|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1-298 |
1.95e-172 |
|
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: 532.83 E-value: 1.95e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1 MSMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKGLAQSGSWGCFDEFNRIDLPVLSVAAQQISI 80
Cdd:pfam12774 31 LHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKGLAQCGAWGCFDEFNRIDIEVLSVVAQQILT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 81 ILTCKKEHKKSFIFtDGDNVTMNPEFGLFLTMNPGYAGRQELPENLKINFRSVAMMVPDRQIIIRVKLASCGFIDNVVLA 160
Cdd:pfam12774 111 IQQALAANLKTFVF-EGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFRPVAMMVPDYALIAEIMLFSEGFSDAKVLA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 161 RKFFTLYKLCEEQLSKQVHYDFGLRNILSVLRTLGAAKRANPMDTESTIVMRVLRDMNLSKLIDEDEPLFLSLIEDLFPN 240
Cdd:pfam12774 190 KKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLLLRALRDMNLPKLVADDVPLFLGLISDLFPG 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462601207 241 ILLDKAGYPELEAAISRQVEEAGLINHPPWKLKVIQLFETQRVRHGMMTLGPSGAGKT 298
Cdd:pfam12774 270 VELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVGPTGSGKT 327
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
2358-2650 |
1.75e-126 |
|
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: 400.46 E-value: 1.75e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 2358 AKDVLDTILGIQPKDTSG--GGDETREAVVARLADDMLEKLPPDYvPFEVKERLQKMGPFQPMNIFLRQEIDRMQRVLSL 2435
Cdd:pfam18199 4 TNELLSTLLSLQPRSDSGggGGGSSREEIVLELAKDILEKLPEPF-DIEEAEEKYPVGYEDPLNTVLLQEIERFNKLLKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 2436 VRSTLTELKLAIDGTIIMSENLRDALDCMFDARIPAWWKKASWISS-TLGFWFTELIERNSQFTSWVF-NGRPHCFWMTG 2513
Cdd:pfam18199 83 IRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLkPLGSWIRDLLERLKQLQDWLDdEGPPKVFWLSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 2514 FFNPQGFLTAMRQEITRANKgWALDNMVLCNEVTKWM-KDDISAPPTEGVYVYGLYLEGAGWDKRNMKLIESKPKVLFEL 2592
Cdd:pfam18199 163 FFFPQAFLTAVLQNYARKNG-WPIDKLSFDFEVTKKVsPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFSP 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 2593 MPVIRIYAENNTL--RDPRFYSCPIYKKPVRTDLNYIAAVDLRTAQTPEHWVLRGVALLC 2650
Cdd:pfam18199 242 LPVIHLKPVESDKkkLDENTYECPVYKTSERHSTNFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
1603-1824 |
3.09e-118 |
|
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: 373.32 E-value: 3.09e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1603 SEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESRNELQITSLNHKYFRNHLEDSLSLGRPLLIEDVG 1682
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1683 EELDPALDNVLERNFIKTGSTFKVKVGDKEVDVLDGFRLYITTKLPNPAYTPEISARTSIIDFTVTMKGLEDQLLGRVIL 1762
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462601207 1763 TEKQELEKERTHLMEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKRTAEEV 1824
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
11-2314 |
1.42e-117 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 419.78 E-value: 1.42e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 11 AGTGKTETTKDMGRCLGKYVvvfncsDQMDFRGlgRIFKGLAQSGSWGcFDEFNRIDLPVLSVAA--QQISIILTCKKEH 88
Cdd:COG5245 952 VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISRTILVdeYLNSDEFRMLEEL 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 89 KKSFIftdgDNVTMNPEFGLFLTMNPgyagRQELPENLKINFRSVAMMVPDRQIIIRVKlascgfidnvVLARKFFTLYK 168
Cdd:COG5245 1023 NSAVV----EHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSNIPFGAIKSRRE----------SLDREIGAFNN 1084
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 169 LCEEQLSKQVHYDFglrnilsvlRTL-GAAKRANPMDTESTivmrvlrdMNLSKLIdedEPLFLSLIEDLFPNI--LLDK 245
Cdd:COG5245 1085 EVDGIAREEDELMF---------YPMfKSLKAKHRMLEEKT--------EYLNKIL---SITGLPLISDTLRERidTLDA 1144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 246 AGYPELEAAISRQVEEAGLINHPPWKlKVIQLFETQRVRHGMMTLGPSGAGKTTCIHTLMRAMTDCGKPHREMRMnpkai 325
