|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1651-1986 |
8.35e-174 |
|
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: 537.84 E-value: 8.35e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1651 YTYEYQGNASKLVYTPLTDKCYLTLTQAMKMGLGGNPYGPAGTGKTESVKALGGLLGRQVLVFNCDEGIDVKSMGRIFVG 1730
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1731 LVKCGAWGCFDEFNRLEESVLSAVSMQIQTIQDALKNHRTVCELLGKEVEVNSNSGIFITMNPagkGYGGRQKLPDNLKQ 1810
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNP---GYAGRTELPDNLKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1811 LFRPVAMSHPDNELIAEVILYSEGFKDAKVLSRKLVAIFNLSRELLTPQQHYDWGLRALKTVLRGSGNLLRQlnksgtTQ 1890
Cdd:pfam12774 158 LFRPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRS------NP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1891 NANESHIVVQALRLNTMSKFTFTDCTRFDALIKDVFPGIELKEVEYDELSAALKQVFEEANYEIIPNQIKKALELYEQLC 1970
Cdd:pfam12774 232 NLNEDVLLLRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETML 311
|
330
....*....|....*.
gi 311033479 1971 QRMGVVIVGPSGAGKS 1986
Cdd:pfam12774 312 VRHGVMLVGPTGSGKT 327
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1361-4016 |
1.38e-159 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 559.61 E-value: 1.38e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1361 LPKEQTRFNRVDEDFRSIMTDIKKDNRvTTLTTHAGIRNSLLTILDQLQRCQKSLNEFLEEKRSAFPRFyfIGDDDLLEI 1440
Cdd:COG5245 644 IPHAVHRKMSLVSGVRGIYKRVVSGCE-AINTILEDVGDDLDLFYKEMDQVFMSIEKVLGLRWREVERA--SEVEELMDR 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1441 LGQSTNPSVIQSHLKKLFAGINSVCFdeKSKHITAMKSLEGEVVPFKNKVPL--SNNVETWLNDlalEMKKTLEQLLkEC 1518
Cdd:COG5245 721 VRELENRVYSYRFFVKKIAKEEMKTV--FSSRIQKKEPFSLDSEAYVGFFRLyeKSIVIRGINR---SMGRVLSQYL-ES 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1519 VttGRSSQGAvDPSLFPSQILC---LAEQIKFTEDVENAIkdhslhqiETQLVnklEQYTNIDTSSEDPGNTESGILELK 1595
Cdd:COG5245 795 V--QEALEIE-DGSFFVSRHRVrdgGLEKGRGCDAWENCF--------DPPLS---EYFRILEKIFPSEEGYFFDEVLKR 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1596 LKALILDIIHNIDVVKQLNQIQVHTTEDWAWKKQLRFYMKSDHTCCVQMVDSEFQYTYEYQGNASKLVYTPLTDKCYLTL 1675
Cdd:COG5245 861 LDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMDTSQHQKL 940
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1676 TQAMKMGLGGNpygpAGTGKTESVKALGGLLGRQVlvfncdEGIDVKSmgRIFVGLVKCGAWGcFDEFNRLEESVLsAVS 1755
Cdd:COG5245 941 FEAVCDEVCRF----VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISR-TIL 1006
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1756 MQIQTIQDALKNHRTVCELLGKEVEVNSNSGIFITMNPagkgyggRQKLPDNLKQLFRPVAMSHPDNElIAEVilysegf 1835
Cdd:COG5245 1007 VDEYLNSDEFRMLEELNSAVVEHGLKSPSTPVEMIINE-------RNIVLEIGRRALDMFLSNIPFGA-IKSR------- 1071
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1836 kdAKVLSRKLVAIFNLSRELLTPQQHYDWglRALKTVLRGSGNLLRQLNKSGTTqnaneshiVVQALRLNTMSkftftdc 1915
Cdd:COG5245 1072 --RESLDREIGAFNNEVDGIAREEDELMF--YPMFKSLKAKHRMLEEKTEYLNK--------ILSITGLPLIS------- 1132
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1916 trfDALIKDvfpgIELKEVEYDEL-SAALKQVFEEANyEIIPNQIKKALELYEQLCQRMGVVIVGPSGAGKSTLWRmlrA 1994
Cdd:COG5245 1133 ---DTLRER----IDTLDAEWDSFcRISESLKKYESQ-QVSGLDVAQFVSFLRSVDTGAFHAEYFRVFLCKIKHYT---D 1201
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1995 ALCKTGKVVKQYTMNPKAMPRYQLLGHIDMDTREWSDGVLTNSARQVVREpqdvsswiicdgdidpEWIESLNSVLDDNR 2074
Cdd:COG5245 1202 ACDYLWHVKSPYVKKKYFDADMELRQFFLMFNREDMEARLADSKMEYEVE----------------RYVEKTKAEVSSLK 1265
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2075 LLTMPSGERiqfgpnvNFVFETHDlscASPATISRMGMIFLSDEETDLNSLIkSWLRNQPAEYRNN-------------- 2140
Cdd:COG5245 1266 LELSSVGEG-------QVVVSNLG---SIGDKVGRCLVEYDSISRLSTKGVF-LDELGDTKRYLDEcldffscfeevqke 1334
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2141 ----LENWIGD--YFEKALQWVLKQNDY-VVETSLVGTVMNG--LSHLHGCRDHDEFIINLIRGLGGNLNMKSRLEFTke 2211
Cdd:COG5245 1335 idelSMVFCADalRFSADLYHIVKERRFsGVLAGSDASESLGgkSIELAAILEHKDLIVEMKRGINDVLKLRIFGDKC-- 1412
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2212 vfhwaRESPPDFHKPMDTYYDSTRGRLATY--VLKKPEDLTADDFSNG-----------LTLP---VIQTPDMQRGLDYF 2275
Cdd:COG5245 1413 -----RESTPRFYLISDGDLIKDLNERSDYeeMLIMMFNISAVITNNGsiagfelrgerVMLRkevVIPTSDTGFVDSFS 1487
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2276 KPWLSsdTKQPFILVGPEGCGKGMLLRYAFSQLRSTQIATVHCSAQTTSRHLLQKLSQTcMVISTNTG--RVYRPKDCER 2353
Cdd:COG5245 1488 NEALN--TLRSYIYCGPPGSGKEMLMCPSLRSELITEVKYFNFSTCTMTPSKLSVLERE-TEYYPNTGvvRLYPKPVVKD 1564
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2354 LVLYLKDINLPKLDKWGTSTLVAFLQQVLTYQGFYDE-NLEWVGLENIQIVASMSAGGRLGRHKLTTRFTSIVRLCSIDY 2432
Cdd:COG5245 1565 LVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSSiAVSWVTICGIILYGACNPGTDEGRVKYYERFIRKPVFVFCCY 1644
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2433 PEREQLQTIYGAYLEPVLHKNLKNHSIwgssskIYLLAGSMVQVYEQVRAKFTVDDYSHYFFTPCILTQWVLGLFRYDLE 2512
Cdd:COG5245 1645 PELASLRNIYEAVLMGSYLCFDEFNRL------SEETMSASVELYLSSKDKTKFFLQMNYGYKPRELTRSLRAIFGYAET 1718
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2513 GgsSNHPLDYVLEIVAYEARRLFRDKIVGAKELHLFDIILTSVFQGDWGSDILDNMSDSFYVTWGARHNSgaraapgqpl 2592
Cdd:COG5245 1719 R--IDTPDVSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREMIAGHIGEAEITFSMILFFG---------- 1786
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2593 pphgkpLGKLNSTDLKDVIKKGLIHYGRDNQNLDILLFHEVLEYMSRIDRVLSFPGGSLLLAGRSGVGRRTITSLVSHMH 2672
Cdd:COG5245 1787 ------MACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLN 1860
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2673 GAVLFSPKISRGYELKQFKNDLKHVLQLAGIEAQQVVLLLEDYQFVHPTFLEMINSLLSSGEVPGLYTLEELEPLLLPLK 2752
Cdd:COG5245 1861 PRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLR 1940
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2753 DQASQDGFF----GPVFNYFTYRIQQNLHIVL-IMDSANSNFMINCESnPALHKKCQVLWMEGWSNSSMKKIP-EMLFSE 2826
Cdd:COG5245 1941 FVFESTSLEkdteATLTRVFLVYMEENLPVVFsACCSQDTSVLAGIRS-PALKNRCFIDFKKLWDTEEMSQYAnSVETLS 2019
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2827 TGGGEKYNDKKRKEEKKKNSVDPDFLKSFLLIHES-------CKAYGATPSRYMTFLHVYSAISSSKKKELLKRQSHLQA 2899
Cdd:COG5245 2020 RDGGRVFFINGELGVGKGALISEVFGDDAVVIEGRgfeismiEGSLGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVE 2099
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2900 GVSKLNEAKALVDELNRKAGEQSVLLKTKQDEADAALQMITVSMQDASEQKTELERLKHRIAEEVVKIEERKNKIDDELK 2979
Cdd:COG5245 2100 GVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKS 2179
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2980 EVQPLVNEAKLAVGNIKPESLSEIRSLRMPPDVIRDILEGVLRLMGIFDTSWVSMKSFLAKRGVREDIATFD-ARNISKE 3058
Cdd:COG5245 2180 SKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLLGFEAKIWFGEQQSLRRDDFIRIIGKYPdEIEFDLE 2259
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3059 IRESVEELLFKNKgSFDPKNAKRASTAAAPLAAWVKANIQYSHVLERIHPLETEQAGLESNLKKTEDRKRKLEELLNSVG 3138
Cdd:COG5245 2260 ARRFREARECSDP-SFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLM 2338
