIGFN 2204
Cdd:COG5245 1066 -----------GAIKSrrESLDREIGAFNNEVDGIAREEDELMF--YPMFKSL------------KAKHRMLEEKTEYLN 1120
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2205 ETLdnnnnndnnnerktttntnesniismeQTLLLKSVCDTVYPKlvsSDIIliqsllkgvfpnvnvgDLEEKGLINEIH 2284
Cdd:COG5245 1121 KIL---------------------------SITGLPLISDTLRER---IDTL----------------DAEWDSFCRISE 1154
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2285 RLCKLRHFTPEEKWITKICQIYQIMKLQHGVMLVGDVGTGKSSAWKILLDsleaLDNIKGVSYVIDaksldkeeiygKLD 2364
Cdd:COG5245 1155 SLKKYESQQVSGLDVAQFVSFLRSVDTGAFHAEYFRVFLCKIKHYTDACD----YLWHVKSPYVKK-----------KYF 1219
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2365 NINLEWTdGVFTGILRKIIynsstQSGNTNKRHWIVFDgdvdpEWAENLNSVLDDNKLLTLPNGERlpipesvRILFE-V 2443
Cdd:COG5245 1220 DADMELR-QFFLMFNREDM-----EARLADSKMEYEVE-----RYVEKTKAEVSSLKLELSSVGEG-------QVVVSnL 1281
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2444 DTlkhaTLATVSRCGMIWFSRDILSPIILFKHKLnmlkyGDNDYPrkmdkfklllinnneriteknqngnengnenekkn 2523
Cdd:COG5245 1282 GS----IGDKVGRCLVEYDSISRLSTKGVFLDEL-----GDTKRY----------------------------------- 1317
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2524 iniinnnnsnnsnniysmnhmnnynvnanehnlqqfdnIDSENIMdnirmnsrifFEENEQetsssyiirtipyraVNII 2603
Cdd:COG5245 1318 --------------------------------------LDECLDF----------FSCFEE---------------VQKE 1334
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2604 SDYFEeNEFVHQCLVEAENYEHVMDYEYIRVIESTCLLLQKgfdnLVKKNEKINNTLSDDDIEKYISKWLVVSILWGIGG 2683
Cdd:COG5245 1335 IDELS-MVFCADALRFSADLYHIVKERRFSGVLAGSDASES----LGGKSIELAAILEHKDLIVEMKRGINDVLKLRIFG 1409
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2684 SLNLETREKFSMFVQSICSIPLPNDLLSKGKMPNMDNTnkisntlldyqpnieDGEWINWKELVQIIDVDRTEISDATLV 2763
Cdd:COG5245 1410 DKCRESTPRFYLISDGDLIKDLNERSDYEEMLIMMFNI---------------SAVITNNGSIAGFELRGERVMLRKEVV 1474
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2764 IETMDTIRHETILEGWLHLKKPFILCGPPGSGKTMTLTSVLKKSSEFDIASLNFSSGSLPNLLLQTFDHYCEYVKTTSEL 2843
Cdd:COG5245 1475 IPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSLRSELITEVKYFNFSTCTMTPSKLSVLERETEYYPNTGVV 1554
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2844 VLRPLQPGKWLIIFADEINLPTPDKYDTQRIIMFMRQIYESQGFWKYDVNNnswnWVKIERITFAGACNPPTDAGRNPLS 2923
Cdd:COG5245 1555 RLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSSIAVS----WVTICGIILYGACNPGTDEGRVKYY 1630
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2924 NRFLRHTSVLYVDFPGYESLKQIYGTFNRAILRKFPQSSHMADNLTQAMVDFYTKFSETFTIDMQPHYIYSPRELTRWKL 3003
Cdd:COG5245 1631 ERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASVELYLSSKDKTKFFLQMNYGYKPRELTRSLR 1710
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3004 ALYETLESCDELKTKDLVRLCICEGLRIFQDRLIYKKEKKETDKIIDDIFKYSFPDITKEDLL-RPILFNSYMKNYYTEI 3082
Cdd:COG5245 1711 AIFGYAETRIDTPDVSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREMIAGHIGeAEITFSMILFFGMACL 1790
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3083 DKKDLKVLILSKLKIFNEEEINVQLVLFDDVLDHITRIDRVLRLPLGHLLLVGASGAGKTILSRFVSWINGLSVFQIRAG 3162
Cdd:COG5245 1791 LKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGH 1870
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3163 RNYTTESFEADLRHIMKRAGIKEEKITFIFDESNVLGPAFLERMNALLASGEVPGLFEGDNYITLINECKSAYRS-NIGL 3241
Cdd:COG5245 1871 RDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFEStSLEK 1950
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3242 D-ESDIFKKFTKQVQQNLHIVFTM-NPANPDFANrQATSPALFNRCVIDWFGDWPYSALLQVASEFIfnlILPDNNFYMD 3319
Cdd:COG5245 1951 DtEATLTRVFLVYMEENLPVVFSAcCSQDTSVLA-GIRSPALKNRCFIDFKKLWDTEEMSQYANSVE---TLSRDGGRVF 2026
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3320 YVGNEDGPIKGKIQYKNnkayfLSRAIVEIHNSVVHINnvlMKKGNryNYMTPRDFLDFIKHFLKIIDEKKEEVSSQKNH 3399
Cdd:COG5245 2027 FINGELGVGKGALISEV-----FGDDAVVIEGRGFEIS---MIEGS--LGESKIKFIGGLKVYDARCVIYIEELDCTNVN 2096
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3400 LNSGLNKLKDTEIQVAELRNSLAIKKKTLAEKDLEAEEKMKLMIEQQTETEDKKKKAEILSKKLDEQFIIIDQRKEVVRK 3479
Cdd:COG5245 2097 LVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMK 2176
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3480 ELSEVEPKFREAEEAVKNIPKKNFDELRAMANPPILVRNAVEAVAILImneGDKNVTWEDARKIMKGQDFINKVL-YLDK 3558
Cdd:COG5245 2177 FKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLL---GFEAKIWFGEQQSLRRDDFIRIIGkYPDE 2253
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3559 KAVKPQTSSQIKKR-INNNDWDVERINKASRAAGPLAKWVESVITFLNILETVQPLEKEIEKLQEETKVAEDQYNEQRDI 3637
Cdd:COG5245 2254 IEFDLEARRFREAReCSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGL 2333
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3638 ICELEKKLVQYKNDYAQLISQVQNIKQEMEMVENKIKRSINLIDNLKSEKERWSETFINLEEASETFVGDCLIAAAFCAY 3717
Cdd:COG5245 2334 SSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPY 2413
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3718 IGFFEHYERQRLKRTWGEIIKMHY-IKYRNDLSFIEFLSRPSERLQWIGNelpSDDLSIENA-IIINNYIRYPMIIDPSD 3795
Cdd:COG5245 2414 IGTLGFLCRAIEFGMSFIRISKEFrDKEIRRRQFITEGVQKIEDFKEEAC---STDYGLENSrIRKDLQDLTAVLNDPSS 2490
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3796 QATTFLLNQYSDKKILKTSFSDKNFIKNLESALRFGSTLLVYDVEKIDAILNSVLNQETHKQGGRLLITIGDSEVDFSPS 3875
Cdd:COG5245 2491 KIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSDKIIGDAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTV 2570
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3876 FNLFLTSRDAHFQFTPDLCSRVTFVNFTLTPSSLQNQCLNMILKNERPDIDKKRCDLLKLQGEYKVKIRELEESLLLELS 3955
Cdd:COG5245 2571 EAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLM 2650
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3956 NVKGNILDDDNVISTMEKLKVQGAEASKEVNIAEEVMVEVENVSNQYLFLAQGSARIYFILQHLCNINFLYQYDLNFFFN 4035
Cdd:COG5245 2651 LSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSS 2730
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 4036 IMKDMFNndhllsiVKKKDHYKERLKVLEDLLFsltynrvargLLQEDRYVFglqlcyvksiinpnidmdqsyLHYLlkd 4115
Cdd:COG5245 2731 EFEKWRR-------MKSKYLCAIRYMLMSSEWI----------LDHEDRSGF---------------------IHRL--- 2769
|
2890 2900 2910 2920 2930 2940 2950 2960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 4116 hysnqeidEFEHKKIEKNLLpeyndeqinalnnlikhksfsnlkKCILNNKqkwiellhsAEPEELVCSILNDMNMSEES 4195
Cdd:COG5245 2770 --------DVSFLLRTKRFV------------------------STLLEDK---------NYRQVLSSCSLYGNDVISHS 2808
|
2970 2980 2990 3000 3010 3020 3030 3040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 4196 MDKsdemlnknknlnilnnveFGKDddipeekryinndntnmdtttknnnnmnnnnnmnnnNNYMLQNKNDISSCLKESL 4275
Cdd:COG5245 2809 CDR------------------FDRD------------------------------------VYRALKHQMDNRTHSTILT 2834
|
3050 3060 3070 3080 3090 3100 3110 3120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 4276 IIKAIRPDKLEnCFNKIINHILGRDFLWIPElsmnDFEKYVKENANGNIPIVLIsspgfdpsnkvqqLSEKCKIPLFSIA 4355
Cdd:COG5245 2835 SNSKTNPYKEY-TYNDSWAEAFEVEDSGDLY----KFEEGLLELIVGHAPLIYA-------------HKKSLENERNVDR 2896
|
3130 3140 3150 3160 3170 3180 3190 3200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 4356 MGSEEGYISAERVIFTAQSNGGWVLLKNIHISTKW----LHELEKNIHKATTNKNFRLFLT-MEFNPRIPQSLMRISLTF 4430
Cdd:COG5245 2897 LGSKENEVYAVLNSLFSRKEKSWFEVYNISLSFGWfkryVEDVVYPIKASRVCGKVKNMWTsMVDADMLPIQLLIAIDSF 2976
|
3210 3220 3230 3240 3250 3260 3270 3280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 4431 MFEPPVGIKFSILRSF-SLFLENRELcepKIARLRLYFIVSYLHAIILERRRYTPIGWTKKYEFSDSDLMCAlsvvdswl 4509
Cdd:COG5245 2977 VSSTYPETGCGYADLVeIDRYPFDYT---LVIACDDAFYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFK-------- 3045
|
3290 3300 3310 3320 3330
....*....|....*....|....*....|....*....|....*....|....