Cdd:COG5245 1145 EWDSFCRISESLKKYESQQVSGLDVA-QFVSFLRSVDTGAFHAEYFRVFLCKIKHYTDACDYLWHVKSPYVKKKY----- 1218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 326 tapqmfgrLDvATNDWTdGIFSTLWRKTLRAK-KGEHIWIILDGpvdaiWIENLNSVLDDNKTLTLANGDRipmapncKI 404
Cdd:COG5245 1219 --------FD-ADMELR-QFFLMFNREDMEARlADSKMEYEVER-----YVEKTKAEVSSLKLELSSVGEG-------QV 1276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 405 IFEphNIDnASPATVSRNGMVFMSSSILDWSPILEGFL--------KKRSPQEAEILRQLYTESF-----PDLYRFCIQ- 470
Cdd:COG5245 1277 VVS--NLG-SIGDKVGRCLVEYDSISRLSTKGVFLDELgdtkryldECLDFFSCFEEVQKEIDELsmvfcADALRFSADl 1353
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 471 ----------NLEYKMEVLEAfVITQSINMLQGLiplKEQGGEVsqaHLGRLFVFALLWSAGAALELDGRRRLELWLR-- 538
Cdd:COG5245 1354 yhivkerrfsGVLAGSDASES-LGGKSIELAAIL---EHKDLIV---EMKRGINDVLKLRIFGDKCRESTPRFYLISDgd 1426
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 539 -SRPTGTLELPPPAGPGDTAFDYYVAPDGTWTHWNTRTQEYLYPSDttpeygsILVPNVDNVRTDFLIQTIAKQGKAVLL 617
Cdd:COG5245 1427 lIKDLNERSDYEEMLIMMFNISAVITNNGSIAGFELRGERVMLRKE-------VVIPTSDTGFVDSFSNEALNTLRSYIY 1499
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 618 IGEQGTAKTVIIKG-FMSKYDPEchmIKSLNFS-SATTPLM---FQRTIESYVDKRMGTTYGPPAGKKMTVFIDDVNMPI 692
Cdd:COG5245 1500 CGPPGSGKEMLMCPsLRSELITE---VKYFNFStCTMTPSKlsvLERETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPY 1576
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 693 INEWGDQVTNEIVRQLMEQNGFYN-LEKpgEFTSIVDIqFLAAMIHPGG--GRNDIPQRLKRQFSIFNCTLPSEASVDKI 769
Cdd:COG5245 1577 GFEYYPPTVIVFLRPLVERQGFWSsIAV--SWVTICGI-ILYGACNPGTdeGRVKYYERFIRKPVFVFCCYPELASLRNI 1653
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 770 FGVIGVGHYCTQRGFSEEVRDSVTKLVPLTRRLWQMTKikmlpTPAKFHYVFNLRDLSRVWQGMLNTTSEVIKEPN-DLL 848
Cdd:COG5245 1654 YEAVLMGSYLCFDEFNRLSEETMSASVELYLSSKDKTK-----FFLQMNYGYKPRELTRSLRAIFGYAETRIDTPDvSLI 1728
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 849 KLWKHECKRVIADRFTVSSDVTWFDKALVSLVEEEFGE-------EKKLFVDcgiDTYFVDFlrdapeaagetsEEADAE 921
Cdd:COG5245 1729 IDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREmiaghigEAEITFS---MILFFGM------------ACLLKK 1793
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 922 TPKIYepiesfshLKERLNMFlqlYNESIRgagMDMVFFADAMVHLVKISRVIRTPQGNALLVGVGGSGKQSLTRLASFI 1001
Cdd:COG5245 1794 DLAVF--------VEEVRKIF---GSSHLD---VEAVAYKDALLHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWL 1859
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1002 AGYVSFQITLTRSYNTSNLMEDLKVLYRTAGQQGKGITFIFTDNEIKDESFLEYMNNVLSSGEVSNLFARDEIDEINSDL 1081
Cdd:COG5245 1860 NPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENL 1939
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1082 ASVMKKEfPRCLPTNENLHDYFMSRVRQNLHIVL-CFSPVGEKFRNRALkFPALISGCTIDWFSRWPKDALVAVSEHFLT 1160
Cdd:COG5245 1940 RFVFEST-SLEKDTEATLTRVFLVYMEENLPVVFsACCSQDTSVLAGIR-SPALKNRCFIDFKKLWDTEEMSQYANSVET 2017
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1161 -SYDIDCSLEIKKEVVQCMGS-FQDGVAEKCVDYFQR-FRRSTHV--TPKSYLSFIQG---YKFIYGEKHVEVRTLANRM 1232
Cdd:COG5245 2018 lSRDGGRVFFINGELGVGKGAlISEVFGDDAVVIEGRgFEISMIEgsLGESKIKFIGGlkvYDARCVIYIEELDCTNVNL 2097
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1233 NTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSISKDKAIAEEK 1312
Cdd:COG5245 2098 VEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKF 2177
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1313 LEAAKPALEEAEAALQTIRPSDIATVRTLGRPPHLIMRIMD--CVLLLFQRKVsavkidleksctmpsWQESLKLMTAGN 1390
Cdd:COG5245 2178 KSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEdvCDLLGFEAKI---------------WFGEQQSLRRDD 2242
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1391 FLQNLQQFPKDT-INEEVIEFL-SPYFEMPDYNIETAKR---VCGNvagLCSWTKAMASFFSINKEVLPLKANLVVQENR 1465