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3139 QKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHKRWNAQVVEITEELATLPKRAQLAAAFITYLSAAP 3218
Cdd:COG5245 2339 TFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLG 2418
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3219 ESLRKTCLEEWTKSAGLE---KFDLRRFLCTESEQLIWKSEGLP-SDDLSIENALVILQSR-VCPFLIDPSSQATEWLKT 3293
Cdd:COG5245 2419 FLCRAIEFGMSFIRISKEfrdKEIRRRQFITEGVQKIEDFKEEAcSTDYGLENSRIRKDLQdLTAVLNDPSSKIVTSQRQ 2498
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3294 HLKDSRLEVINQQDSNFITALELAVRFGKTLIIQEMDGVEPVLYPLLRRDLVAQGPRYVVQIGDKIIDYNEEFRLFLSTR 3373
Cdd:COG5245 2499 MYDEKKAILGSFREMEFAFGLSQARREGSDKIIGDAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSE 2578
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3374 NPNPFIPPDAASIVTEVNFTTTRSGLRGQLLALTIQHEKPDLEEQKTKLLQQEEDKKIQLAKLEESLLETLATSQGNILE 3453
Cdd:COG5245 2579 GRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQ 2658
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3454 NKDLIESLNQTKASSALIQESLKESYKLQISLDQERDAYLPLAESASKMYFIISDLSKINNMYRFSLAAFLRLFQRALQN 3533
Cdd:COG5245 2659 TDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFEKWRRM 2738
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3534 KqdSENTEQRIQSLISSLQHMVYEYICRCLFKAD--------QLMFALHFVRGMHPELfqENEWDTFTGVVVgdmlrkaD 3605
Cdd:COG5245 2739 K--SKYLCAIRYMLMSSEWILDHEDRSGFIHRLDvsfllrtkRFVSTLLEDKNYRQVL--SSCSLYGNDVIS-------H 2807
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3606 SQQKI-RDQLPSWIDQERSWAVATLKialpsLYQTLCFEDAAlwRTYYN--NSMCEQEFPSILAKkvslfqqilvvqalr 3682
Cdd:COG5245 2808 SCDRFdRDVYRALKHQMDNRTHSTIL-----TSNSKTNPYKE--YTYNDswAEAFEVEDSGDLYK--------------- 2865
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3683 pdrlqsamalfacKTLGLKEVSPLPLNLKRLYKETLEIEPIliiispgadpsqeLQELANAERSgecyhqvamgqgqaDL 3762
Cdd:COG5245 2866 -------------FEEGLLELIVGHAPLIYAHKKSLENERN-------------VDRLGSKENE--------------VY 2905
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3763 AIQMLKECARNGDWLCLKNLHLVVSWL-----PVLEKELNTLQPKDTFRLWLTAEVHPNFTPILLQSSLKITYESPPGLK 3837
Cdd:COG5245 2906 AVLNSLFSRKEKSWFEVYNISLSFGWFkryveDVVYPIKASRVCGKVKNMWTSMVDADMLPIQLLIAIDSFVSSTYPETG 2985
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3838 KNLMRTYES-WTPEQISKkdnTHRAHALFSLAWFHAACQERRNYIPQGWTKFYEFSLSDLRAGYNIIDRLF--DGAKDVQ 3914
Cdd:COG5245 2986 CGYADLVEIdRYPFDYTL---VIACDDAFYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNILflNHLNARK 3062
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3915 WEFVHGLLENAIYGGRIDNYFDLRVLQSYLKQFF----NSSVID--VFNQRNKKSIFPYSVSlpQSCSILdyraVIEKIP 3988
Cdd:COG5245 3063 WGNNRDLIFTIVYGKKHSLMEDSKVVDKYCRGYGahetSSQILAsvPGGDPELVKFHMEEMC--RSSAFG----VIGQLP 3136
|
2730 2740
....*....|....*....|....*...
gi 311033479 3989 EDDKPSFFGLPANIARSSQRMISSQVIS 4016
Cdd:COG5245 3137 DLALCAWLMGPCDSEYLKAIVYSSRIDM 3164
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1120-1518 |
6.13e-125 |
|
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: 400.87 E-value: 6.13e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1120 ISKDIESCAQIWAFYEEFQQGFQEMANEDWITFrtKTYLFEEFLMNWHDRLRKVE---EHSVMTVKLQSEVDKYKIVIPI 1196
Cdd:pfam08393 4 IKKELEPLKKLWDLVSEWQESLEEWKNGPFSDL--DVEELEEELEEFLKELKKLPkelRDWDVAEELKKKIDDFKKSLPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1197 LKYVRGEHLSPDHWLDLFRLLGLPRGTSLEKLLFGDLLRVadTIVAKAADLKDLNSRAQGEVTIREALRELDLWGVGAVF 1276
Cdd:pfam08393 82 IEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDL--NLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1277 TLIDYEDsqsRTMKLIKDWKDIVNQVGDNRCLLQSLKDSPYYKGFEDKVSIWERKLAELDEYLQNLNHIQRKWVYLEPIF 1356
Cdd:pfam08393 160 ELVPYKD---TGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1357 G----RGALPKEQTRFNRVDEDFRSIMTDIKKDNRVTTLTTHAGIRNSLLTILDQLQRCQKSLNEFLEEKRSAFPRFYFI 1432
Cdd:pfam08393 237 SsediRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1433 GDDDLLEILGQSTNPSVIQSHLKKLFAGINSVCFDEkSKHITAMKSLEGEVVPF-KNKVPLSNNVETWLNDLALEMKKTL 1511
Cdd:pfam08393 317 SNDELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE-NKEITGMISKEGEVVPFsKPPVEAKGNVEEWLNELEEEMRETL 395
|
....*..
gi 311033479 1512 EQLLKEC 1518
Cdd:pfam08393 396 RDLLKEA 402
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3253-3471 |
5.67e-96 |
|
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: 310.14 E-value: 5.67e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3253 WKSEGLPSDDLSIENALVILQSRVCPFLIDPSSQATEWLKTHLKDSRLEVINQQDSNFITALELAVRFGKTLIIQEM-DG 3331
Cdd:pfam12781 3 WNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVgEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3332 VEPVLYPLLRRDLVAQGPRYVVQIGDKIIDYNEEFRLFLSTRNPNPFIPPDAASIVTEVNFTTTRSGLRGQLLALTIQHE 3411
Cdd:pfam12781 83 LDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVKKE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3412 KPDLEEQKTKLLQQEEDKKIQLAKLEESLLETLATSQGNILENKDLIESLNQTKASSALI 3471
Cdd:pfam12781 163 RPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4011-4304 |
1.16e-53 |
|
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: 191.68 E-value: 1.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 4011 SSQVISQLRILGRSITAGSKFDREiwSNElSPVLNLWKKLNQnsnlihqKVPPPND----------RQGSPILSFIILEQ 4080
Cdd:pfam18199 4 TNELLSTLLSLQPRSDSGGGGGGS--SRE-EIVLELAKDILE-------KLPEPFDieeaeekypvGYEDPLNTVLLQEI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 4081 FNAIRLVQSVHQSLAALSKVIRGTTLLSSEVQKLASALLNQKCPLAWQSKWEGPEDPL-QYLRGLVARALAIQNWVDKAE 4159
Cdd:pfam18199 74 ERFNKLLKVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLgSWIRDLLERLKQLQDWLDDEG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 4160 KQAllseTLDLSELFHPDTFLNALRQETARAVGRSVDSLKFVASWKGRLQEAKLQIK------ISGLLLEGCSFDG--NQ 4231
Cdd:pfam18199 154 PPK----VFWLSGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTKKVSPEEVTEPpedgvyVHGLFLEGARWDRknGC 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 311033479 4232 LSEnQLDSPSVSSVLPCFMGWIPQDAcgPYSPDECISLPVYTSAERDR--VVTNIDVPCGGNQDQWIQCGAALFL 4304
Cdd:pfam18199 230 LVE-SEPKELFSPLPVIHLKPVESDK--KKLDENTYECPVYKTSERHStnFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
234-674 |
6.03e-25 |
|
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: 113.06 E-value: 6.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 234 VWRQTEHdhYPES-RMLHLLDIIGGSFGRFVQKKLGTLNLWEDPYYLVKESLKAGISICEQWVIVCNHLTGQVWQRYVPH 312
Cdd:pfam08385 128 IWSISRY--YNTSeRMTVLLEKISNQLIEQCKKYLSPEGIFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRER 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 313 PWK-NEKYFPETLDKLGKRLEEVLAIRTIHEKFLYFLPASEEKIICLTRVFEP--------FTGLNPVQYNP--YTEPLW 381
Cdd:pfam08385 206 PWDfSERYIFGRFDAFLERLEKILELFETIEQFSKLEKIGGTKGPELEGVIEEileefqeaYKVFKSKTYDIldVSNEGF 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 382 KAAVSQYEKIIAPAEQKIAGKLKNYISEIQdSPQQLLQAFLKYKELVKRPTISKELMLERETLLARLVDSIKDFRLDFEN 461