gi 1371546339 4510 dkasTKIGKNVSEHIDPCNIPWEAIKKILNEAIYGGRLDNMVDQKILDTFIDHL 4563
Cdd:COG5245 3046 ----THLLKNILFLNHLNARKWGNNRDLIFTIVYGKKHSLMEDSKVVDKYCRGY 3095
|
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1958-2326 |
8.31e-162 |
|
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: 503.55 E-value: 8.31e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1958 YGYEYLGMCEKLVQTELTDACFLTLTQALKMKLGGNPFGPAGTGKTESVKALGAQLGRYVLVFNCDESFDFTAMGRIFVG 2037
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2038 LCQVGAWGCFDEFNRLEERILSAVSEQILTIQTSLVQRKNEIEILNKKIGLNKNVGIFVTMNPGYAGRSNLPDNLKQLFR 2117
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2118 SFAMIEPNKQLIVEVTLFSQGFISAEHLSSKIVSLFDLCSEQLSKQPHYDFGLRSLKSVLNSAGNLKRltllkdeskyvq 2197
Cdd:pfam12774 161 PVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKR------------ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2198 nnqigfnetldnnnnndnnnerkttTNTNESniismEQTLLLKSVCDTVYPKLVSSDIILIQSLLKGVFPNVNVGDLEEK 2277
Cdd:pfam12774 229 -------------------------SNPNLN-----EDVLLLRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYG 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1371546339 2278 GLINEIHRLCKLRHFTPEEKWITKICQIYQIMKLQHGVMLVGDVGTGKS 2326
Cdd:pfam12774 279 ELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVGPTGSGKT 327
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
284-854 |
4.45e-98 |
|
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: 329.92 E-value: 4.45e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 284 INQLQKDVTKWIEDIQKLTRLNGEFKSGGsALSEINFWIGYENALYQLESQLKNPEVILTLHILKNAKRYFATMSFDSDI 363
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQGRNPG-PLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKALDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 364 QLKQSKEYVLNVNILMKDF--PIEDLLGATSIQQIIQAVRNIFNHL-KKLKNTTKYPLS-RSYNFVESLSRDLNNTMKKV 439
Cdd:pfam08385 80 ELTDALNEAKDNVKYLKTLerPFEDLEELTDPPEIIEAIPPLMNTIrLIWSISRYYNTSeRMTVLLEKISNQLIEQCKKY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 440 LCTQSLMNMDYEEFDVLISGCVEIFRLWNEEMRIFKDMVRELIKKRSFNerAPAKMVFEHI-HLQERLDEIKKFRKQHEK 518
Cdd:pfam08385 160 LSPEGIFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERPWD--FSERYIFGRFdAFLERLEKILELFETIEQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 519 FkSVISTVFGSNNKSLG--I-NLYKDINTAYNIF--LSLDPLDLSKNGednWEKAKLSYESKVNRVESQITFKLRDQLGG 593
Cdd:pfam08385 238 F-SKLEKIGGTKGPELEgvIeEILEEFQEAYKVFksKTYDILDVSNEG---FDDDYEEFKERIKDLERRLQAFIDQAFDD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 594 SKTSAEMFHAFSKFNPLFFRPKIRGAIQEYQNTLIQIVVDDLRKLQMIYINGYlksdSQKVSTIRDIPLVAGSIIWAKQI 673
Cdd:pfam08385 314 ARSTESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDKQK----YNPSPIAKNMPPVAGAIIWARQL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 674 ERKLEDSLKRIENVLGRGweQHSEGKILRQNIDNFKNLLSQ--NKTFEKWLKNIKSADKFDMYDNIINIKKLGGNNYEIl 751
Cdd:pfam08385 390 FRRIQEPMKRFKEELGLL--KHAEGKKVIKKYNELAKKLDEyeRLIYEAWLKEVEEASEGNLKRPLLVRHPETGKLLSV- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 752 aNYDFQFFNIFKEVRYLQSINLRVPYSIKVKADETKLIYPYALTLQKTFRTYMKICISMdnqakdvpfNQTIKKLVAAIH 831
Cdd:pfam08385 467 -NFDPQLLALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTL---------LPVERPLLAPHL 536
|
570 580
....*....|....*....|....
gi 1371546339 832 NTVQNKIKEGIY-LHWDSDIIETY 854
Cdd:pfam08385 537 KDIDEKLEPGLTtLTWNSLGIDEY 560
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4748-5061 |
4.42e-27 |
|
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein heavy chain. This domain is a complex structure comprising six alpha-helices and an incomplete six-stranded antiparallel beta-barrel. The shape of this domain is distinctively flat, spreading over the AAA1, AAA5 and AAA6 domain.
Pssm-ID: 465677 Cd Length: 301 Bit Score: 115.03 E-value: 4.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 4748 INKILENLPQNI---PCLEKNEEKLRNAVFRCFERENNLFSDLLKLIKTNLNQLKNVLEEKVKYTNKIRALAKDLNSFNV 4824
Cdd:pfam18199 37 AKDILEKLPEPFdieEAEEKYPVGYEDPLNTVLLQEIERFNKLLKVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 4825 PSNWLLDGNTTNLNLTNWLKELINRLYQIIVItlefnekscIDINEKKKQkniniennedhnlndfykrnndnilshfkl 4904
Cdd:pfam18199 117 PESWAKKSYPSLKPLGSWIRDLLERLKQLQDW---------LDDEGPPKV------------------------------ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 4905 nnkekklsinfIWLGGLFYPRAFITATRQLSAFKFKNSLDDLELSVLIgnnnnMKYDDMIHFT--------ITCLSIEGA 4976
Cdd:pfam18199 158 -----------FWLSGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEV-----TKKVSPEEVTeppedgvyVHGLFLEGA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 4977 EWSNKDNCLILSD--ELTIDLPPVTLTWEKKEILKQKQKesssslhFMNLPIYLDKSRNS--FIgfWNFPVSKGISEQIW 5052
Cdd:pfam18199 222 RWDRKNGCLVESEpkELFSPLPVIHLKPVESDKKKLDEN-------TYECPVYKTSERHStnFV--FSVDLPTDKPPDHW 292
|
....*....