Cdd:COG5245 2243 FIRIIGKYPDEIeFDLEARRFReARECSDPSFTGSILNRaskACGP---LKRWLVRECNRSKVLEVKIPLREEEKRIDGE 2319
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1466 HLLAMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDAERCRHKMQTASTLISGLAGEKERWTEQSQEFAAQTKR 1545
Cdd:COG5245 2320 AFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVE 2399
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1546 LVGDVLLATAFLSYSGPFNQEFRDLLLNDwRKEMKARKIPFGKNLNLSEMLIDAPTISEWNLQGLPNDDLSIQNGIIVTK 1625
Cdd:COG5245 2400 LDGDGHPSSCLHPYIGTLGFLCRAIEFGM-SFIRISKEFRDKEIRRRQFITEGVQKIEDFKEEACSTDYGLENSRIRKDL 2478
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1626 ASRYPLLIDPQTQGKIWIKNKESRNELQITSLNHKYFRNHLEDSLSLGRPLLIEDvGEELDPALDNVLERNFIKTGSTFK 1705
Cdd:COG5245 2479 QDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSDKIIGD-AEALDEEIGRLIKEEFKSNLSEVK 2557
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1706 VKVGDKEVDVLDGFRLYITTKLPNPAYTPEISARTSIIDFTVTMKGLEDQLLGRVILTEKQELEKERTHLMEDVTANKRR 1785
Cdd:COG5245 2558 VMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKALNALKACGSLF 2637
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1786 MKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKRTAEEVTQKLEISAETEVQINSAREEYRPVATRGSILYFLITEMRLV 1865
Cdd:COG5245 2638 LWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEK 2717
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1866 NEMYQTSLRQFLGLFDlsLARSVKSpitskRIANIIEHMTYEVYKYaargLYEEhkflFTLLLTLKIDIQRN-RVKHEEF 1944
Cdd:COG5245 2718 ALMYNKSICELSSEFE--KWRRMKS-----KYLCAIRYMLMSSEWI----LDHE----DRSGFIHRLDVSFLlRTKRFVS 2782
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1945 LTLIKGGASLDLKACppkpskwilDITWLNLVELSKLRQFSDVLDQISRNEKMWKIWFDKenpeeeplpnAYDKSLDCFR 2024
Cdd:COG5245 2783 TLLEDKNYRQVLSSC---------SLYGNDVISHSCDRFDRDVYRALKHQMDNRTHSTIL----------TSNSKTNPYK 2843
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 2025 RLLLIRSWcpdrtiaqARKYIVDSMGEKYaegvilDLEK-TWEESDPRTPLICLLsMGSDPTDSIIalgKRLKIETRyvs 2103
Cdd:COG5245 2844 EYTYNDSW--------AEAFEVEDSGDLY------KFEEgLLELIVGHAPLIYAH-KKSLENERNV---DRLGSKEN--- 2902
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 2104 mgqgqEVHARKLLQQTMANGGWALLQNCHLGLDFMDELMDIIIE----TELVHDAFRLWMTTEAHKQFPITLLQMSIKFA 2179
Cdd:COG5245 2903 -----EVYAVLNSLFSRKEKSWFEVYNISLSFGWFKRYVEDVVYpikaSRVCGKVKNMWTSMVDADMLPIQLLIAIDSFV 2977
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 2180 NDPPQGLRAGLKrtysgvsqDLLdvssGSQWKPMLYA----------VAFLHSTVQERRKFGALGWNIPYEFNQADFNAT 2249
Cdd:COG5245 2978 SSTYPETGCGYA--------DLV----EIDRYPFDYTlviacddafyLSWEHAAVASVISAGPKENNEEIYFGDKDFEFK 3045
|
2330 2340 2350 2360 2370 2380 2390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462601207 2250 VQFIQNHLdDMDVKKGVSWTTIRYMIGEIQYGGR--------VTDDYDKRLLNTFAKVWFSENMFGPDFSFYQ 2314
Cdd:COG5245 3046 THLLKNIL-FLNHLNARKWGNNRDLIFTIVYGKKhslmedskVVDKYCRGYGAHETSSQILASVPGGDPELVK 3117
|
|
| AAA_8 |
pfam12780 |
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
955-1215 |
2.07e-100 |
|
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: 323.79 E-value: 2.07e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 955 MDMVFFADAMVHLVKISRVIRTPQGNALLVGVGGSGKQSLTRLASFIAGYVSFQITLTRSYNTSNLMEDLKVLYRTAGQQ 1034
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1035 GKGITFIFTDNEIKDESFLEYMNNVLSSGEVSNLFARDEIDEINSDLASVMKKEfpRCLPTNENLHDYFMSRVRQNLHIV 1114
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQ--NIEDSREAVYNYFVKRCRNNLHIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1115 LCFSPVGEKFRNRALKFPALISGCTIDWFSRWPKDALVAVSEHFLTsyDIDCSLEIKKEVVQCMGSFQDGVAEKCVDYFQ 1194
Cdd:pfam12780 159 LCMSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFLE--DIEIPEELKSNVVKVFVYVHSSVEDMSKKFYE 236
|
250 260
....*....|....*....|.