Cdd:pfam08385 286 DDDYEEFKERIKDLERRLQAFIDQAFDDAR-STESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDK 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 462 rcrgipGDASGPLSGKNLSEVVNSIVWVRQLELKVDDTIKIAEALLSDLpgfrcFHQSAKDLLD-------QLKLYEQEQ 534
Cdd:pfam08385 365 ------QKYNPSPIAKNMPPVAGAIIWARQLFRRIQEPMKRFKEELGLL-----KHAEGKKVIKkynelakKLDEYERLI 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 535 FDDWSRDIqsglsDSRSGLCIEASsrIMELD-SNDGLLKVHYSDRLVILLREVRQLSALGFVIPAKIQQVANIAQKFCKQ 613
Cdd:pfam08385 434 YEAWLKEV-----EEASEGNLKRP--LLVRHpETGKLLSVNFDPQLLALLREVKYLQKLGFEIPESALNIALKEERLRPY 506
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 311033479 614 AIILKQVAHFYNSIDQQMIQSQRPMMLQSALAFEQIIKNskagsgGKSQITWDNpKELEGY 674
Cdd:pfam08385 507 AESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEP------GLTTLTWNS-LGIDEY 560
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2886-3238 |
1.32e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2886 KKKELLKRQSHLQAGVSKLNEAKALVDELNRkageqsvlLKTKQDEadaalqmitVSMQDASEQKTELERLKHRIAEEVV 2965
Cdd:PRK03918 346 KLKELEKRLEELEERHELYEEAKAKKEELER--------LKKRLTG---------LTPEKLEKELEELEKAKEEIEEEIS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2966 KIEERKNKIDDELKEVQPLVNEAKLAVG---------------NIKPESLSEIRSLRMPPDVIRDILEGVLRLMgifdts 3030
Cdd:PRK03918 409 KITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKEL------ 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3031 wVSMKSFLAKRgvREDIATfdaRNISKEIRESVEELlfknkGSFDPKNAKrastaaaplaawvKANIQYSHVLERIHPLE 3110
Cdd:PRK03918 483 -RELEKVLKKE--SELIKL---KELAEQLKELEEKL-----KKYNLEELE-------------KKAEEYEKLKEKLIKLK 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3111 TEQAGLESNLKKTEDRKRKLEELLNsvgqKVSELKEkfqsrtsEAAKLEAEVSK-AQETIKAAEVLINQLDREHKRWN-- 3187
Cdd:PRK03918 539 GEIKSLKKELEKLEELKKKLAELEK----KLDELEE-------ELAELLKELEElGFESVEELEERLKELEPFYNEYLel 607
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 311033479 3188 ----AQVVEITEELATLPKRAQLAAAFITYLSAAPESLRKTcLEEWTKSAGLEKF 3238
Cdd:PRK03918 608 kdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE-LEELEKKYSEEEY 661
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2885-3202 |
2.67e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2885 SKKKELLKRQshLQAGVSKLNEAKALVDELNRKAGEQSVLLKTKQDEADAALQmitvsmqDASEQKTELERLKHRIAEEV 2964
Cdd:TIGR02169 680 RERLEGLKRE--LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ-------EEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2965 VKIEERKNKIDDELKEVQPL---VNEAKLAVGNIKPE-SLSEIRSLRmppDVIRDILEGVLRLMGIFDtswvSMKSFLAK 3040
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELeedLHKLEEALNDLEARlSHSRIPEIQ---AELSKLEEEVSRIEARLR----EIEQKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3041 RGVREDIAtfdarniSKEIRESVEELLfknkgsfdpknakrastaaaplaawvKANIQYSHVLERIHPLETEQAGLESNL 3120
Cdd:TIGR02169 824 LTLEKEYL-------EKEIQELQEQRI--------------------------DLKEQIKSIEKEIENLNGKKEELEEEL 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3121 KKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIK----AAEVLINQLDrEHKRWNAQVVEITEE 3196
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSelkaKLEALEEELS-EIEDPKGEDEEIPEE 949
|
....*.
gi 311033479 3197 LATLPK 3202
Cdd:TIGR02169 950 ELSLED 955
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1928-1999 |
1.03e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 46.88 E-value: 1.03e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 311033479 1928 GIELKEVEydelsaalKQVFEEANYEIIPNQIkkalelyeqlcqrmgVVIVGPSGAGKSTLWRMLRAALCKT 1999
Cdd:COG2401 35 GVELRVVE--------RYVLRDLNLEIEPGEI---------------VLIVGASGSGKSTLLRLLAGALKGT 83
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
1688-1728 |
3.02e-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: 41.50 E-value: 3.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 311033479 1688 YGPAGTGKTESVKALGGLLGRQVLVFNCDEGIDV------KSMGRIF 1728
Cdd:cd19481 32 YGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKyvgeseKNLRKIF 78
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1975-1991 |
4.84e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 42.52 E-value: 4.84e-03
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1651-1986 |
8.35e-174 |
|
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: 537.84 E-value: 8.35e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1651 YTYEYQGNASKLVYTPLTDKCYLTLTQAMKMGLGGNPYGPAGTGKTESVKALGGLLGRQVLVFNCDEGIDVKSMGRIFVG 1730
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1731 LVKCGAWGCFDEFNRLEESVLSAVSMQIQTIQDALKNHRTVCELLGKEVEVNSNSGIFITMNPagkGYGGRQKLPDNLKQ 1810
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNP---GYAGRTELPDNLKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1811 LFRPVAMSHPDNELIAEVILYSEGFKDAKVLSRKLVAIFNLSRELLTPQQHYDWGLRALKTVLRGSGNLLRQlnksgtTQ 1890
Cdd:pfam12774 158 LFRPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRS------NP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1891 NANESHIVVQALRLNTMSKFTFTDCTRFDALIKDVFPGIELKEVEYDELSAALKQVFEEANYEIIPNQIKKALELYEQLC 1970
Cdd:pfam12774 232 NLNEDVLLLRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETML 311
|
330
....*....|....*.
gi 311033479 1971 QRMGVVIVGPSGAGKS 1986
Cdd:pfam12774 312 VRHGVMLVGPTGSGKT 327
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1361-4016 |
1.38e-159 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 559.61 E-value: 1.38e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1361 LPKEQTRFNRVDEDFRSIMTDIKKDNRvTTLTTHAGIRNSLLTILDQLQRCQKSLNEFLEEKRSAFPRFyfIGDDDLLEI 1440
Cdd:COG5245 644 IPHAVHRKMSLVSGVRGIYKRVVSGCE-AINTILEDVGDDLDLFYKEMDQVFMSIEKVLGLRWREVERA--SEVEELMDR 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1441 LGQSTNPSVIQSHLKKLFAGINSVCFdeKSKHITAMKSLEGEVVPFKNKVPL--SNNVETWLNDlalEMKKTLEQLLkEC 1518
Cdd:COG5245 721 VRELENRVYSYRFFVKKIAKEEMKTV--FSSRIQKKEPFSLDSEAYVGFFRLyeKSIVIRGINR---SMGRVLSQYL-ES 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1519 VttGRSSQGAvDPSLFPSQILC---LAEQIKFTEDVENAIkdhslhqiETQLVnklEQYTNIDTSSEDPGNTESGILELK 1595
Cdd:COG5245 795 V--QEALEIE-DGSFFVSRHRVrdgGLEKGRGCDAWENCF--------DPPLS---EYFRILEKIFPSEEGYFFDEVLKR 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1596 LKALILDIIHNIDVVKQLNQIQVHTTEDWAWKKQLRFYMKSDHTCCVQMVDSEFQYTYEYQGNASKLVYTPLTDKCYLTL 1675
Cdd:COG5245 861 LDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMDTSQHQKL 940
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1676 TQAMKMGLGGNpygpAGTGKTESVKALGGLLGRQVlvfncdEGIDVKSmgRIFVGLVKCGAWGcFDEFNRLEESVLsAVS 1755
Cdd:COG5245 941 FEAVCDEVCRF----VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISR-TIL 1006
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1756 MQIQTIQDALKNHRTVCELLGKEVEVNSNSGIFITMNPagkgyggRQKLPDNLKQLFRPVAMSHPDNElIAEVilysegf 1835
Cdd:COG5245 1007 VDEYLNSDEFRMLEELNSAVVEHGLKSPSTPVEMIINE-------RNIVLEIGRRALDMFLSNIPFGA-IKSR------- 1071
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1836 kdAKVLSRKLVAIFNLSRELLTPQQHYDWglRALKTVLRGSGNLLRQLNKSGTTqnaneshiVVQALRLNTMSkftftdc 1915