gi 1371546339 5053 YQRGVAIFL 5061
Cdd:pfam18199 293 ILRGVALLL 301
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3382-3682 |
8.49e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 8.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3382 FLKIIDEKKE-EVSSQKNHLNSGLNKLKDTEIQVAELRNSLAIKKKTLAEKDLEAEEKMKLMIEQQTETEDKKKK---AE 3457
Cdd:TIGR02168 215 YKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyaLA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3458 ILSKKLDEQFIIIDQRKEVVRKELSEVEPKfREAEEAVKNIPKKNFDELRAMANPpilVRNAVEAVAILIMNEGDKnvtW 3537
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQ-LEELESKLDELAEELAELEEKLEE---LKEELESLEAELEELEAE---L 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3538 EDARKIMKGQDfiNKVLYLDKKAVKP-QTSSQIKKRINNNDWDVERINK-----ASRAAGPLAKWVESviTFLNILETVQ 3611
Cdd:TIGR02168 368 EELESRLEELE--EQLETLRSKVAQLeLQIASLNNEIERLEARLERLEDrrerlQQEIEELLKKLEEA--ELKELQAELE 443
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371546339 3612 PLEKEIEKLQEETKVAEDQYNEQRDIICELEKKLVQYKNDYAQLISQVQNIKQEMEMVENKIKRSINLIDN 3682
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2779-2929 |
5.11e-06 |
|
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: 49.45 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2779 WLHLKKPFILCGPPGSGKTMTLTSVLKKSSEFDIASLNFSSGSLPNLLLqtfdhYCEYVKTTSELVLR-PLQPGKWLIIF 2857
Cdd:cd00009 15 ELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLV-----VAELFGHFLVRLLFeLAEKAKPGVLF 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371546339 2858 ADEINLPTPDKydTQRIIMFMRQIYESQgfwkydvnnnswnwVKIERITFAGACNPPTDAG-RNPLSNRFLRH 2929
Cdd:cd00009 90 IDEIDSLSRGA--QNALLRVLETLNDLR--------------IDRENVRVIGATNRPLLGDlDRALYDRLDIR 146
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3388-3705 |
9.63e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3388 EKKEEVSSQKNHLNSGLNKLKDTEIQVAELRNSLAIKKKTLAEKDLEAEEKMKLMIEQQTETEDKKKKAEILSKKLDEQf 3467
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE- 1645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3468 iiiDQRKEVVRKElsEVEPKFREAEEAVK-NIPKKNFDELRAMAnppilvrnaveavailimnegdknvtwEDARKimkg 3546
Cdd:PTZ00121 1646 ---KKKAEELKKA--EEENKIKAAEEAKKaEEDKKKAEEAKKAE---------------------------EDEKK---- 1689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3547 qdfinKVLYLDKKAVKPQTSSQIKKRINNNDWDVERINKASRAAGPLAkwvesvitflnilETVQPLEKEIEKLQEETKV 3626
Cdd:PTZ00121 1690 -----AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA-------------EEAKKEAEEDKKKAEEAKK 1751
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3627 AEDQYNEQRDIICELEKKLVQYKNDYAQLISqvQNIKQEMEMVENKIKRSI-NLIDNLKSEKERWSETFINLEEASETFV 3705
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE--EELDEEDEKRRMEVDKKIkDIFDNFANIIEGGKEGNLVINDSKEMED 1829
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1253-4563 |
0e+00 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 803.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1253 IEKINeINKKEELEWSKKCDLLKQSEVLLEKQRYTFPTNWLYIDNIIGKLETVKQICKYQIKLiKDYLPYIQSMVLDFDR 1332
Cdd:COG5245 289 MDSLA-RLIVDRICEYVSIEWLGCCEELLTCSMESMSSLVNSFDGEESEAMSLESSLFYEFRG-GEHLAGFYSAFGDIKR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1333 KvqNNIKELFEEWNKNKPSHGNANSTKALQIITTFEERIDIINEQ-YEISEKIRKLLELENSESEIGfHVSPNILKEEIn 1411
Cdd:COG5245 367 I--LLFTWSFKKLGTLLPSLPGYSSGGMDYGEEYRSLLWELGSEVgDPDSGPVRKWMRKDLFDAKVR-SGVSFGKQEEF- 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1412 cvkgIWDELKIIYSNICDMKKMLWSNVDpkDVKHRLNNLLESiKKIPaKYRQYEIFDNVQNEIQQYLKTYSLLLDLKSES 1491
Cdd:COG5245 443 ----VSDIFNITFERIHGMDPTTLEDDE--EDTPALAILLGQ-EEAG-RFVKLCKIMRMFSFFNSLEMFSRRTLANRMAI 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1492 LKerHWKLILQKLNIKIYYNKLTLGNLWSLHLCIHENVLSEILNQAQGEMA--LEQFLRGLKDTWNEYELElvqyqnkcK 1569
Cdd:COG5245 515 VK--YLSSVVRTGPLFLQRDFFGRMSELLMARDMFMEVDGVLRLFFGGEWSgiVQLSGIRRAKRCVERQID--------D 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1570 LIKGWndifstIDDHLNAIQSMKISSYikiFEEETftwdDKLNRLRNLLDVWMnvqRKWVYLEGVLKGSSDIKSLLPQEY 1649
Cdd:COG5245 585 EIREW------CSSVLSDDFLEERAVR---VERGA----DGARRLRASSGSPV---LRRLDEYLMMMSLEDLMPLIPHAV 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1650 NRFKIIDSDFINIMKKTSDKPKLLELFQMEGFQkQLDRLSDSLSKIQKALGEYLEKQRNKFPRFyfVGDEDLLEMIGNSK 1729
Cdd:COG5245 649 HRKMSLVSGVRGIYKRVVSGCEAINTILEDVGD-DLDLFYKEMDQVFMSIEKVLGLRWREVERA--SEVEELMDRVRELE 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1730 DAKIIQRNVNKMFAGINSFILKEntnDIILGMSSREGEevlfleALNISSFNTLKEWLIVLE---KSMKSSLEFYLDeAA 1806
Cdd:COG5245 726 NRVYSYRFFVKKIAKEEMKTVFS---SRIQKKEPFSLD------SEAYVGFFRLYEKSIVIRginRSMGRVLSQYLE-SV 795
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1807 KEILEMDMIEctkiennkilLWSEKYPNQIILLCLQiLWTTNIENELinfskNPPdeSNTLFHKSEKICLNLLEFLAVNV 1886
Cdd:COG5245 796 QEALEIEDGS----------FFVSRHRVRDGGLEKG-RGCDAWENCF-----DPP--LSEYFRILEKIFPSEEGYFFDEV 857
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1887 VKQKDhrtrqkfvQMITELVHQRDVIRILIDKNVNNVNSFIWLQYMRYYWDSKKKenkinLIIKMADATFEYGYEYLGMC 1966
Cdd:COG5245 858 LKRLD--------PGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLYKR-----FIKVRSSYRSAEMFAKNTIP 924
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1967 EKLVQTELTDACFLTLTQALKMKLGGNpfgpAGTGKTESVKALGAQLGRYVlvfncdESFDFTAmgRIFVGLCQVGAWGc 2046
Cdd:COG5245 925 FFVFEHSMDTSQHQKLFEAVCDEVCRF----VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG- 991
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2047 FDEFNRLEERILsAVSEQILTIQTSLVQRKNEIEILNKKIGLNKNVGIFVTMNPgyagRSNLPDNLKQLFRSFAMIEPNk 2126
Cdd:COG5245 992 TEESALLDEISR-TILVDEYLNSDEFRMLEELNSAVVEHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSNIPF- 1065
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2127 qlivevtlfsqGFISA--EHLSSKIVSLFDLCSEQLSKQPHYDFglRSLKSVLnsagnlkrltllKDESKYVQNNQIGFN 2204
Cdd:COG5245 1066 -----------GAIKSrrESLDREIGAFNNEVDGIAREEDELMF--YPMFKSL------------KAKHRMLEEKTEYLN 1120
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2205 ETLdnnnnndnnnerktttntnesniismeQTLLLKSVCDTVYPKlvsSDIIliqsllkgvfpnvnvgDLEEKGLINEIH 2284
Cdd:COG5245 1121 KIL---------------------------SITGLPLISDTLRER---IDTL----------------DAEWDSFCRISE 1154
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2285 RLCKLRHFTPEEKWITKICQIYQIMKLQHGVMLVGDVGTGKSSAWKILLDsleaLDNIKGVSYVIDaksldkeeiygKLD 2364
Cdd:COG5245 1155 SLKKYESQQVSGLDVAQFVSFLRSVDTGAFHAEYFRVFLCKIKHYTDACD----YLWHVKSPYVKK-----------KYF 1219
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2365 NINLEWTdGVFTGILRKIIynsstQSGNTNKRHWIVFDgdvdpEWAENLNSVLDDNKLLTLPNGERlpipesvRILFE-V 2443
Cdd:COG5245 1220 DADMELR-QFFLMFNREDM-----EARLADSKMEYEVE-----RYVEKTKAEVSSLKLELSSVGEG-------QVVVSnL 1281
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2444 DTlkhaTLATVSRCGMIWFSRDILSPIILFKHKLnmlkyGDNDYPrkmdkfklllinnneriteknqngnengnenekkn 2523