gi 2462601207 1195 RFRRSTHVTPKSYLSFIQGYK 1215
Cdd:pfam12780 237 ELKRKNYVTPKSYLELLRLYK 257
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
9-427 |
2.25e-12 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 73.48 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 9 GPAGTGKTETTKDMG-RCLGKYVVVFNCSDQMdfRGLGRIFKGLAQsGSWGCFDEFNRIDLPVLSVAaqqISIILTCKKE 87
Cdd:COG5245 1616 GACNPGTDEGRVKYYeRFIRKPVFVFCCYPEL--ASLRNIYEAVLM-GSYLCFDEFNRLSEETMSAS---VELYLSSKDK 1689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 88 HKksfiftdgdnvtmnpefgLFLTMNPGYAGRqELPENLkINFRSVAMMVPDRQIIIRVKLASCGFIdnvvlARKFFTLY 167
Cdd:COG5245 1690 TK------------------FFLQMNYGYKPR-ELTRSL-RAIFGYAETRIDTPDVSLIIDWYCEAI-----REKIDRLV 1744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 168 KLCEEQLSKQVHYDFGLRNILSVLRTLGAakranpmdtESTIVMRVLRDMNLSKLIDEDEPLFLSLIEDLFPNilldkaG 247
Cdd:COG5245 1745 QQKESSTSRQDLYDFGLRAIREMIAGHIG---------EAEITFSMILFFGMACLLKKDLAVFVEEVRKIFGS------S 1809
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 248 YPELEAAISRQVEEAGLINHPpwKLKVIQLfetqrvrHGMMtLGPSGAGKTtcihTLMRAMtdCGKPHREMRmnpkaita 327
Cdd:COG5245 1810 HLDVEAVAYKDALLHILRSRR--GLLVVGG-------HGVL-KGVLIRGAC----DAREFV--CWLNPRNMR-------- 1865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 328 pQMFGRLDVATNDWTDGIFSTLWRKTLraKKGEHIWIILDG-PVDAIWIENLNSVLDDNKTLTLANG-DRIPMAPNCKII 405
Cdd:COG5245 1866 -EIFGHRDELTGDFRDSLKVQDLRRNI--HGGRECLFIFESiPVESSFLEDFNPLLDNNRFLCLFSGnERIRIPENLRFV 1942
|
410 420
....*....|....*....|..
gi 2462601207 406 FEPHNIDNASPATVSRNGMVFM 427
Cdd:COG5245 1943 FESTSLEKDTEATLTRVFLVYM 1964
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
1208-1329 |
3.61e-07 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 52.65 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1208 LSFIQGYKFIYGEKHVEvRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQA-----AE 1282
Cdd:PRK07352 29 LAIVIGLLYYFGRGFLG-KILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAiraeiEK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462601207 1283 KVKAEVQKVKDRAQAIVDSiSKDKAIAEEKLEAAKPALEEAEAALQT 1329
Cdd:PRK07352 108 QAIEDMARLKQTAAADLSA-EQERVIAQLRREAAELAIAKAESQLPG 153
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1237-1326 |
1.80e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 49.46 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1237 EKLKEASESVAALSKELEAKEKELQVANDKADmvlKEVTMKAQAAEKVKAEVQKVKDRAQAivdsisKDKAIAEEKLeAA 1316
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE---EEAKAKAAAEAKKKAEEAKKKAEAEA------KAKAEAEAKA-KA 191
|
90
....*....|
gi 2462601207 1317 KPALEEAEAA 1326
Cdd:TIGR02794 192 EEAKAKAEAA 201
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1214-1328 |
9.31e-05 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 44.35 E-value: 9.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1214 YKFIYgeKHVeVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKE-----VTMKAQAAEKVKAEV 1288
Cdd:cd06503 17 KKFLW--KPI-LKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEarkeaEKIKEEILAEAKEEA 93
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2462601207 1289 QKVKDRAQAIVDSiSKDKAIAEEKLEAAKPALEEAEAALQ 1328
Cdd:cd06503 94 ERILEQAKAEIEQ-EKEKALAELRKEVADLAVEAAEKILG 132
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1-298 |
1.95e-172 |
|
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: 532.83 E-value: 1.95e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1 MSMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKGLAQSGSWGCFDEFNRIDLPVLSVAAQQISI 80
Cdd:pfam12774 31 LHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKGLAQCGAWGCFDEFNRIDIEVLSVVAQQILT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 81 ILTCKKEHKKSFIFtDGDNVTMNPEFGLFLTMNPGYAGRQELPENLKINFRSVAMMVPDRQIIIRVKLASCGFIDNVVLA 160
Cdd:pfam12774 111 IQQALAANLKTFVF-EGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFRPVAMMVPDYALIAEIMLFSEGFSDAKVLA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 161 RKFFTLYKLCEEQLSKQVHYDFGLRNILSVLRTLGAAKRANPMDTESTIVMRVLRDMNLSKLIDEDEPLFLSLIEDLFPN 240
Cdd:pfam12774 190 KKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLLLRALRDMNLPKLVADDVPLFLGLISDLFPG 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462601207 241 ILLDKAGYPELEAAISRQVEEAGLINHPPWKLKVIQLFETQRVRHGMMTLGPSGAGKT 298