Cdd:COG5245 1072 --RESLDREIGAFNNEVDGIAREEDELMF--YPMFKSLKAKHRMLEEKTEYLNK--------ILSITGLPLIS------- 1132
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1916 trfDALIKDvfpgIELKEVEYDEL-SAALKQVFEEANyEIIPNQIKKALELYEQLCQRMGVVIVGPSGAGKSTLWRmlrA 1994
Cdd:COG5245 1133 ---DTLRER----IDTLDAEWDSFcRISESLKKYESQ-QVSGLDVAQFVSFLRSVDTGAFHAEYFRVFLCKIKHYT---D 1201
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1995 ALCKTGKVVKQYTMNPKAMPRYQLLGHIDMDTREWSDGVLTNSARQVVREpqdvsswiicdgdidpEWIESLNSVLDDNR 2074
Cdd:COG5245 1202 ACDYLWHVKSPYVKKKYFDADMELRQFFLMFNREDMEARLADSKMEYEVE----------------RYVEKTKAEVSSLK 1265
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2075 LLTMPSGERiqfgpnvNFVFETHDlscASPATISRMGMIFLSDEETDLNSLIkSWLRNQPAEYRNN-------------- 2140
Cdd:COG5245 1266 LELSSVGEG-------QVVVSNLG---SIGDKVGRCLVEYDSISRLSTKGVF-LDELGDTKRYLDEcldffscfeevqke 1334
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2141 ----LENWIGD--YFEKALQWVLKQNDY-VVETSLVGTVMNG--LSHLHGCRDHDEFIINLIRGLGGNLNMKSRLEFTke 2211
Cdd:COG5245 1335 idelSMVFCADalRFSADLYHIVKERRFsGVLAGSDASESLGgkSIELAAILEHKDLIVEMKRGINDVLKLRIFGDKC-- 1412
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2212 vfhwaRESPPDFHKPMDTYYDSTRGRLATY--VLKKPEDLTADDFSNG-----------LTLP---VIQTPDMQRGLDYF 2275
Cdd:COG5245 1413 -----RESTPRFYLISDGDLIKDLNERSDYeeMLIMMFNISAVITNNGsiagfelrgerVMLRkevVIPTSDTGFVDSFS 1487
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2276 KPWLSsdTKQPFILVGPEGCGKGMLLRYAFSQLRSTQIATVHCSAQTTSRHLLQKLSQTcMVISTNTG--RVYRPKDCER 2353
Cdd:COG5245 1488 NEALN--TLRSYIYCGPPGSGKEMLMCPSLRSELITEVKYFNFSTCTMTPSKLSVLERE-TEYYPNTGvvRLYPKPVVKD 1564
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2354 LVLYLKDINLPKLDKWGTSTLVAFLQQVLTYQGFYDE-NLEWVGLENIQIVASMSAGGRLGRHKLTTRFTSIVRLCSIDY 2432
Cdd:COG5245 1565 LVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSSiAVSWVTICGIILYGACNPGTDEGRVKYYERFIRKPVFVFCCY 1644
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2433 PEREQLQTIYGAYLEPVLHKNLKNHSIwgssskIYLLAGSMVQVYEQVRAKFTVDDYSHYFFTPCILTQWVLGLFRYDLE 2512
Cdd:COG5245 1645 PELASLRNIYEAVLMGSYLCFDEFNRL------SEETMSASVELYLSSKDKTKFFLQMNYGYKPRELTRSLRAIFGYAET 1718
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2513 GgsSNHPLDYVLEIVAYEARRLFRDKIVGAKELHLFDIILTSVFQGDWGSDILDNMSDSFYVTWGARHNSgaraapgqpl 2592
Cdd:COG5245 1719 R--IDTPDVSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREMIAGHIGEAEITFSMILFFG---------- 1786
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2593 pphgkpLGKLNSTDLKDVIKKGLIHYGRDNQNLDILLFHEVLEYMSRIDRVLSFPGGSLLLAGRSGVGRRTITSLVSHMH 2672
Cdd:COG5245 1787 ------MACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLN 1860
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2673 GAVLFSPKISRGYELKQFKNDLKHVLQLAGIEAQQVVLLLEDYQFVHPTFLEMINSLLSSGEVPGLYTLEELEPLLLPLK 2752
Cdd:COG5245 1861 PRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLR 1940
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2753 DQASQDGFF----GPVFNYFTYRIQQNLHIVL-IMDSANSNFMINCESnPALHKKCQVLWMEGWSNSSMKKIP-EMLFSE 2826
Cdd:COG5245 1941 FVFESTSLEkdteATLTRVFLVYMEENLPVVFsACCSQDTSVLAGIRS-PALKNRCFIDFKKLWDTEEMSQYAnSVETLS 2019
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2827 TGGGEKYNDKKRKEEKKKNSVDPDFLKSFLLIHES-------CKAYGATPSRYMTFLHVYSAISSSKKKELLKRQSHLQA 2899
Cdd:COG5245 2020 RDGGRVFFINGELGVGKGALISEVFGDDAVVIEGRgfeismiEGSLGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVE 2099
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2900 GVSKLNEAKALVDELNRKAGEQSVLLKTKQDEADAALQMITVSMQDASEQKTELERLKHRIAEEVVKIEERKNKIDDELK 2979
Cdd:COG5245 2100 GVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKS 2179
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2980 EVQPLVNEAKLAVGNIKPESLSEIRSLRMPPDVIRDILEGVLRLMGIFDTSWVSMKSFLAKRGVREDIATFD-ARNISKE 3058
Cdd:COG5245 2180 SKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLLGFEAKIWFGEQQSLRRDDFIRIIGKYPdEIEFDLE 2259
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3059 IRESVEELLFKNKgSFDPKNAKRASTAAAPLAAWVKANIQYSHVLERIHPLETEQAGLESNLKKTEDRKRKLEELLNSVG 3138
Cdd:COG5245 2260 ARRFREARECSDP-SFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLM 2338
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3139 QKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHKRWNAQVVEITEELATLPKRAQLAAAFITYLSAAP 3218
Cdd:COG5245 2339 TFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLG 2418
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3219 ESLRKTCLEEWTKSAGLE---KFDLRRFLCTESEQLIWKSEGLP-SDDLSIENALVILQSR-VCPFLIDPSSQATEWLKT 3293
Cdd:COG5245 2419 FLCRAIEFGMSFIRISKEfrdKEIRRRQFITEGVQKIEDFKEEAcSTDYGLENSRIRKDLQdLTAVLNDPSSKIVTSQRQ 2498
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3294 HLKDSRLEVINQQDSNFITALELAVRFGKTLIIQEMDGVEPVLYPLLRRDLVAQGPRYVVQIGDKIIDYNEEFRLFLSTR 3373
Cdd:COG5245 2499 MYDEKKAILGSFREMEFAFGLSQARREGSDKIIGDAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSE 2578
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3374 NPNPFIPPDAASIVTEVNFTTTRSGLRGQLLALTIQHEKPDLEEQKTKLLQQEEDKKIQLAKLEESLLETLATSQGNILE 3453
Cdd:COG5245 2579 GRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQ 2658
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3454 NKDLIESLNQTKASSALIQESLKESYKLQISLDQERDAYLPLAESASKMYFIISDLSKINNMYRFSLAAFLRLFQRALQN 3533
Cdd:COG5245 2659 TDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFEKWRRM 2738
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3534 KqdSENTEQRIQSLISSLQHMVYEYICRCLFKAD--------QLMFALHFVRGMHPELfqENEWDTFTGVVVgdmlrkaD 3605
Cdd:COG5245 2739 K--SKYLCAIRYMLMSSEWILDHEDRSGFIHRLDvsfllrtkRFVSTLLEDKNYRQVL--SSCSLYGNDVIS-------H 2807
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3606 SQQKI-RDQLPSWIDQERSWAVATLKialpsLYQTLCFEDAAlwRTYYN--NSMCEQEFPSILAKkvslfqqilvvqalr 3682
Cdd:COG5245 2808 SCDRFdRDVYRALKHQMDNRTHSTIL-----TSNSKTNPYKE--YTYNDswAEAFEVEDSGDLYK--------------- 2865
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3683 pdrlqsamalfacKTLGLKEVSPLPLNLKRLYKETLEIEPIliiispgadpsqeLQELANAERSgecyhqvamgqgqaDL 3762
Cdd:COG5245 2866 -------------FEEGLLELIVGHAPLIYAHKKSLENERN-------------VDRLGSKENE--------------VY 2905
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3763 AIQMLKECARNGDWLCLKNLHLVVSWL-----PVLEKELNTLQPKDTFRLWLTAEVHPNFTPILLQSSLKITYESPPGLK 3837
Cdd:COG5245 2906 AVLNSLFSRKEKSWFEVYNISLSFGWFkryveDVVYPIKASRVCGKVKNMWTSMVDADMLPIQLLIAIDSFVSSTYPETG 2985
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3838 KNLMRTYES-WTPEQISKkdnTHRAHALFSLAWFHAACQERRNYIPQGWTKFYEFSLSDLRAGYNIIDRLF--DGAKDVQ 3914
Cdd:COG5245 2986 CGYADLVEIdRYPFDYTL---VIACDDAFYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNILflNHLNARK 3062
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3915 WEFVHGLLENAIYGGRIDNYFDLRVLQSYLKQFF----NSSVID--VFNQRNKKSIFPYSVSlpQSCSILdyraVIEKIP 3988
Cdd:COG5245 3063 WGNNRDLIFTIVYGKKHSLMEDSKVVDKYCRGYGahetSSQILAsvPGGDPELVKFHMEEMC--RSSAFG----VIGQLP 3136
|
2730 2740
....*....|....*....|....*...