Cdd:COG5245 1282 GS----IGDKVGRCLVEYDSISRLSTKGVFLDEL-----GDTKRY----------------------------------- 1317
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2524 iniinnnnsnnsnniysmnhmnnynvnanehnlqqfdnIDSENIMdnirmnsrifFEENEQetsssyiirtipyraVNII 2603
Cdd:COG5245 1318 --------------------------------------LDECLDF----------FSCFEE---------------VQKE 1334
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2604 SDYFEeNEFVHQCLVEAENYEHVMDYEYIRVIESTCLLLQKgfdnLVKKNEKINNTLSDDDIEKYISKWLVVSILWGIGG 2683
Cdd:COG5245 1335 IDELS-MVFCADALRFSADLYHIVKERRFSGVLAGSDASES----LGGKSIELAAILEHKDLIVEMKRGINDVLKLRIFG 1409
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2684 SLNLETREKFSMFVQSICSIPLPNDLLSKGKMPNMDNTnkisntlldyqpnieDGEWINWKELVQIIDVDRTEISDATLV 2763
Cdd:COG5245 1410 DKCRESTPRFYLISDGDLIKDLNERSDYEEMLIMMFNI---------------SAVITNNGSIAGFELRGERVMLRKEVV 1474
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2764 IETMDTIRHETILEGWLHLKKPFILCGPPGSGKTMTLTSVLKKSSEFDIASLNFSSGSLPNLLLQTFDHYCEYVKTTSEL 2843
Cdd:COG5245 1475 IPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSLRSELITEVKYFNFSTCTMTPSKLSVLERETEYYPNTGVV 1554
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2844 VLRPLQPGKWLIIFADEINLPTPDKYDTQRIIMFMRQIYESQGFWKYDVNNnswnWVKIERITFAGACNPPTDAGRNPLS 2923
Cdd:COG5245 1555 RLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSSIAVS----WVTICGIILYGACNPGTDEGRVKYY 1630
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2924 NRFLRHTSVLYVDFPGYESLKQIYGTFNRAILRKFPQSSHMADNLTQAMVDFYTKFSETFTIDMQPHYIYSPRELTRWKL 3003
Cdd:COG5245 1631 ERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASVELYLSSKDKTKFFLQMNYGYKPRELTRSLR 1710
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3004 ALYETLESCDELKTKDLVRLCICEGLRIFQDRLIYKKEKKETDKIIDDIFKYSFPDITKEDLL-RPILFNSYMKNYYTEI 3082
Cdd:COG5245 1711 AIFGYAETRIDTPDVSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREMIAGHIGeAEITFSMILFFGMACL 1790
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3083 DKKDLKVLILSKLKIFNEEEINVQLVLFDDVLDHITRIDRVLRLPLGHLLLVGASGAGKTILSRFVSWINGLSVFQIRAG 3162
Cdd:COG5245 1791 LKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGH 1870
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3163 RNYTTESFEADLRHIMKRAGIKEEKITFIFDESNVLGPAFLERMNALLASGEVPGLFEGDNYITLINECKSAYRS-NIGL 3241
Cdd:COG5245 1871 RDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFEStSLEK 1950
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3242 D-ESDIFKKFTKQVQQNLHIVFTM-NPANPDFANrQATSPALFNRCVIDWFGDWPYSALLQVASEFIfnlILPDNNFYMD 3319
Cdd:COG5245 1951 DtEATLTRVFLVYMEENLPVVFSAcCSQDTSVLA-GIRSPALKNRCFIDFKKLWDTEEMSQYANSVE---TLSRDGGRVF 2026
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3320 YVGNEDGPIKGKIQYKNnkayfLSRAIVEIHNSVVHINnvlMKKGNryNYMTPRDFLDFIKHFLKIIDEKKEEVSSQKNH 3399
Cdd:COG5245 2027 FINGELGVGKGALISEV-----FGDDAVVIEGRGFEIS---MIEGS--LGESKIKFIGGLKVYDARCVIYIEELDCTNVN 2096
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3400 LNSGLNKLKDTEIQVAELRNSLAIKKKTLAEKDLEAEEKMKLMIEQQTETEDKKKKAEILSKKLDEQFIIIDQRKEVVRK 3479
Cdd:COG5245 2097 LVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMK 2176
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3480 ELSEVEPKFREAEEAVKNIPKKNFDELRAMANPPILVRNAVEAVAILImneGDKNVTWEDARKIMKGQDFINKVL-YLDK 3558
Cdd:COG5245 2177 FKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLL---GFEAKIWFGEQQSLRRDDFIRIIGkYPDE 2253
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3559 KAVKPQTSSQIKKR-INNNDWDVERINKASRAAGPLAKWVESVITFLNILETVQPLEKEIEKLQEETKVAEDQYNEQRDI 3637
Cdd:COG5245 2254 IEFDLEARRFREAReCSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGL 2333
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3638 ICELEKKLVQYKNDYAQLISQVQNIKQEMEMVENKIKRSINLIDNLKSEKERWSETFINLEEASETFVGDCLIAAAFCAY 3717
Cdd:COG5245 2334 SSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPY 2413
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3718 IGFFEHYERQRLKRTWGEIIKMHY-IKYRNDLSFIEFLSRPSERLQWIGNelpSDDLSIENA-IIINNYIRYPMIIDPSD 3795
Cdd:COG5245 2414 IGTLGFLCRAIEFGMSFIRISKEFrDKEIRRRQFITEGVQKIEDFKEEAC---STDYGLENSrIRKDLQDLTAVLNDPSS 2490
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3796 QATTFLLNQYSDKKILKTSFSDKNFIKNLESALRFGSTLLVYDVEKIDAILNSVLNQETHKQGGRLLITIGDSEVDFSPS 3875
Cdd:COG5245 2491 KIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSDKIIGDAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTV 2570
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3876 FNLFLTSRDAHFQFTPDLCSRVTFVNFTLTPSSLQNQCLNMILKNERPDIDKKRCDLLKLQGEYKVKIRELEESLLLELS 3955
Cdd:COG5245 2571 EAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLM 2650
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3956 NVKGNILDDDNVISTMEKLKVQGAEASKEVNIAEEVMVEVENVSNQYLFLAQGSARIYFILQHLCNINFLYQYDLNFFFN 4035
Cdd:COG5245 2651 LSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSS 2730
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 4036 IMKDMFNndhllsiVKKKDHYKERLKVLEDLLFsltynrvargLLQEDRYVFglqlcyvksiinpnidmdqsyLHYLlkd 4115
Cdd:COG5245 2731 EFEKWRR-------MKSKYLCAIRYMLMSSEWI----------LDHEDRSGF---------------------IHRL--- 2769
|
2890 2900 2910 2920 2930 2940 2950 2960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 4116 hysnqeidEFEHKKIEKNLLpeyndeqinalnnlikhksfsnlkKCILNNKqkwiellhsAEPEELVCSILNDMNMSEES 4195
Cdd:COG5245 2770 --------DVSFLLRTKRFV------------------------STLLEDK---------NYRQVLSSCSLYGNDVISHS 2808
|
2970 2980 2990 3000 3010 3020 3030 3040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 4196 MDKsdemlnknknlnilnnveFGKDddipeekryinndntnmdtttknnnnmnnnnnmnnnNNYMLQNKNDISSCLKESL 4275
Cdd:COG5245 2809 CDR------------------FDRD------------------------------------VYRALKHQMDNRTHSTILT 2834
|
3050 3060 3070 3080 3090 3100 3110 3120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 4276 IIKAIRPDKLEnCFNKIINHILGRDFLWIPElsmnDFEKYVKENANGNIPIVLIsspgfdpsnkvqqLSEKCKIPLFSIA 4355
Cdd:COG5245 2835 SNSKTNPYKEY-TYNDSWAEAFEVEDSGDLY----KFEEGLLELIVGHAPLIYA-------------HKKSLENERNVDR 2896
|
3130 3140 3150 3160 3170 3180 3190 3200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 4356 MGSEEGYISAERVIFTAQSNGGWVLLKNIHISTKW----LHELEKNIHKATTNKNFRLFLT-MEFNPRIPQSLMRISLTF 4430
Cdd:COG5245 2897 LGSKENEVYAVLNSLFSRKEKSWFEVYNISLSFGWfkryVEDVVYPIKASRVCGKVKNMWTsMVDADMLPIQLLIAIDSF 2976
|
3210 3220 3230 3240 3250 3260 3270 3280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 4431 MFEPPVGIKFSILRSF-SLFLENRELcepKIARLRLYFIVSYLHAIILERRRYTPIGWTKKYEFSDSDLMCAlsvvdswl 4509
Cdd:COG5245 2977 VSSTYPETGCGYADLVeIDRYPFDYT---LVIACDDAFYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFK-------- 3045
|
3290 3300 3310 3320 3330
....*....|....*....|....*....|....*....|....*....|....