Cdd:pfam12774 270 VELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVGPTGSGKT 327
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
2358-2650 |
1.75e-126 |
|
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: 400.46 E-value: 1.75e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 2358 AKDVLDTILGIQPKDTSG--GGDETREAVVARLADDMLEKLPPDYvPFEVKERLQKMGPFQPMNIFLRQEIDRMQRVLSL 2435
Cdd:pfam18199 4 TNELLSTLLSLQPRSDSGggGGGSSREEIVLELAKDILEKLPEPF-DIEEAEEKYPVGYEDPLNTVLLQEIERFNKLLKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 2436 VRSTLTELKLAIDGTIIMSENLRDALDCMFDARIPAWWKKASWISS-TLGFWFTELIERNSQFTSWVF-NGRPHCFWMTG 2513
Cdd:pfam18199 83 IRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLkPLGSWIRDLLERLKQLQDWLDdEGPPKVFWLSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 2514 FFNPQGFLTAMRQEITRANKgWALDNMVLCNEVTKWM-KDDISAPPTEGVYVYGLYLEGAGWDKRNMKLIESKPKVLFEL 2592
Cdd:pfam18199 163 FFFPQAFLTAVLQNYARKNG-WPIDKLSFDFEVTKKVsPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFSP 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 2593 MPVIRIYAENNTL--RDPRFYSCPIYKKPVRTDLNYIAAVDLRTAQTPEHWVLRGVALLC 2650
Cdd:pfam18199 242 LPVIHLKPVESDKkkLDENTYECPVYKTSERHSTNFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
1603-1824 |
3.09e-118 |
|
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: 373.32 E-value: 3.09e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1603 SEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESRNELQITSLNHKYFRNHLEDSLSLGRPLLIEDVG 1682
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1683 EELDPALDNVLERNFIKTGSTFKVKVGDKEVDVLDGFRLYITTKLPNPAYTPEISARTSIIDFTVTMKGLEDQLLGRVIL 1762
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462601207 1763 TEKQELEKERTHLMEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKRTAEEV 1824
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
11-2314 |
1.42e-117 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 419.78 E-value: 1.42e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 11 AGTGKTETTKDMGRCLGKYVvvfncsDQMDFRGlgRIFKGLAQSGSWGcFDEFNRIDLPVLSVAA--QQISIILTCKKEH 88
Cdd:COG5245 952 VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISRTILVdeYLNSDEFRMLEEL 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 89 KKSFIftdgDNVTMNPEFGLFLTMNPgyagRQELPENLKINFRSVAMMVPDRQIIIRVKlascgfidnvVLARKFFTLYK 168
Cdd:COG5245 1023 NSAVV----EHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSNIPFGAIKSRRE----------SLDREIGAFNN 1084
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 169 LCEEQLSKQVHYDFglrnilsvlRTL-GAAKRANPMDTESTivmrvlrdMNLSKLIdedEPLFLSLIEDLFPNI--LLDK 245
Cdd:COG5245 1085 EVDGIAREEDELMF---------YPMfKSLKAKHRMLEEKT--------EYLNKIL---SITGLPLISDTLRERidTLDA 1144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 246 AGYPELEAAISRQVEEAGLINHPPWKlKVIQLFETQRVRHGMMTLGPSGAGKTTCIHTLMRAMTDCGKPHREMRMnpkai 325
Cdd:COG5245 1145 EWDSFCRISESLKKYESQQVSGLDVA-QFVSFLRSVDTGAFHAEYFRVFLCKIKHYTDACDYLWHVKSPYVKKKY----- 1218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 326 tapqmfgrLDvATNDWTdGIFSTLWRKTLRAK-KGEHIWIILDGpvdaiWIENLNSVLDDNKTLTLANGDRipmapncKI 404
Cdd:COG5245 1219 --------FD-ADMELR-QFFLMFNREDMEARlADSKMEYEVER-----YVEKTKAEVSSLKLELSSVGEG-------QV 1276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 405 IFEphNIDnASPATVSRNGMVFMSSSILDWSPILEGFL--------KKRSPQEAEILRQLYTESF-----PDLYRFCIQ- 470
Cdd:COG5245 1277 VVS--NLG-SIGDKVGRCLVEYDSISRLSTKGVFLDELgdtkryldECLDFFSCFEEVQKEIDELsmvfcADALRFSADl 1353
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 471 ----------NLEYKMEVLEAfVITQSINMLQGLiplKEQGGEVsqaHLGRLFVFALLWSAGAALELDGRRRLELWLR-- 538
Cdd:COG5245 1354 yhivkerrfsGVLAGSDASES-LGGKSIELAAIL---EHKDLIV---EMKRGINDVLKLRIFGDKCRESTPRFYLISDgd 1426
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 539 -SRPTGTLELPPPAGPGDTAFDYYVAPDGTWTHWNTRTQEYLYPSDttpeygsILVPNVDNVRTDFLIQTIAKQGKAVLL 617
Cdd:COG5245 1427 lIKDLNERSDYEEMLIMMFNISAVITNNGSIAGFELRGERVMLRKE-------VVIPTSDTGFVDSFSNEALNTLRSYIY 1499
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 618 IGEQGTAKTVIIKG-FMSKYDPEchmIKSLNFS-SATTPLM---FQRTIESYVDKRMGTTYGPPAGKKMTVFIDDVNMPI 692