gi 311033479 3989 EDDKPSFFGLPANIARSSQRMISSQVIS 4016
Cdd:COG5245 3137 DLALCAWLMGPCDSEYLKAIVYSSRIDM 3164
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1120-1518 |
6.13e-125 |
|
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: 400.87 E-value: 6.13e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1120 ISKDIESCAQIWAFYEEFQQGFQEMANEDWITFrtKTYLFEEFLMNWHDRLRKVE---EHSVMTVKLQSEVDKYKIVIPI 1196
Cdd:pfam08393 4 IKKELEPLKKLWDLVSEWQESLEEWKNGPFSDL--DVEELEEELEEFLKELKKLPkelRDWDVAEELKKKIDDFKKSLPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1197 LKYVRGEHLSPDHWLDLFRLLGLPRGTSLEKLLFGDLLRVadTIVAKAADLKDLNSRAQGEVTIREALRELDLWGVGAVF 1276
Cdd:pfam08393 82 IEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDL--NLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1277 TLIDYEDsqsRTMKLIKDWKDIVNQVGDNRCLLQSLKDSPYYKGFEDKVSIWERKLAELDEYLQNLNHIQRKWVYLEPIF 1356
Cdd:pfam08393 160 ELVPYKD---TGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1357 G----RGALPKEQTRFNRVDEDFRSIMTDIKKDNRVTTLTTHAGIRNSLLTILDQLQRCQKSLNEFLEEKRSAFPRFYFI 1432
Cdd:pfam08393 237 SsediRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1433 GDDDLLEILGQSTNPSVIQSHLKKLFAGINSVCFDEkSKHITAMKSLEGEVVPF-KNKVPLSNNVETWLNDLALEMKKTL 1511
Cdd:pfam08393 317 SNDELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE-NKEITGMISKEGEVVPFsKPPVEAKGNVEEWLNELEEEMRETL 395
|
....*..
gi 311033479 1512 EQLLKEC 1518
Cdd:pfam08393 396 RDLLKEA 402
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3253-3471 |
5.67e-96 |
|
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: 310.14 E-value: 5.67e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3253 WKSEGLPSDDLSIENALVILQSRVCPFLIDPSSQATEWLKTHLKDSRLEVINQQDSNFITALELAVRFGKTLIIQEM-DG 3331
Cdd:pfam12781 3 WNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVgEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3332 VEPVLYPLLRRDLVAQGPRYVVQIGDKIIDYNEEFRLFLSTRNPNPFIPPDAASIVTEVNFTTTRSGLRGQLLALTIQHE 3411
Cdd:pfam12781 83 LDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVKKE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3412 KPDLEEQKTKLLQQEEDKKIQLAKLEESLLETLATSQGNILENKDLIESLNQTKASSALI 3471
Cdd:pfam12781 163 RPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4011-4304 |
1.16e-53 |
|
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: 191.68 E-value: 1.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 4011 SSQVISQLRILGRSITAGSKFDREiwSNElSPVLNLWKKLNQnsnlihqKVPPPND----------RQGSPILSFIILEQ 4080
Cdd:pfam18199 4 TNELLSTLLSLQPRSDSGGGGGGS--SRE-EIVLELAKDILE-------KLPEPFDieeaeekypvGYEDPLNTVLLQEI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 4081 FNAIRLVQSVHQSLAALSKVIRGTTLLSSEVQKLASALLNQKCPLAWQSKWEGPEDPL-QYLRGLVARALAIQNWVDKAE 4159
Cdd:pfam18199 74 ERFNKLLKVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLgSWIRDLLERLKQLQDWLDDEG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 4160 KQAllseTLDLSELFHPDTFLNALRQETARAVGRSVDSLKFVASWKGRLQEAKLQIK------ISGLLLEGCSFDG--NQ 4231
Cdd:pfam18199 154 PPK----VFWLSGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTKKVSPEEVTEPpedgvyVHGLFLEGARWDRknGC 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 311033479 4232 LSEnQLDSPSVSSVLPCFMGWIPQDAcgPYSPDECISLPVYTSAERDR--VVTNIDVPCGGNQDQWIQCGAALFL 4304
Cdd:pfam18199 230 LVE-SEPKELFSPLPVIHLKPVESDK--KKLDENTYECPVYKTSERHStnFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| AAA_lid_11 |
pfam18198 |
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the ... |
3864-4002 |
3.62e-49 |
|
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: 172.64 E-value: 3.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3864 LFSLAWFHAACQERRNYIPQGWTKFYEFSLSDLRAGYNIIDRLFDGAKD-VQWEFVHGLLENAIYGGRIDNYFDLRVLQS 3942
Cdd:pfam18198 5 LFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLDEYDEkIPWDALRYLIGEINYGGRVTDDWDRRLLNT 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3943 YLKQFFNSSVIDvfnqrNKKSIFPYSVSLPQSCSILDYRAVIEKIPEDDKPSFFGLPANI 4002
Cdd:pfam18198 85 YLEEFFNPEVLE-----EDFKFSPSLYYIPPDGDLEDYLEYIESLPLVDSPEVFGLHPNA 139
|
|
| AAA_8 |
pfam12780 |
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
2625-2811 |
1.30e-44 |
|
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: 163.93 E-value: 1.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2625 LDILLFHEVLEYMSRIDRVLSFPGGSLLLAGRSGVGRRTITSLVSHMHGAVLFSPKISRGYELKQFKNDLKHVLQLAGIE 2704
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2705 AQQVVLLLEDYQFVHPTFLEMINSLLSSGEVPGLYTLEELEPLLLPLKDQASQDGFFGP---VFNYFTYRIQQNLHIVLI 2781
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSreaVYNYFVKRCRNNLHIVLC 160
|
170 180 190
....*....|....*....|....*....|
gi 311033479 2782 MDSANSNFMINCESNPALHKKCQVLWMEGW 2811
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEW 190
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
3730-3829 |
2.13e-39 |
|
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: 143.74 E-value: 2.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3730 GADPSQELQELANAERSGECYHQVAMGQGQADLAIQMLKECARNGDWLCLKNLHLVVSWLPVLEKELNTLQPK---DTFR 3806
Cdd:pfam03028 13 GSDPTADLEKLAKKLGFGGKLHSISLGQGQGPIAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKILEELPEEtlhPDFR 92
|
90 100
....*....|....*....|...
gi 311033479 3807 LWLTAEVHPNFTPILLQSSLKIT 3829
Cdd:pfam03028 93 LWLTSEPSPKFPISILQNSIKIT 115
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1974-2110 |
1.00e-29 |
|
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: 116.62 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1974 GVVIVGPSGAGKSTLWRMLRAALCKTgkvVKQYTMNPKAMPRYQLLGHIDMDTR--EWSDGVLTNSARqvvrepqdvSSW 2051
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNR---PVFYVQLTRDTTEEDLFGRRNIDPGgaSWVDGPLVRAAR---------EGE 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 311033479 2052 IICDGDID---PEWIESLNSVLDDNRLLTMPSGERIQFGP-NVNFVFETHDL----SCASPATISRM 2110
Cdd:pfam07728 69 IAVLDEINranPDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIATMNPLdrglNELSPALRSRF 135
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
2897-3229 |
2.04e-26 |
|
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: 114.02 E-value: 2.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2897 LQAGVSKLNEAKALVDELNRKAGEQSVLLKTKQDEADAALQMITVSMQDASEQKTELERLKHRIAEEVVKIEERKNKIDD 2976
Cdd:pfam12777 3 LENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKACEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2977 ELKEVQPLVNEAKLAVGNIKPESLSEIRSLRMPPDVIRDILEGVLRLMGIF-----DTSWVSMKSFLAK-RGVREDIATF 3050
Cdd:pfam12777 83 DLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMAPGgkipkDKSWKAAKIMMAKvDGFLDSLIKF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3051 DARNISKEIRESVEEllFKNKGSFDPKNAKRASTAAAPLAAWVKANIQYSHVLERIHP----LETEQAGLESNLKKTEDR 3126
Cdd:pfam12777 163 DKEHIHEACLKAFKP--YLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPkrqaLEEANADLAAAQEKLAAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3127 KRKLEELlnsvGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHKRWNAQVVEITEELATLPKRAQL 3206
Cdd:pfam12777 241 KAKIAEL----NANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDILL 316
|
330 340
....*....|....*....|....