gi 1371546339 4510 dkasTKIGKNVSEHIDPCNIPWEAIKKILNEAIYGGRLDNMVDQKILDTFIDHL 4563
Cdd:COG5245 3046 ----THLLKNILFLNHLNARKWGNNRDLIFTIVYGKKHSLMEDSKVVDKYCRGY 3095
|
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1958-2326 |
8.31e-162 |
|
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: 503.55 E-value: 8.31e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1958 YGYEYLGMCEKLVQTELTDACFLTLTQALKMKLGGNPFGPAGTGKTESVKALGAQLGRYVLVFNCDESFDFTAMGRIFVG 2037
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2038 LCQVGAWGCFDEFNRLEERILSAVSEQILTIQTSLVQRKNEIEILNKKIGLNKNVGIFVTMNPGYAGRSNLPDNLKQLFR 2117
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2118 SFAMIEPNKQLIVEVTLFSQGFISAEHLSSKIVSLFDLCSEQLSKQPHYDFGLRSLKSVLNSAGNLKRltllkdeskyvq 2197
Cdd:pfam12774 161 PVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKR------------ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2198 nnqigfnetldnnnnndnnnerkttTNTNESniismEQTLLLKSVCDTVYPKLVSSDIILIQSLLKGVFPNVNVGDLEEK 2277
Cdd:pfam12774 229 -------------------------SNPNLN-----EDVLLLRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYG 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1371546339 2278 GLINEIHRLCKLRHFTPEEKWITKICQIYQIMKLQHGVMLVGDVGTGKS 2326
Cdd:pfam12774 279 ELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVGPTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1406-1805 |
3.76e-123 |
|
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: 395.86 E-value: 3.76e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1406 LKEEINCVKGIWDELKIIYSNICDMKKMLWSNVDPKDVKHRLNNLLESIKKIPAKYRQYEIFDNVQNEIQQYLKTYSLLL 1485
Cdd:pfam08393 4 IKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLPLIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1486 DLKSESLKERHWKLILQKLNIKI--YYNKLTLGNLWSLHLCIHENVLSEILNQAQGEMALEQFLRGLKDTWNEYELELVQ 1563
Cdd:pfam08393 84 DLRNPALRERHWKQLSEILGFDFdpLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFELVP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1564 YQN-KCKLIKGWNDIFSTIDDHLNAIQSMKISSYIKIFEEETFTWDDKLNRLRNLLDVWMNVQRKWVYLEGVLkGSSDIK 1642
Cdd:pfam08393 164 YKDtGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIF-SSEDIR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1643 SLLPQEYNRFKIIDSDFINIMKKTSDKPKLLELFQMEGFQKQLDRLSDSLSKIQKALGEYLEKQRNKFPRFYFVGDEDLL 1722
Cdd:pfam08393 243 KQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLSNDELL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 1723 EMIGNSKDAKIIQRNVNKMFAGINSfiLKENTNDIILGMSSREGEEVLFLEALNISSFNtLKEWLIVLEKSMKSSLEFYL 1802
Cdd:pfam08393 323 EILSQTKDPTRVQPHLKKCFEGIAS--LEFDENKEITGMISKEGEVVPFSKPPVEAKGN-VEEWLNELEEEMRETLRDLL 399
|
...
gi 1371546339 1803 DEA 1805
Cdd:pfam08393 400 KEA 402
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
284-854 |
4.45e-98 |
|
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: 329.92 E-value: 4.45e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 284 INQLQKDVTKWIEDIQKLTRLNGEFKSGGsALSEINFWIGYENALYQLESQLKNPEVILTLHILKNAKRYFATMSFDSDI 363
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQGRNPG-PLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKALDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 364 QLKQSKEYVLNVNILMKDF--PIEDLLGATSIQQIIQAVRNIFNHL-KKLKNTTKYPLS-RSYNFVESLSRDLNNTMKKV 439
Cdd:pfam08385 80 ELTDALNEAKDNVKYLKTLerPFEDLEELTDPPEIIEAIPPLMNTIrLIWSISRYYNTSeRMTVLLEKISNQLIEQCKKY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 440 LCTQSLMNMDYEEFDVLISGCVEIFRLWNEEMRIFKDMVRELIKKRSFNerAPAKMVFEHI-HLQERLDEIKKFRKQHEK 518
Cdd:pfam08385 160 LSPEGIFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERPWD--FSERYIFGRFdAFLERLEKILELFETIEQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 519 FkSVISTVFGSNNKSLG--I-NLYKDINTAYNIF--LSLDPLDLSKNGednWEKAKLSYESKVNRVESQITFKLRDQLGG 593
Cdd:pfam08385 238 F-SKLEKIGGTKGPELEgvIeEILEEFQEAYKVFksKTYDILDVSNEG---FDDDYEEFKERIKDLERRLQAFIDQAFDD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 594 SKTSAEMFHAFSKFNPLFFRPKIRGAIQEYQNTLIQIVVDDLRKLQMIYINGYlksdSQKVSTIRDIPLVAGSIIWAKQI 673
Cdd:pfam08385 314 ARSTESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDKQK----YNPSPIAKNMPPVAGAIIWARQL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 674 ERKLEDSLKRIENVLGRGweQHSEGKILRQNIDNFKNLLSQ--NKTFEKWLKNIKSADKFDMYDNIINIKKLGGNNYEIl 751
Cdd:pfam08385 390 FRRIQEPMKRFKEELGLL--KHAEGKKVIKKYNELAKKLDEyeRLIYEAWLKEVEEASEGNLKRPLLVRHPETGKLLSV- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 752 aNYDFQFFNIFKEVRYLQSINLRVPYSIKVKADETKLIYPYALTLQKTFRTYMKICISMdnqakdvpfNQTIKKLVAAIH 831
Cdd:pfam08385 467 -NFDPQLLALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTL---------LPVERPLLAPHL 536
|
570 580
....*....|....*....|....