Cdd:COG5245 1500 CGPPGSGKEMLMCPsLRSELITE---VKYFNFStCTMTPSKlsvLERETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPY 1576
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 693 INEWGDQVTNEIVRQLMEQNGFYN-LEKpgEFTSIVDIqFLAAMIHPGG--GRNDIPQRLKRQFSIFNCTLPSEASVDKI 769
Cdd:COG5245 1577 GFEYYPPTVIVFLRPLVERQGFWSsIAV--SWVTICGI-ILYGACNPGTdeGRVKYYERFIRKPVFVFCCYPELASLRNI 1653
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 770 FGVIGVGHYCTQRGFSEEVRDSVTKLVPLTRRLWQMTKikmlpTPAKFHYVFNLRDLSRVWQGMLNTTSEVIKEPN-DLL 848
Cdd:COG5245 1654 YEAVLMGSYLCFDEFNRLSEETMSASVELYLSSKDKTK-----FFLQMNYGYKPRELTRSLRAIFGYAETRIDTPDvSLI 1728
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 849 KLWKHECKRVIADRFTVSSDVTWFDKALVSLVEEEFGE-------EKKLFVDcgiDTYFVDFlrdapeaagetsEEADAE 921
Cdd:COG5245 1729 IDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREmiaghigEAEITFS---MILFFGM------------ACLLKK 1793
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 922 TPKIYepiesfshLKERLNMFlqlYNESIRgagMDMVFFADAMVHLVKISRVIRTPQGNALLVGVGGSGKQSLTRLASFI 1001
Cdd:COG5245 1794 DLAVF--------VEEVRKIF---GSSHLD---VEAVAYKDALLHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWL 1859
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1002 AGYVSFQITLTRSYNTSNLMEDLKVLYRTAGQQGKGITFIFTDNEIKDESFLEYMNNVLSSGEVSNLFARDEIDEINSDL 1081
Cdd:COG5245 1860 NPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENL 1939
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1082 ASVMKKEfPRCLPTNENLHDYFMSRVRQNLHIVL-CFSPVGEKFRNRALkFPALISGCTIDWFSRWPKDALVAVSEHFLT 1160
Cdd:COG5245 1940 RFVFEST-SLEKDTEATLTRVFLVYMEENLPVVFsACCSQDTSVLAGIR-SPALKNRCFIDFKKLWDTEEMSQYANSVET 2017
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1161 -SYDIDCSLEIKKEVVQCMGS-FQDGVAEKCVDYFQR-FRRSTHV--TPKSYLSFIQG---YKFIYGEKHVEVRTLANRM 1232
Cdd:COG5245 2018 lSRDGGRVFFINGELGVGKGAlISEVFGDDAVVIEGRgFEISMIEgsLGESKIKFIGGlkvYDARCVIYIEELDCTNVNL 2097
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1233 NTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSISKDKAIAEEK 1312
Cdd:COG5245 2098 VEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKF 2177
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1313 LEAAKPALEEAEAALQTIRPSDIATVRTLGRPPHLIMRIMD--CVLLLFQRKVsavkidleksctmpsWQESLKLMTAGN 1390
Cdd:COG5245 2178 KSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEdvCDLLGFEAKI---------------WFGEQQSLRRDD 2242
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1391 FLQNLQQFPKDT-INEEVIEFL-SPYFEMPDYNIETAKR---VCGNvagLCSWTKAMASFFSINKEVLPLKANLVVQENR 1465
Cdd:COG5245 2243 FIRIIGKYPDEIeFDLEARRFReARECSDPSFTGSILNRaskACGP---LKRWLVRECNRSKVLEVKIPLREEEKRIDGE 2319
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1466 HLLAMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDAERCRHKMQTASTLISGLAGEKERWTEQSQEFAAQTKR 1545
Cdd:COG5245 2320 AFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVE 2399
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1546 LVGDVLLATAFLSYSGPFNQEFRDLLLNDwRKEMKARKIPFGKNLNLSEMLIDAPTISEWNLQGLPNDDLSIQNGIIVTK 1625
Cdd:COG5245 2400 LDGDGHPSSCLHPYIGTLGFLCRAIEFGM-SFIRISKEFRDKEIRRRQFITEGVQKIEDFKEEACSTDYGLENSRIRKDL 2478
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1626 ASRYPLLIDPQTQGKIWIKNKESRNELQITSLNHKYFRNHLEDSLSLGRPLLIEDvGEELDPALDNVLERNFIKTGSTFK 1705
Cdd:COG5245 2479 QDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSDKIIGD-AEALDEEIGRLIKEEFKSNLSEVK 2557
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1706 VKVGDKEVDVLDGFRLYITTKLPNPAYTPEISARTSIIDFTVTMKGLEDQLLGRVILTEKQELEKERTHLMEDVTANKRR 1785
Cdd:COG5245 2558 VMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKALNALKACGSLF 2637
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1786 MKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKRTAEEVTQKLEISAETEVQINSAREEYRPVATRGSILYFLITEMRLV 1865
Cdd:COG5245 2638 LWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEK 2717
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1866 NEMYQTSLRQFLGLFDlsLARSVKSpitskRIANIIEHMTYEVYKYaargLYEEhkflFTLLLTLKIDIQRN-RVKHEEF 1944
Cdd:COG5245 2718 ALMYNKSICELSSEFE--KWRRMKS-----KYLCAIRYMLMSSEWI----LDHE----DRSGFIHRLDVSFLlRTKRFVS 2782