gi 311033479 3207 AAAFITYLSAAPESLRKTCLEE-W 3229
Cdd:pfam12777 317 ISAFISYLGFFTKKYRNELLDKfW 340
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
234-674 |
6.03e-25 |
|
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: 113.06 E-value: 6.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 234 VWRQTEHdhYPES-RMLHLLDIIGGSFGRFVQKKLGTLNLWEDPYYLVKESLKAGISICEQWVIVCNHLTGQVWQRYVPH 312
Cdd:pfam08385 128 IWSISRY--YNTSeRMTVLLEKISNQLIEQCKKYLSPEGIFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRER 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 313 PWK-NEKYFPETLDKLGKRLEEVLAIRTIHEKFLYFLPASEEKIICLTRVFEP--------FTGLNPVQYNP--YTEPLW 381
Cdd:pfam08385 206 PWDfSERYIFGRFDAFLERLEKILELFETIEQFSKLEKIGGTKGPELEGVIEEileefqeaYKVFKSKTYDIldVSNEGF 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 382 KAAVSQYEKIIAPAEQKIAGKLKNYISEIQdSPQQLLQAFLKYKELVKRPTISKELMLERETLLARLVDSIKDFRLDFEN 461
Cdd:pfam08385 286 DDDYEEFKERIKDLERRLQAFIDQAFDDAR-STESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDK 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 462 rcrgipGDASGPLSGKNLSEVVNSIVWVRQLELKVDDTIKIAEALLSDLpgfrcFHQSAKDLLD-------QLKLYEQEQ 534
Cdd:pfam08385 365 ------QKYNPSPIAKNMPPVAGAIIWARQLFRRIQEPMKRFKEELGLL-----KHAEGKKVIKkynelakKLDEYERLI 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 535 FDDWSRDIqsglsDSRSGLCIEASsrIMELD-SNDGLLKVHYSDRLVILLREVRQLSALGFVIPAKIQQVANIAQKFCKQ 613
Cdd:pfam08385 434 YEAWLKEV-----EEASEGNLKRP--LLVRHpETGKLLSVNFDPQLLALLREVKYLQKLGFEIPESALNIALKEERLRPY 506
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 311033479 614 AIILKQVAHFYNSIDQQMIQSQRPMMLQSALAFEQIIKNskagsgGKSQITWDNpKELEGY 674
Cdd:pfam08385 507 AESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEP------GLTTLTWNS-LGIDEY 560
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2284-2423 |
2.00e-20 |
|
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: 91.68 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2284 KQPFILVGPEGCGKGMLLRYAFSQL--RSTQIATVHCSAQTTSrhllqklSQTCMVISTN----TGRVYRPKDCERLVLY 2357
Cdd:pfam12775 31 GKPVLLVGPTGTGKTVIIQNLLRKLdkEKYLPLFINFSAQTTS-------NQTQDIIESKlekrRKGVYGPPGGKKLVVF 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311033479 2358 LKDINLPKLDKWGTSTLVAFLQQVLTYQGFYD-ENLEWVGLENIQIVASMS-AGGrlGRHKLTTRFTS 2423
Cdd:pfam12775 104 IDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDrKKLTFKEIVDVQFVAAMGpPGG--GRNDITPRLLR 169
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2886-3238 |
1.32e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2886 KKKELLKRQSHLQAGVSKLNEAKALVDELNRkageqsvlLKTKQDEadaalqmitVSMQDASEQKTELERLKHRIAEEVV 2965
Cdd:PRK03918 346 KLKELEKRLEELEERHELYEEAKAKKEELER--------LKKRLTG---------LTPEKLEKELEELEKAKEEIEEEIS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2966 KIEERKNKIDDELKEVQPLVNEAKLAVG---------------NIKPESLSEIRSLRMPPDVIRDILEGVLRLMgifdts 3030
Cdd:PRK03918 409 KITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKEL------ 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3031 wVSMKSFLAKRgvREDIATfdaRNISKEIRESVEELlfknkGSFDPKNAKrastaaaplaawvKANIQYSHVLERIHPLE 3110
Cdd:PRK03918 483 -RELEKVLKKE--SELIKL---KELAEQLKELEEKL-----KKYNLEELE-------------KKAEEYEKLKEKLIKLK 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3111 TEQAGLESNLKKTEDRKRKLEELLNsvgqKVSELKEkfqsrtsEAAKLEAEVSK-AQETIKAAEVLINQLDREHKRWN-- 3187
Cdd:PRK03918 539 GEIKSLKKELEKLEELKKKLAELEK----KLDELEE-------ELAELLKELEElGFESVEELEERLKELEPFYNEYLel 607
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 311033479 3188 ----AQVVEITEELATLPKRAQLAAAFITYLSAAPESLRKTcLEEWTKSAGLEKF 3238
Cdd:PRK03918 608 kdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE-LEELEKKYSEEEY 661
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2885-3202 |
2.67e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2885 SKKKELLKRQshLQAGVSKLNEAKALVDELNRKAGEQSVLLKTKQDEADAALQmitvsmqDASEQKTELERLKHRIAEEV 2964
Cdd:TIGR02169 680 RERLEGLKRE--LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ-------EEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2965 VKIEERKNKIDDELKEVQPL---VNEAKLAVGNIKPE-SLSEIRSLRmppDVIRDILEGVLRLMGIFDtswvSMKSFLAK 3040
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELeedLHKLEEALNDLEARlSHSRIPEIQ---AELSKLEEEVSRIEARLR----EIEQKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3041 RGVREDIAtfdarniSKEIRESVEELLfknkgsfdpknakrastaaaplaawvKANIQYSHVLERIHPLETEQAGLESNL 3120
Cdd:TIGR02169 824 LTLEKEYL-------EKEIQELQEQRI--------------------------DLKEQIKSIEKEIENLNGKKEELEEEL 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3121 KKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIK----AAEVLINQLDrEHKRWNAQVVEITEE 3196
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSelkaKLEALEEELS-EIEDPKGEDEEIPEE 949
|
....*.
gi 311033479 3197 LATLPK 3202
Cdd:TIGR02169 950 ELSLED 955
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3092-3209 |
3.08e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3092 WVKANIQYSHVLERIHPLETEQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKA 3171
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110
....*....|....*....|....*....|....*...
gi 311033479 3172 AEVLINQLDREHKRWNAQVVEITEELATLpkRAQLAAA 3209
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEEL--EEELEEA 349
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2886-3207 |
4.08e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2886 KKKELLKRQSHLQagvSKLNEAKALVDELNRKAGEqsvllKTKQDEADAALQMitvsmQDASEQKTELERLKhriAEEVV 2965
Cdd:PTZ00121 1477 KKAEEAKKADEAK---KKAEEAKKKADEAKKAAEA-----KKKADEAKKAEEA-----KKADEAKKAEEAKK---ADEAK 1540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2966 KIEERKNKidDELKEVQPLVN-EAKLAVGNIKPESLSEIRSLRMPpDVIRDILEGVLRLMGIFDTSWVSMKSFLAKRGVR 3044
Cdd:PTZ00121 1541 KAEEKKKA--DELKKAEELKKaEEKKKAEEAKKAEEDKNMALRKA-EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3045 EDIATFDARNiSKEIRESVEELlfKNKGSFDPKNA----KRASTAAAPLAAWVKANIQYSHVLERIHPLETEQAGLESNL 3120
Cdd:PTZ00121 1618 AKIKAEELKK-AEEEKKKVEQL--KKKEAEEKKKAeelkKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3121 KKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLinQLDREHKRWNAQVVEITEELATL 3200
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA--KKDEEEKKKIAHLKKEEEKKAEE 1772
|
....*..
gi 311033479 3201 PKRAQLA 3207
Cdd:PTZ00121 1773 IRKEKEA 1779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2890-3200 |
2.06e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2890 LLKRQSHLQAGVSKLNEAKALVD----ELNRKAGEQSVLLKTKQDEADAALQMITVSMQDASEQKTELERLKHRIAEEVV 2965
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEerleEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2966 KIEERKNKIDDELKEVQPLVNEAKLAVGNIkpESLS-EIRSLRMPPDVIRDILEGVLRLMGifdtswvSMKSFLAKRGVR 3044
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDI--ESLAaEIEELEELIEELESELEALLNERA-------SLEEALALLRSE 895
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3045 EDIATFDARNISKEIRESVEELlfknkgsfDPKNAKRASTAAAplaaWVKANIQYSHVLERI--------HPLETEQAGL 3116
Cdd:TIGR02168 896 LEELSEELRELESKRSELRREL--------EELREKLAQLELR----LEGLEVRIDNLQERLseeysltlEEAEALENKI 963
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3117 ESNLKKTEDRKRKLEELLNSVG-------QKVSELKEKFQSRTSEAAKLEAEVSKAQETikaaevlINQLDRE-HKRWNA 3188
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKELGpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLEEA-------IEEIDREaRERFKD 1036
|
330
....*....|..
gi 311033479 3189 QVVEITEELATL 3200
Cdd:TIGR02168 1037 TFDQVNENFQRV 1048
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2884-3196 |
2.45e-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: 50.84 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2884 SSKKKELLKRQSHLQAGVSKLNEAKALVDELNRK----AGEQSVLLKTKQDEADAALQMItVSMQDASEQktELERLkhr 2959
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKikdlGEEEQLRVKEKIGELEAEIASL-ERSIAEKER--ELEDA--- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2960 iAEEVVKIEERKNKIDDELKEVqplvnEAKLAVGNIKPESLSEIrslrmppdvirdilegvlrlmgifdtswvsmksFLA 3039
Cdd:TIGR02169 321 -EERLAKLEAEIDKLLAEIEEL-----EREIEEERKRRDKLTEE---------------------------------YAE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3040 KRGVREDIATfDARNISKEIRESVEELlfknkgsfdpKNAKRASTAAAPLAAWVKANIqySHVLERIHPLETEQAGLESN 3119
Cdd:TIGR02169 362 LKEELEDLRA-ELEEVDKEFAETRDEL----------KDYREKLEKLKREINELKREL--DRLQEELQRLSEELADLNAA 428
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 311033479 3120 LKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHKRWNAQVVEITEE 3196
Cdd:TIGR02169 429 IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
3109-3196 |
3.16e-05 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 46.24 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3109 LETEQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSR---TSEAAKLEAEVSKAQETIKAAE-------VLINQ 3178
Cdd:pfam04871 6 LESEASSLKNENTELKAELQELSKQYNSLEQKESQAKELEAEVkklEEALKKLKAELSEEKQKEKEKQselddllLLLGD 85
|
90
....*....|....*...