gi 1371546339 832 NTVQNKIKEGIY-LHWDSDIIETY 854
Cdd:pfam08385 537 KDIDEKLEPGLTtLTWNSLGIDEY 560
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3761-3980 |
9.60e-79 |
|
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: 260.84 E-value: 9.60e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3761 LQWIGNELPSDDLSIENAIIINNYIRYPMIIDPSDQATTFLLNQYSDKKILKTSFSDKNFIKNLESALRFGSTLLVYDV- 3839
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3840 EKIDAILNSVLNQETHKQGGRLLITIGDSEVDFSPSFNLFLTSRDAHFQFTPDLCSRVTFVNFTLTPSSLQNQCLNMILK 3919
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371546339 3920 NERPDIDKKRCDLLKLQGEYKVKIRELEESLLLELSNVKGNILDDDNVISTMEKLKVQGAE 3980
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEE 221
|
|
| AAA_8 |
pfam12780 |
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
3107-3385 |
7.56e-55 |
|
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: 193.59 E-value: 7.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3107 LVLFDDVLDHITRIDRVLRLPLGHLLLVGASGAGKTILSRFVSWINGLSVFQIRAGRNYTTESFEADLRHIMKRAGIKEE 3186
Cdd:pfam12780 3 LVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3187 KITFIFDESNVLGPAFLERMNALLASGEVPGLFEGDNYITLINECKS-AYRSNIGLDESDIFKKFTKQVQQNLHIVFTMN 3265
Cdd:pfam12780 83 PTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDdAKAQNIEDSREAVYNYFVKRCRNNLHIVLCMS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3266 PANPDFANRQATSPALFNRCVIDWFGDWPYSALLQVASEFIFNLILPDNnfymdyvgnedgpikgkiqYKNNkayfLSRA 3345
Cdd:pfam12780 163 PVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFLEDIEIPEE-------------------LKSN----VVKV 219
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1371546339 3346 IVEIHNSVVHINNVLMKKGNRYNYMTPRDFLDFIKHFLKI 3385
Cdd:pfam12780 220 FVYVHSSVEDMSKKFYEELKRKNYVTPKSYLELLRLYKNL 259
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
3400-3733 |
2.72e-39 |
|
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: 151.76 E-value: 2.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3400 LNSGLNKLKDTEIQVAELRNSLAIKKKTLAEKDLEAEEKMKLMIEQQTETEDKKKKAEILSKKLDEQFIIIDQRKEVVRK 3479
Cdd:pfam12777 3 LENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKACEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3480 ELSEVEPKFREAEEAVKNIPKKNFDELRAMANPPILVRNAVEAVAILIMNEGD--KNVTWEDARKIMKGQD-FINKVLYL 3556
Cdd:pfam12777 83 DLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMAPGGKipKDKSWKAAKIMMAKVDgFLDSLIKF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3557 DKKAVKPQTSSQIKKRINNNDWDVERINKASRAAGPLAKWVESVITFLNILETVQPLEKEIEKLQEETKVAEDQYNEQRD 3636
Cdd:pfam12777 163 DKEHIHEACLKAFKPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQEKLAAIKA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3637 IICELEKKLVQYKNDYAQLISQVQNIKQEMEMVENKIKRSINLIDNLKSEKERWSETFINLEEASETFVGDCLIAAAFCA 3716
Cdd:pfam12777 243 KIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDILLISAFIS 322
|
330
....*....|....*...
gi 1371546339 3717 YIGFF-EHYERQRLKRTW 3733
Cdd:pfam12777 323 YLGFFtKKYRNELLDKFW 340
|
|
| AAA_lid_11 |
pfam18198 |
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the ... |
4464-4617 |
6.62e-36 |
|
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: 134.89 E-value: 6.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 4464 RLYFIVSYLHAIILERRRYTPIGWTKKYEFSDSDLMCALSVVDSWLDKASTKigknvsehidpcnIPWEAIKKILNEAIY 4543
Cdd:pfam18198 3 KLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLDEYDEK-------------IPWDALRYLIGEINY 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371546339 4544 GGRLDNMVDQKILDTFIDHLMNSNSFETDFKLnicnstslnkdflvSPDLFR-----NINDYINWTNNMSNTDLPAWLG 4617
Cdd:pfam18198 70 GGRVTDDWDRRLLNTYLEEFFNPEVLEEDFKF--------------SPSLYYippdgDLEDYLEYIESLPLVDSPEVFG 134
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
4323-4428 |
9.79e-33 |
|
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: 124.86 E-value: 9.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 4323 NIPIVLISSPGFDPSNKVQQLSEKCKIP--LFSIAMGSEEGYIsAERVIFTAQSNGGWVLLKNIHISTKWLHELEK---N 4397
Cdd:pfam03028 3 TTPLIFILSPGSDPTADLEKLAKKLGFGgkLHSISLGQGQGPI-AEKLIEEAAKEGGWVLLQNCHLALSWMPELEKileE 81
|
90 100 110
....*....|....*....|....*....|.
gi 1371546339 4398 IHKATTNKNFRLFLTMEFNPRIPQSLMRISL 4428
Cdd:pfam03028 82 LPEETLHPDFRLWLTSEPSPKFPISILQNSI 112
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2762-2938 |
2.06e-31 |
|
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: 123.27 E-value: 2.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2762 LVIETMDTIRHETILEGWLHLKKPFILCGPPGSGKTMTLTSVLKK--SSEFDIASLNFSSGSLPNLLLQTFDHYCEYVKT 2839
Cdd:pfam12775 10 ILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKldKEKYLPLFINFSAQTTSNQTQDIIESKLEKRRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2840 TselVLRPLqPGKWLIIFADEINLPTPDKYDTQRIIMFMRQIYEsQGFWkYDVNNNSwnWVKIERITFAGACNPPTdAGR 2919
Cdd:pfam12775 90 G---VYGPP-GGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLD-YGGW-YDRKKLT--FKEIVDVQFVAAMGPPG-GGR 160
|
170
....*....|....*....
gi 1371546339 2920 NPLSNRFLRHTSVLYVDFP 2938
Cdd:pfam12775 161 NDITPRLLRHFNVFNITFP 179
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4748-5061 |
4.42e-27 |
|
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein heavy chain. This domain is a complex structure comprising six alpha-helices and an incomplete six-stranded antiparallel beta-barrel. The shape of this domain is distinctively flat, spreading over the AAA1, AAA5 and AAA6 domain.
Pssm-ID: 465677 Cd Length: 301 Bit Score: 115.03 E-value: 4.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 4748 INKILENLPQNI---PCLEKNEEKLRNAVFRCFERENNLFSDLLKLIKTNLNQLKNVLEEKVKYTNKIRALAKDLNSFNV 4824
Cdd:pfam18199 37 AKDILEKLPEPFdieEAEEKYPVGYEDPLNTVLLQEIERFNKLLKVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 4825 PSNWLLDGNTTNLNLTNWLKELINRLYQIIVItlefnekscIDINEKKKQkniniennedhnlndfykrnndnilshfkl 4904
Cdd:pfam18199 117 PESWAKKSYPSLKPLGSWIRDLLERLKQLQDW---------LDDEGPPKV------------------------------ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 4905 nnkekklsinfIWLGGLFYPRAFITATRQLSAFKFKNSLDDLELSVLIgnnnnMKYDDMIHFT--------ITCLSIEGA 4976
Cdd:pfam18199 158 -----------FWLSGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEV-----TKKVSPEEVTeppedgvyVHGLFLEGA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 4977 EWSNKDNCLILSD--ELTIDLPPVTLTWEKKEILKQKQKesssslhFMNLPIYLDKSRNS--FIgfWNFPVSKGISEQIW 5052
Cdd:pfam18199 222 RWDRKNGCLVESEpkELFSPLPVIHLKPVESDKKKLDEN-------TYECPVYKTSERHStnFV--FSVDLPTDKPPDHW 292
|
....*....