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1945 LTLIKGGASLDLKACppkpskwilDITWLNLVELSKLRQFSDVLDQISRNEKMWKIWFDKenpeeeplpnAYDKSLDCFR 2024
Cdd:COG5245 2783 TLLEDKNYRQVLSSC---------SLYGNDVISHSCDRFDRDVYRALKHQMDNRTHSTIL----------TSNSKTNPYK 2843
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 2025 RLLLIRSWcpdrtiaqARKYIVDSMGEKYaegvilDLEK-TWEESDPRTPLICLLsMGSDPTDSIIalgKRLKIETRyvs 2103
Cdd:COG5245 2844 EYTYNDSW--------AEAFEVEDSGDLY------KFEEgLLELIVGHAPLIYAH-KKSLENERNV---DRLGSKEN--- 2902
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 2104 mgqgqEVHARKLLQQTMANGGWALLQNCHLGLDFMDELMDIIIE----TELVHDAFRLWMTTEAHKQFPITLLQMSIKFA 2179
Cdd:COG5245 2903 -----EVYAVLNSLFSRKEKSWFEVYNISLSFGWFKRYVEDVVYpikaSRVCGKVKNMWTSMVDADMLPIQLLIAIDSFV 2977
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 2180 NDPPQGLRAGLKrtysgvsqDLLdvssGSQWKPMLYA----------VAFLHSTVQERRKFGALGWNIPYEFNQADFNAT 2249
Cdd:COG5245 2978 SSTYPETGCGYA--------DLV----EIDRYPFDYTlviacddafyLSWEHAAVASVISAGPKENNEEIYFGDKDFEFK 3045
|
2330 2340 2350 2360 2370 2380 2390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462601207 2250 VQFIQNHLdDMDVKKGVSWTTIRYMIGEIQYGGR--------VTDDYDKRLLNTFAKVWFSENMFGPDFSFYQ 2314
Cdd:COG5245 3046 THLLKNIL-FLNHLNARKWGNNRDLIFTIVYGKKhslmedskVVDKYCRGYGAHETSSQILASVPGGDPELVK 3117
|
|
| AAA_8 |
pfam12780 |
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
955-1215 |
2.07e-100 |
|
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: 323.79 E-value: 2.07e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 955 MDMVFFADAMVHLVKISRVIRTPQGNALLVGVGGSGKQSLTRLASFIAGYVSFQITLTRSYNTSNLMEDLKVLYRTAGQQ 1034
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1035 GKGITFIFTDNEIKDESFLEYMNNVLSSGEVSNLFARDEIDEINSDLASVMKKEfpRCLPTNENLHDYFMSRVRQNLHIV 1114
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQ--NIEDSREAVYNYFVKRCRNNLHIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1115 LCFSPVGEKFRNRALKFPALISGCTIDWFSRWPKDALVAVSEHFLTsyDIDCSLEIKKEVVQCMGSFQDGVAEKCVDYFQ 1194
Cdd:pfam12780 159 LCMSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFLE--DIEIPEELKSNVVKVFVYVHSSVEDMSKKFYE 236
|
250 260
....*....|....*....|.
gi 2462601207 1195 RFRRSTHVTPKSYLSFIQGYK 1215
Cdd:pfam12780 237 ELKRKNYVTPKSYLELLRLYK 257
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
580-761 |
7.19e-88 |
|
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: 284.28 E-value: 7.19e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 580 YPSDTtpEYGSILVPNVDNVRTDFLIQTIAKQGKAVLLIGEQGTAKTVIIKGFMSKYDPECHMIKSLNFSSATTPLMFQR 659
Cdd:pfam12775 1 IPPDV--PFSEILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPLFINFSAQTTSNQTQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 660 TIESYVDKRMGTTYGPPAGKKMTVFIDDVNMPIINEWGDQVTNEIVRQLMEQNGFYNLEKPgEFTSIVDIQFLAAMIHPG 739
Cdd:pfam12775 79 IIESKLEKRRKGVYGPPGGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKL-TFKEIVDVQFVAAMGPPG 157
|
170 180
....*....|....*....|..
gi 2462601207 740 GGRNDIPQRLKRQFSIFNCTLP 761
Cdd:pfam12775 158 GGRNDITPRLLRHFNVFNITFP 179
|
|
| AAA_lid_11 |
pfam18198 |
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the ... |
2210-2349 |
3.09e-75 |
|
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: 246.60 E-value: 3.09e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 2210 WKPMLYAVAFLHSTVQERRKFGALGWNIPYEFNQADFNATVQFIQNHLDdmDVKKGVSWTTIRYMIGEIQYGGRVTDDYD 2289
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLD--EYDEKIPWDALRYLIGEINYGGRVTDDWD 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462601207 2290 KRLLNTFAKVWFSENMFGPDFSFYQG-YNIPKCSTVDNYLQYIQSLPAYDSPEVFGLHPNA 2349
Cdd:pfam18198 79 RRLLNTYLEEFFNPEVLEEDFKFSPSlYYIPPDGDLEDYLEYIESLPLVDSPEVFGLHPNA 139
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
2069-2178 |
4.61e-51 |
|
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: 176.10 E-value: 4.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 2069 DPRTPLICLLSMGSDPTDSIIALGKRLKIETRY--VSMGQGQEVHARKLLQQTMANGGWALLQNCHLGLDFMDELMDII- 2145
Cdd:pfam03028 1 SPTTPLIFILSPGSDPTADLEKLAKKLGFGGKLhsISLGQGQGPIAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKILe 80
|
90 100 110
....*....|....*....|....*....|....