gi 311033479 3179 LDREHKRWNAQVVEITEE 3196
Cdd:pfam04871 86 LEEKVEKYKARLKELGEE 103
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2880-3223 |
5.79e-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: 49.68 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2880 SAISSSKKKELLKRQSHLQAGVSKLNEAKALVDELnRKAgEQSVLLKTKQDeADAALQMITVSMQDASEQKTELERLKHR 2959
Cdd:TIGR02169 186 IERLDLIIDEKRQQLERLRREREKAERYQALLKEK-REY-EGYELLKEKEA-LERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2960 IAEEVVKIEerknkidDELKE----VQPLVNEAKLAVGNIKPESLSEIRSLRmppDVIRDILEGVLRLMGIFDTSWVSMK 3035
Cdd:TIGR02169 263 LEKRLEEIE-------QLLEElnkkIKDLGEEEQLRVKEKIGELEAEIASLE---RSIAEKERELEDAEERLAKLEAEID 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3036 SFLAK-RGVREDIATFDAR--NISKEI--RESVEELLFKNKGSFDPKNAkrastaaaplaAWVKANIQYSHVLE----RI 3106
Cdd:TIGR02169 333 KLLAEiEELEREIEEERKRrdKLTEEYaeLKEELEDLRAELEEVDKEFA-----------ETRDELKDYREKLEklkrEI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3107 HPLETEQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHKRW 3186
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
330 340 350
....*....|....*....|....*....|....*..
gi 311033479 3187 NAQVVEITEELATLPKRAQLAAAFITYLSAAPESLRK 3223
Cdd:TIGR02169 482 EKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3109-3328 |
8.65e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 8.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3109 LETEQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHKRWNA 3188
Cdd:COG4372 78 LEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3189 QVVEITEELATLPK------RAQLAAAFITYLSAAPESLRKTCLEEWTKSAGLEKFDLRRF-----LCTESEQLIWKSEG 3257
Cdd:COG4372 158 QLESLQEELAALEQelqalsEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEelleaKDSLEAKLGLALSA 237
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 311033479 3258 LpSDDLSIENALVILQSRVCPFLIDPSSQATEWLKTHLKDSRLEVINQQDSNFITALELAVRFGKTLIIQE 3328
Cdd:COG4372 238 L-LDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAAL 307
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1928-1999 |
1.03e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 46.88 E-value: 1.03e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 311033479 1928 GIELKEVEydelsaalKQVFEEANYEIIPNQIkkalelyeqlcqrmgVVIVGPSGAGKSTLWRMLRAALCKT 1999
Cdd:COG2401 35 GVELRVVE--------RYVLRDLNLEIEPGEI---------------VLIVGASGSGKSTLLRLLAGALKGT 83
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2885-3256 |
1.28e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2885 SKKKELLKRQSHLQAGVSKLNEAKA-LVDELNRKAGEQSVLLKtKQDEADAALQMITVSMQDASEQKTELERLKHRIAEE 2963
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDdLLAEAGLDDADAEAVEA-RREELEDRDEELRDRLEECRVAAQAHNEEAESLRED 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2964 VVKIEERKNKIDDELKEVQPLVNEAKLAVGNIKpESLSEIRslrmppDVIRDILEGVlrlmGIFDTSWVSMKSFLA---- 3039
Cdd:PRK02224 351 ADDLEERAEELREEAAELESELEEAREAVEDRR-EEIEELE------EEIEELRERF----GDAPVDLGNAEDFLEelre 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3040 -KRGVREDIATFDA--RNISKEIRESvEELLFKNK---------GS-----FDPKNAKRASTAAAPLaawvKANIQYSHV 3102
Cdd:PRK02224 420 eRDELREREAELEAtlRTARERVEEA-EALLEAGKcpecgqpveGSphvetIEEDRERVEELEAELE----DLEEEVEEV 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3103 LERIHPLEtEQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDRE 3182
Cdd:PRK02224 495 EERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE 573
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 311033479 3183 HKRWNAQVVEITEELATLPKRAQLAAAfITYLSAAPESLRKTcLEEWTksaglEKFDLRRflctesEQLIWKSE 3256
Cdd:PRK02224 574 VAELNSKLAELKERIESLERIRTLLAA-IADAEDEIERLREK-REALA-----ELNDERR------ERLAEKRE 634
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2888-3209 |
1.37e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2888 KELLKRQSHLQAGVSKLNEAKALVDELNRKAGEQSVL---LKTKQDEADAALQMITVS----MQDASEQKTELERLKHRI 2960
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEELeaeLAELQEELEELLEQLSLAteeeLQDLAEELEELQQRLAEL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2961 AEEVVKIEERKNKIDDELKEVQPLV----NEAKLAVGNIKPESLSEIRSLRMPPDVIRDILEGVLRLMGIFD--TSWVSM 3034
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELeaaaLEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLglLALLFL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3035 KSFLAKRGVREDIATFDARNISKEIRESVEELLFKNKGSFDPKNAKRASTAAAPLAAWVKANIQYSHVLER--IHPLETE 3112
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElqLEELEQE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3113 QAGL--------ESNLKKTEDRKRKLEELLnsvgQKVSELKEKFQSRTSEAAKLEAEVSKAQ--ETIKAAEVLINQLDRE 3182
Cdd:COG4717 372 IAALlaeagvedEEELRAALEQAEEYQELK----EELEELEEQLEELLGELEELLEALDEEEleEELEELEEELEELEEE 447
|
330 340
....*....|....*....|....*..
gi 311033479 3183 HKRWNAQVVEITEELATLPKRAQLAAA 3209
Cdd:COG4717 448 LEELREELAELEAELEQLEEDGELAEL 474
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2874-3173 |
1.55e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2874 TFLHVYSAISSSKKKELLKRQshLQAGVSKLNEAKALVDELNRKAGEQSVLLKTKQDEADAALQMITVSMQDASEQKTEL 2953
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAE--LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2954 ERLKHRIAEEVVKIEERKNKIDDELKEVQPLVNEAKLAVGnIKPESLSE-IRSLRMppdvirdilegvlrlmgifdtswv 3032
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALL-LSPEDFLDaVRRLQY------------------------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3033 sMKSFLAKRgvrediatfdaRNISKEIRESVEELlfknkgsfdpkNAKRAStaaaplaawvkaniqyshvlerihpLETE 3112
Cdd:COG4942 141 -LKYLAPAR-----------REQAEELRADLAEL-----------AALRAE-------------------------LEAE 172
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 311033479 3113 QAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAE 3173
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3110-3190 |
1.85e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3110 ETEQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHKRWNAQ 3189
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
.
gi 311033479 3190 V 3190
Cdd:COG3883 95 L 95
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
3109-3173 |
2.76e-04 |
|
Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.
Pssm-ID: 428400 [Multi-domain] Cd Length: 188 Bit Score: 44.96 E-value: 2.76e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 311033479 3109 LETEQAGLESNLKKTEDRKRKLEELLNSVGQKVSEL-------KEKFQSRTSEAAKLEAEVSKAQETIKAAE 3173
Cdd:pfam05266 107 LLEELKKLEKKIAEEESEKRKLEEEIDELEKKILELerqlalaKEKKEAADKEIARLKSEAEKLEQEIQDVE 178
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3098-3208 |
2.81e-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: 45.69 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3098 QYSHVLERIHPLETEQAGLESNLKKTEDRKRKLEELLNSVG---------QKVSELKEKFQSRTSEAAKLEAEVSKAQET 3168
Cdd:COG1579 46 RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyealqKEIESLKRRISDLEDEILELMERIEELEEE 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 311033479 3169 IKAAEVLIN----QLDREHKRWNAQVVEITEELATLP-KRAQLAA 3208
Cdd:COG1579 126 LAELEAELAeleaELEEKKAELDEELAELEAELEELEaEREELAA 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2944-3201 |
3.12e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2944 QDASEQKTELERLKHRIAEEVVKIEERKNKIDDELKEVQPLvnEAKLAvgnikpESLSEIRSLRMPPDVIRDILEGVLRL 3023
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--ERRIA------ALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3024 MGIFDTSWVSMKSFLAKRgvrediatfdARNISKEIRESVEELLFKNKgsfDPKNAKRASTaaaplaaWVKANIQYshVL 3103
Cdd:COG4942 92 IAELRAELEAQKEELAEL----------LRALYRLGRQPPLALLLSPE---DFLDAVRRLQ-------YLKYLAPA--RR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3104 ERIHPLETEQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREH 3183
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|....*...