gi 1371546339 5053 YQRGVAIFL 5061
Cdd:pfam18199 293 ILRGVALLL 301
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
2603-2745 |
1.16e-21 |
|
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: 93.50 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2603 ISDYFEEneFVHQCLVEA-ENYEHVMDYEYIRVIESTCLLLQKGFDNLVKKNEKinNTLSDDDIEKYISKWLVVSILWGI 2681
Cdd:pfam17852 1 LEPLFEW--LVPPALEFVrKNCKEIVPTSDLNLVQSLCRLLESLLDEVLEYNGV--HPLSPDKLKEYLEKLFLFALVWSI 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371546339 2682 GGSLNLETREKFSMFVQsicsiplpnDLLSKGKMPNMDNtnkisNTLLDYQPNIEDGEWINWKE 2745
Cdd:pfam17852 77 GGTLDEDSRKKFDEFLR---------ELFSGLDLPPPEK-----GTVYDYFVDLEKGEWVPWSD 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2314-2457 |
3.94e-11 |
|
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: 63.85 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2314 GVMLVGDVGTGKSSAWKILLdslEALDNiKGVSYVIDAKSLDKEEIYGKLDNINL--EWTDGVFTGILRKiiynsstqsg 2391
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLA---AALSN-RPVFYVQLTRDTTEEDLFGRRNIDPGgaSWVDGPLVRAARE---------- 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371546339 2392 ntnkrHWIVFDGDVD---PEWAENLNSVLDDNKLLTLPNGERLPI-PESVRILFEVDTL----KHATLATVSRC 2457
Cdd:pfam07728 67 -----GEIAVLDEINranPDVLNSLLSLLDERRLLLPDGGELVKAaPDGFRLIATMNPLdrglNELSPALRSRF 135
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3382-3682 |
8.49e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 8.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3382 FLKIIDEKKE-EVSSQKNHLNSGLNKLKDTEIQVAELRNSLAIKKKTLAEKDLEAEEKMKLMIEQQTETEDKKKK---AE 3457
Cdd:TIGR02168 215 YKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyaLA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3458 ILSKKLDEQFIIIDQRKEVVRKELSEVEPKfREAEEAVKNIPKKNFDELRAMANPpilVRNAVEAVAILIMNEGDKnvtW 3537
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQ-LEELESKLDELAEELAELEEKLEE---LKEELESLEAELEELEAE---L 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3538 EDARKIMKGQDfiNKVLYLDKKAVKP-QTSSQIKKRINNNDWDVERINK-----ASRAAGPLAKWVESviTFLNILETVQ 3611
Cdd:TIGR02168 368 EELESRLEELE--EQLETLRSKVAQLeLQIASLNNEIERLEARLERLEDrrerlQQEIEELLKKLEEA--ELKELQAELE 443
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371546339 3612 PLEKEIEKLQEETKVAEDQYNEQRDIICELEKKLVQYKNDYAQLISQVQNIKQEMEMVENKIKRSINLIDN 3682
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2779-2929 |
5.11e-06 |
|
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: 49.45 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2779 WLHLKKPFILCGPPGSGKTMTLTSVLKKSSEFDIASLNFSSGSLPNLLLqtfdhYCEYVKTTSELVLR-PLQPGKWLIIF 2857
Cdd:cd00009 15 ELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLV-----VAELFGHFLVRLLFeLAEKAKPGVLF 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371546339 2858 ADEINLPTPDKydTQRIIMFMRQIYESQgfwkydvnnnswnwVKIERITFAGACNPPTDAG-RNPLSNRFLRH 2929
Cdd:cd00009 90 IDEIDSLSRGA--QNALLRVLETLNDLR--------------IDRENVRVIGATNRPLLGDlDRALYDRLDIR 146
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3388-3702 |
3.23e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3388 EKKEEVSSQKNHLNSGLNKLKDTEIQVAELRNSLAIKKKTLAEKDLEAEEKMKLM-IEQQTETEDKKKKAEILSKK---L 3463
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRlaeL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3464 DEQFIIIDQRKEVVRKELSEVEPKFREAEEavknipKKNFDELRAManppILVRNAVEAVAILIMNEGDKNVTWEDARKI 3543
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAAL------EERLKEARLL----LLIAAALLALLGLGGSLLSLILTIAGVLFL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3544 MKGQDFINKVLYLDKKAVKPQTSSQIKKRINNNDWDVERINKASRAAG-PLAKWVESVITFLNILETVQPLEKEIEKLQE 3622
Cdd:COG4717 282 VLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3623 EtkVAEDQYNEQRDIIC---------ELEKKLVQYKnDYAQLISQVQNIKQEmemVENKIKRSINLIDNLKSE--KERWS 3691
Cdd:COG4717 362 E--LQLEELEQEIAALLaeagvedeeELRAALEQAE-EYQELKEELEELEEQ---LEELLGELEELLEALDEEelEEELE 435
|
330
....*....|.
gi 1371546339 3692 ETFINLEEASE 3702
Cdd:COG4717 436 ELEEELEELEE 446
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3409-3693 |
5.28e-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: 50.07 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3409 DTEIQVAelRNSLAIKKKTLAEKDLEAEEKMKLMIEQQTETEDKKKKAEILSKKLDEQFIIIDQRKEVVRKELSEVEPKF 3488
Cdd:TIGR02169 169 DRKKEKA--LEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3489 REAEEAVKNIpKKNFDELRAmanppilvrnavEAVAILIMNEgdknvtwEDARKIMK-GQDFINkvlyldkkavkpqtss 3567
Cdd:TIGR02169 247 ASLEEELEKL-TEEISELEK------------RLEEIEQLLE-------ELNKKIKDlGEEEQL---------------- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3568 QIKKRINNNDWDVERINKASRAAgplakwvesvitflniletvqplEKEIEKLQEETKVAEDQYNEQRDIICELEKKLVQ 3647
Cdd:TIGR02169 291 RVKEKIGELEAEIASLERSIAEK-----------------------ERELEDAEERLAKLEAEIDKLLAEIEELEREIEE 347
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3648 YKNDYAQLISQVQNIKQEMEMVENKI----KRSINLIDNLKSEKERWSET 3693
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEELEDLRAELeevdKEFAETRDELKDYREKLEKL 397
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3388-3705 |
9.63e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3388 EKKEEVSSQKNHLNSGLNKLKDTEIQVAELRNSLAIKKKTLAEKDLEAEEKMKLMIEQQTETEDKKKKAEILSKKLDEQf 3467
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE- 1645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3468 iiiDQRKEVVRKElsEVEPKFREAEEAVK-NIPKKNFDELRAMAnppilvrnaveavailimnegdknvtwEDARKimkg 3546
Cdd:PTZ00121 1646 ---KKKAEELKKA--EEENKIKAAEEAKKaEEDKKKAEEAKKAE---------------------------EDEKK---- 1689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3547 qdfinKVLYLDKKAVKPQTSSQIKKRINNNDWDVERINKASRAAGPLAkwvesvitflnilETVQPLEKEIEKLQEETKV 3626
Cdd:PTZ00121 1690 -----AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA-------------EEAKKEAEEDKKKAEEAKK 1751
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3627 AEDQYNEQRDIICELEKKLVQYKNDYAQLISqvQNIKQEMEMVENKIKRSI-NLIDNLKSEKERWSETFINLEEASETFV 3705
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE--EELDEEDEKRRMEVDKKIkDIFDNFANIIEGGKEGNLVINDSKEMED 1829
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3373-3703 |
5.05e-04 |
|
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: 46.59 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3373 RDFLDFIKHFLKIIDEKKEEVSSQKNHLNSGLNKLKDTEIQVAELRNSLAIKKKTLAEKDLEAEEKMKLMIEQQTETEDK 3452
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3453 KKKAEILSKKLDEQFIIIDQRKEVVRKELSEVEPKFREAEEAVKNIPKKNFDELRAMANppiLVRNAVEAVAILIMNEGD 3532
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED---LEEQIEELSEDIESLAAE 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3533 KNVTWEDARKImkgQDFINKVlyLDKKAVKPQTSSQIKKRINN-----NDWDvERINKASRAAGPLAKWVESVITflnil 3607
Cdd:TIGR02168 861 IEELEELIEEL---ESELEAL--LNERASLEEALALLRSELEElseelRELE-SKRSELRRELEELREKLAQLEL----- 929
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3608 eTVQPLEKEIEKLQEetKVAEDQYNEQRDIIcELEKKLVqykndyaqliSQVQNIKQEMEMVENKIKR--SINL--IDNL 3683
Cdd:TIGR02168 930 -RLEGLEVRIDNLQE--RLSEEYSLTLEEAE-ALENKIE----------DDEEEARRRLKRLENKIKElgPVNLaaIEEY 995
|
330 340
....*....|....*....|....*
gi 1371546339 3684 KSEKERWSetFIN-----LEEASET 3703
Cdd:TIGR02168 996 EELKERYD--FLTaqkedLTEAKET 1018
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3604-3688 |
7.00e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3604 LNILETVQPLEKEIEKLQEETKVAEDQYNEQRDIICELEKKLVQYKNDYAQLISQVQNIKQEMEMVENKIKRSINLIDNL 3683
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV 85
|
....*
gi 1371546339 3684 KSEKE 3688
Cdd:COG1579 86 RNNKE 90
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
3374-3688 |
9.73e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3374 DFLDFIKHFLKIIDEKKEEVSSQKNHLNSGLNKLKDT----EIQVAELRNSLAIKKKTLAEKDLEAE----------EKM 3439
Cdd:TIGR04523 307 DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQisqlKKELTNSESENSEKQRELEEKQNEIEklkkenqsykQEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3440 KLMIEQQTETEDKKKKAEILSKKLDEQFIIIDQRKEVVRKELSEV---------EPKFREAEEAVKNIPKKNFDELRAMA 3510
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLketiiknnsEIKDLTNQDSVKELIIKNLDNTRESL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3511 NppilvrNAVEAVAILIMNEGD--KNVTWEDARKIMKGQDFINKVLYLDKKAVK-PQTSSQIKKRINNNDWDVERINKAS 3587
Cdd:TIGR04523 467 E------TQLKVLSRSINKIKQnlEQKQKELKSKEKELKKLNEEKKELEEKVKDlTKKISSLKEKIEKLESEKKEKESKI 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3588 RAAGPLAKWVESVITFLNILETVQPLEKEIEKLQEETKVAEDQYNEQRDIICELEKKLVQYKNDYAQLISQVQNIKQEME 3667
Cdd:TIGR04523 541 SDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELE 620
|
330 340
....*....|....*....|.
gi 1371546339 3668 MVENKIKRSINLIDNLKSEKE 3688
Cdd:TIGR04523 621 KAKKENEKLSSIIKNIKSKKN 641
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3379-3692 |
1.03e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3379 IKHFLKIIDEKKEEVSSQKNHLNSGLNKLKDteiQVAELRNSLAIKKKT-----LAEKDLEAEEKMKLMieqqtetedKK 3453
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKK---EIKELKKAIEELKKAkgkcpVCGRELTEEHRKELL---------EE 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3454 KKAEIlsKKLDEQFIIIDQRKEVVRKELSEVEPKFREAEEAVKNipKKNFDELRAMA------NPPILVRNAVEAVAI-- 3525
Cdd:PRK03918 457 YTAEL--KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL--KELAEQLKELEeklkkyNLEELEKKAEEYEKLke 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3526 -LIMNEGDKNVTWEDARKImkgQDFINKVLYLDKKAVKPQTS-SQIKKRINNNDWdvERINKASRAAGPLAKWVESVITF 3603
Cdd:PRK03918 533 kLIKLKGEIKSLKKELEKL---EELKKKLAELEKKLDELEEElAELLKELEELGF--ESVEELEERLKELEPFYNEYLEL 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3604 LNILETVQPLEKEIEKLQEETKVAEDQYNEQRDIICELEKKLVQYK------------NDYAQLISQVQNIKQEMEMVEN 3671
Cdd:PRK03918 608 KDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEkkyseeeyeelrEEYLELSRELAGLRAELEELEK 687
|
330 340
....*....|....*....|.
gi 1371546339 3672 KIKRSINLIDNLKSEKERWSE 3692
Cdd:PRK03918 688 RREEIKKTLEKLKEELEEREK 708
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3383-3702 |
1.13e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3383 LKIIDEKKEEVSSQKNHLNSGLNKLKDTEIQVAELrnslaikkktlaEKDLEAEEKMKlmiEQQTETEDKKKKAEILSK- 3461
Cdd:PRK03918 323 INGIEERIKELEEKEERLEELKKKLKELEKRLEEL------------EERHELYEEAK---AKKEELERLKKRLTGLTPe 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3462 KLDEQFIIIDQRKEVVRKELSEVEPKFREAEEAVKNIpKKNFDELR-AMANPPILVRNAVEAVAILIMNE---------G 3531
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL-KKAIEELKkAKGKCPVCGRELTEEHRKELLEEytaelkrieK 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3532 DKNVTWEDARKIMKGQDFINKVLYLDKKAVK-PQTSSQIKKRINN-NDWDVERINKASRAA----GPLAKWVESVITFLN 3605
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESELIKlKELAEQLKELEEKlKKYNLEELEKKAEEYeklkEKLIKLKGEIKSLKK 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3606 ILETVQPLEKEIEKLQEETKVAEDQYNEQRDIIC--------ELEKKLVQYKNDYAQLISqVQNIKQEMEMVENKIKRSI 3677
Cdd:PRK03918 547 ELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfesveELEERLKELEPFYNEYLE-LKDAEKELEREEKELKKLE 625
|
330 340
....*....|....*....|....*
gi 1371546339 3678 NLIDnlKSEKErWSETFINLEEASE 3702
Cdd:PRK03918 626 EELD--KAFEE-LAETEKRLEELRK 647
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2785-2928 |
1.43e-03 |
|
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: 41.89 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 2785 PFILCGPPGSGKTMTLTSVLKKSSEFDIASLNFSSGSLPNLLLQTFDhyceYVKTTSELVLRPL----QPGKwlIIFADE 2860
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQLTRDTTEEDLFGRRN----IDPGGASWVDGPLvraaREGE--IAVLDE 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371546339 2861 INLPTPDKYDTQRIIMFMRQIYESQGFWKYDVNNNSWNwvkieritFAGACNPPtDAGRNPLSNRFLR 2928
Cdd:pfam07728 75 INRANPDVLNSLLSLLDERRLLLPDGGELVKAAPDGFR--------LIATMNPL-DRGLNELSPALRS 133
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3602-3707 |
2.40e-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: 44.66 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3602 TFLNILETVQPLEKEIEKLQEETKVAEDQYNEQRDIICELEKKLVQYKNDYAQLISQVQNIKQEMEMVENKIKRSINLID 3681
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
90 100
....*....|....*....|....*.
gi 1371546339 3682 NLKSEKErwsetfiNLEEASETFVGD 3707
Cdd:TIGR02168 369 ELESRLE-------ELEEQLETLRSK 387
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3388-3495 |
2.95e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3388 EKKEEVSSQKNHLNSGLNKLKDT----EIQVAELRNSLAIKKKTLAEKDLEAEEKmKLMIEQQT----ETEDKKKKAEIL 3459
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEElqrlSEELADLNAAIAGIEAKINELEEEKEDK-ALEIKKQEwkleQLAADLSKYEQE 470
|
90 100 110
....*....|....*....|....*....|....*.
gi 1371546339 3460 SKKLDEQFIIIDQRKEVVRKELSEVEPKFREAEEAV 3495
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3391-3675 |
3.21e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3391 EEVSSQKNHLNSGLNKLKDTEIQVAELRNSLAIKKKTLAEKDLEAEekmklMIEQQTETEdkKKKAEILSKKLDEqfiiI 3470
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-----QLEQEEEKL--KERLEELEEDLSS----L 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3471 DQRKEVVRKELSEVEPKFREAEEAVKNIpKKNFDELRAMANPPIlVRNAVEAvailiMNEGDKNVTWEDARKIMKGQDfI 3550
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDLHKL-EEALNDLEARLSHSR-IPEIQAE-----LSKLEEEVSRIEARLREIEQK-L 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3551 NKVLYLDKKAvkpQTSSQIKKRINNnDWDverINKASRAagplaKWVESVITFLNILET--------VQPLEKEIEKLQE 3622
Cdd:TIGR02169 822 NRLTLEKEYL---EKEIQELQEQRI-DLK---EQIKSIE-----KEIENLNGKKEELEEeleeleaaLRDLESRLGDLKK 889
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1371546339 3623 ETKVAEDQYNEQRDIICELEKKLVQYKNDYAQLISQVQNIKQEMEMVENKIKR 3675
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3384-3507 |
4.52e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3384 KIIDEKKEEVSSQKNHLNSGLNKLKDTEIQVAELRNSLAIKKKTLAEKDLEAEEKMKLMIEQQTETEDKKKKAEiLSKKL 3463
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE-EAKKA 1670
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1371546339 3464 DEqfiiiDQRK-EVVRKELSE----VEPKFREAEEA--VKNIPKKNFDELR 3507
Cdd:PTZ00121 1671 EE-----DKKKaEEAKKAEEDekkaAEALKKEAEEAkkAEELKKKEAEEKK 1716
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3613-3703 |
4.69e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3613 LEKEIEKLQEETKVAEDQYNEQRDIICELEKKLVQYKNDYAQLISQVQNIKQEMEMVENKIKRSINLIDNLKSEKERWSE 3692
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
90
....*....|.
gi 1371546339 3693 TFINLEEASET 3703
Cdd:COG1196 331 ELEELEEELEE 341
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3397-3700 |
9.26e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3397 KNHLNSGLNKLKDTEIQVAELRNSLAIKKKTLAEKDLEAEEKMKLMIEQQTETEDKKKKAEILsKKLDEQFIIIDQRKEV 3476
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-EELKEEIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3477 VRKELSEVEPKFREAEEAVKNIpKKNFDELRamanppilvrnavEAVAILIMNEGDKnvtwEDARKIMKGQDFINKVLY- 3555
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEEL-KKEIEELE-------------EKVKELKELKEKA----EEYIKLSEFYEEYLDELRe 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546339 3556 LDKKAVK-PQTSSQIKKRINNNDWDVERINKASRAAGPLAKWVESVITFLNILETVQPLEKEIEKLQEETKVAEdqyneq 3634
Cdd:PRK03918 312 IEKRLSRlEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLT------ 385
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371546339 3635 rdiICELEKKLvqykndyaqlisqvQNIKQEMEMVENKIKRSINLIDNLKSEKERWSETFINLEEA 3700
Cdd:PRK03918 386 ---PEKLEKEL--------------EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434
|
|
| |