gi 311033479 3184 KRWNAQVVEITEELATLP 3201
Cdd:COG4942 230 ARLEAEAAAAAERTPAAG 247
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2886-3501 |
3.21e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2886 KKKELLKRQSHLQAGVSKLNEAKALVDELNRKAGEQSVLLKTKQDEADAALQMITVSMQDASEQKTELERLKHRIAEEVV 2965
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2966 KIEERKNKIDDELKEVQPLVNEAKlavgnikpESLSEIRSLRmppdvirdilegvlrlmgifdtswvsmksflakrgvre 3045
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAE--------AELAEAEEAL-------------------------------------- 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3046 diatfdaRNISKEIRESVEEllfknkgsfdpknakrastaaaplaaWVKANIQYSHVLERIHPLETEQAGLESNLKKTED 3125
Cdd:COG1196 368 -------LEAEAELAEAEEE--------------------------LEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3126 RKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHKRWNAQVVEITEELATLPKRAQ 3205
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3206 LAAAFITYLSAAPESLRKtcleewtksagLEKFDLRRFLCTESEQLIWkseglpsDDLSIENALVILQSRVCPFLIDPSS 3285
Cdd:COG1196 495 LLLEAEADYEGFLEGVKA-----------ALLLAGLRGLAGAVAVLIG-------VEAAYEAALEAALAAALQNIVVEDD 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3286 QATEWLKTHLKDSRLEVINQQDSNFITALELAVRfgKTLIIQEMDGVEPVLYPLLRRDLVAQGPRYVVQIGDKIIDYNEE 3365
Cdd:COG1196 557 EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAA--ALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3366 FRLFLSTRNPNPFIppdAASIVTEVNFTTTRSGLRGQLLALTIQHEKPDLEEQKTKLLQQEEDKKIQLAKLEESLLETLA 3445
Cdd:COG1196 635 ALRRAVTLAGRLRE---VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 311033479 3446 TSQGNILENKDLIESLNQTKASSALIQESLKESYKLQISLDQERDAYLPLAESASK 3501
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3043-3302 |
7.36e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3043 VREDIATFDArnISKEIRESVEELLF-KNKGS--FDPKNAKRASTAAAPLAAWVKANIQYSHVLERIHPLETEQAGLESN 3119
Cdd:TIGR02169 182 VEENIERLDL--IIDEKRQQLERLRReREKAEryQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3120 LKKTEDRKRKLEELLNSVGQKVSEL--------KEKFQSRTSEAAK--------------LEAEVSKAQETIKAAEVLIN 3177
Cdd:TIGR02169 260 ISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASlersiaekereledAEERLAKLEAEIDKLLAEIE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3178 QLDREHKRWNAQVVEITEELATLPKRAQLAAAFITYLSAAPESLRKTCLEEWTKSAGL--EKFDLRRflctESEQLIWKS 3255
Cdd:TIGR02169 340 ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLkrEINELKR----ELDRLQEEL 415
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 311033479 3256 EGLPSDDLSIENALVILQSRVcpflidpssqaTEwLKTHLKDSRLEV 3302
Cdd:TIGR02169 416 QRLSEELADLNAAIAGIEAKI-----------NE-LEEEKEDKALEI 450
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1689-1812 |
1.24e-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: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1689 GPAGTGKTESVKALGGLL-GRQVLVFNCDE---------GIDVKSMGRIFVGLV-----KCGAWGCFDEFNRLEESVLSA 1753
Cdd:pfam07728 6 GPPGTGKTELAERLAAALsNRPVFYVQLTRdtteedlfgRRNIDPGGASWVDGPlvraaREGEIAVLDEINRANPDVLNS 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1754 VSMQIQTiqdalkNHRTVCElLGKEVEVNSNSGIFI-TMNPAGKgygGRQKLPDNLKQLF 1812
Cdd:pfam07728 86 LLSLLDE------RRLLLPD-GGELVKAAPDGFRLIaTMNPLDR---GLNELSPALRSRF 135
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3109-3354 |
1.75e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3109 LETEQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHKRWNA 3188
Cdd:COG4372 57 AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3189 QVVEITEELATLPKRAQLAAAFITYLSAAPESLRKTCLEEWTKSAGLEKFDLRRFLCTESEQLIWKSEGLPSDDLSIENA 3268
Cdd:COG4372 137 QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPREL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3269 LVILQSRVCPFLIDPSSQATEWLKTHLKDSRLEVINQQDSNFITALELAVRFGKTLIIQEMDGVEPVLYPLLRRDLVAQG 3348
Cdd:COG4372 217 AEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELK 296
|
....*.
gi 311033479 3349 PRYVVQ 3354
Cdd:COG4372 297 LLALLL 302
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3120-3223 |
1.89e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3120 LKKTEDRKRKLEELLNSVGQKVSELKEKfqsrtseAAKLEAEVSKAQETIKAAEVLINQLDREHKRWNAQVVEITEELAT 3199
Cdd:COG3883 135 LEELKADKAELEAKKAELEAKLAELEAL-------KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
90 100
....*....|....*....|....
gi 311033479 3200 LPKRAQLAAAFITYLSAAPESLRK 3223
Cdd:COG3883 208 AEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3121-3208 |
3.01e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3121 KKTEDRKRKLEEL---LNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHKRWNAQVVEITEEL 3197
Cdd:COG4942 20 DAAAEAEAELEQLqqeIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90
....*....|.
gi 311033479 3198 ATLpkRAQLAA 3208
Cdd:COG4942 100 EAQ--KEELAE 108
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
1688-1728 |
3.02e-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: 41.50 E-value: 3.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 311033479 1688 YGPAGTGKTESVKALGGLLGRQVLVFNCDEGIDV------KSMGRIF 1728
Cdd:cd19481 32 YGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKyvgeseKNLRKIF 78
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2946-3203 |
3.26e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 2946 ASEQKTELERLKHRIAEEVvkieERKNKIDDELKEvqplvNEAKLAvgnikpESLSEIRSLRMPPDVIRDILEGVLRLMG 3025
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFI----KRTENIEELIKE-----KEKELE------EVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3026 IFDTSWVSMKSF-LAKRGVREDIATFDARniSKEIRESVEELlfKNKGSFDPKNAKRastaaaplaawvkaniqyshvLE 3104
Cdd:PRK03918 232 ELEELKEEIEELeKELESLEGSKRKLEEK--IRELEERIEEL--KKEIEELEEKVKE---------------------LK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3105 RIHPLETEQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFqsrtSEAAKLEAEVSKAQETIKAAEVLINQLDREHK 3184
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI----KELEEKEERLEELKKKLKELEKRLEELEERHE 362
|
250
....*....|....*....
gi 311033479 3185 RWNaQVVEITEELATLPKR 3203
Cdd:PRK03918 363 LYE-EAKAKKEELERLKKR 380
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1688-1771 |
3.29e-03 |
|
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: 40.98 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 1688 YGPAGTGKTESVKALGGLLGRQ---VLVFNC--------DEGIDVKSMGRIFVGLVKCGAWGC--FDEFNRLEESVLSAV 1754
Cdd:cd00009 25 YGPPGTGKTTLARAIANELFRPgapFLYLNAsdlleglvVAELFGHFLVRLLFELAEKAKPGVlfIDEIDSLSRGAQNAL 104
|
90
....*....|....*..
gi 311033479 1755 SMQIQTIQDALKNHRTV 1771
Cdd:cd00009 105 LRVLETLNDLRIDRENV 121
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3105-3205 |
3.62e-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: 43.51 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3105 RIHPLETEQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHK 3184
Cdd:TIGR02168 720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
90 100
....*....|....*....|.
gi 311033479 3185 RWNAQVVEITEELATLPKRAQ 3205
Cdd:TIGR02168 800 ALREALDELRAELTLLNEEAA 820
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3112-3210 |
3.90e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3112 EQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHKRWNAQVV 3191
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90
....*....|....*....
gi 311033479 3192 EITEELAtlpkrAQLAAAF 3210
Cdd:COG4942 101 AQKEELA-----ELLRALY 114
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
3104-3228 |
4.12e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3104 ERIHPLETEQAGLESNLKKTEDRKRKLEELLnsvgQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREH 3183
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQREQARETR----DEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEV 281
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 311033479 3184 KRWNAQVVEITEELATLPKRAQLAAAFITYLSAAPESL--RKTCLEE 3228
Cdd:PRK02224 282 RDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELedRDEELRD 328
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1975-1991 |
4.84e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 42.52 E-value: 4.84e-03
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3104-3203 |
5.20e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033479 3104 ERIHPLETEQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAA----KLEAEVSKAQETIKAAEVLINQL 3179
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAalleALEEELEALEEALAEAEAALRDL 417
|
90 100
....*....|....*....|....
gi 311033479 3180 DREHKrwnaqvvEITEELATLPKR 3203
Cdd:COG4913 418 RRELR-------ELEAEIASLERR 434
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1975-1992 |
5.21e-03 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 42.37 E-value: 5.21e-03
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1975-2003 |
9.71e-03 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 40.88 E-value: 9.71e-03
10 20 30
....*....|....*....|....*....|
gi 311033479 1975 VVIVGPSGAGKSTLWRML-RAALCKTGKVV 2003
Cdd:COG4778 40 VALTGPSGAGKSTLLKCIyGNYLPDSGSIL 69
|
|
| |