gi 2462601207 2146 -IETELVHDAFRLWMTTEAHKQFPITLLQMSIKF 2178
Cdd:pfam03028 81 eLPEETLHPDFRLWLTSEPSPKFPISILQNSIKI 114
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
1231-1576 |
1.10e-47 |
|
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: 175.26 E-value: 1.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1231 RMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSISKDKAIAE 1310
Cdd:pfam12777 2 RLENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKACE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1311 EKLEAAKPALEEAEAALQTIRPSDIATVRTLGRPPHLIMRIMDCVLLLFqrkVSAVKIDLEKsctmpSWQESlKLMTA-- 1388
Cdd:pfam12777 82 EDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILM---APGGKIPKDK-----SWKAA-KIMMAkv 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1389 GNFLQNLQQFPKDTINEEVIEFLSPYFEMPDYNIETAKRVCGNVAGLCSWTKAMASFFSINKEVLPlKANLVVQENRHLL 1468
Cdd:pfam12777 153 DGFLDSLIKFDKEHIHEACLKAFKPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAP-KRQALEEANADLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1469 AMQD-LQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDAERCRHKMQTASTLISGLAGEKERWTEQSQEFAAQTKRLV 1547
Cdd:pfam12777 232 AAQEkLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLC 311
|
330 340 350
....*....|....*....|....*....|
gi 2462601207 1548 GDVLLATAFLSYSGPFNQEFRDLLLND-WR 1576
Cdd:pfam12777 312 GDILLISAFISYLGFFTKKYRNELLDKfWI 341
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
453-572 |
1.80e-22 |
|
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA domain 5 in the dynein heavy chain. This domain is composed of 8 alpha helices.
Pssm-ID: 465532 [Multi-domain] Cd Length: 126 Bit Score: 95.04 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 453 LRQLYTESFPDLYRFCIQNLEYKMEVLEAFVITQSINMLQGLIP-------LKEQGGEVSQAHLGRLFVFALLWSAGAAL 525
Cdd:pfam17852 1 LEPLFEWLVPPALEFVRKNCKEIVPTSDLNLVQSLCRLLESLLDevleyngVHPLSPDKLKEYLEKLFLFALVWSIGGTL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2462601207 526 ELDGRRRLELWLRSRPTGtLELPPPagPGDTAFDYYV-APDGTWTHWN 572
Cdd:pfam17852 81 DEDSRKKFDEFLRELFSG-LDLPPP--EKGTVYDYFVdLEKGEWVPWS 125
|
|
| AAA_lid_1 |
pfam17857 |
AAA+ lid domain; This domain represents the AAA lid domain from dynein heavy chain D3. |
795-884 |
7.79e-18 |
|
AAA+ lid domain; This domain represents the AAA lid domain from dynein heavy chain D3.
Pssm-ID: 465535 [Multi-domain] Cd Length: 100 Bit Score: 80.75 E-value: 7.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 795 LVPLTRRLWQMTKIKMLPTPAKFHYVFNLRDLSRVWQGMLNTTSEVIKEPNDLLKLWKHECKRVIADRFTVSSDVTWFDK 874
Cdd:pfam17857 1 LIAAALAFHQKIAATFLPTAIKFHYIFNLRDFANIFQGILFSSAECLKSPLDLIRLWLHESERVYGDKMVDEKDFDLFDK 80
|
90
....*....|
gi 2462601207 875 ALVSLVEEEF 884
Cdd:pfam17857 81 IQMASLKKFF 90
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
9-427 |
2.25e-12 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 73.48 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 9 GPAGTGKTETTKDMG-RCLGKYVVVFNCSDQMdfRGLGRIFKGLAQsGSWGCFDEFNRIDLPVLSVAaqqISIILTCKKE 87
Cdd:COG5245 1616 GACNPGTDEGRVKYYeRFIRKPVFVFCCYPEL--ASLRNIYEAVLM-GSYLCFDEFNRLSEETMSAS---VELYLSSKDK 1689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 88 HKksfiftdgdnvtmnpefgLFLTMNPGYAGRqELPENLkINFRSVAMMVPDRQIIIRVKLASCGFIdnvvlARKFFTLY 167
Cdd:COG5245 1690 TK------------------FFLQMNYGYKPR-ELTRSL-RAIFGYAETRIDTPDVSLIIDWYCEAI-----REKIDRLV 1744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 168 KLCEEQLSKQVHYDFGLRNILSVLRTLGAakranpmdtESTIVMRVLRDMNLSKLIDEDEPLFLSLIEDLFPNilldkaG 247
Cdd:COG5245 1745 QQKESSTSRQDLYDFGLRAIREMIAGHIG---------EAEITFSMILFFGMACLLKKDLAVFVEEVRKIFGS------S 1809
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 248 YPELEAAISRQVEEAGLINHPpwKLKVIQLfetqrvrHGMMtLGPSGAGKTtcihTLMRAMtdCGKPHREMRmnpkaita 327
Cdd:COG5245 1810 HLDVEAVAYKDALLHILRSRR--GLLVVGG-------HGVL-KGVLIRGAC----DAREFV--CWLNPRNMR-------- 1865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 328 pQMFGRLDVATNDWTDGIFSTLWRKTLraKKGEHIWIILDG-PVDAIWIENLNSVLDDNKTLTLANG-DRIPMAPNCKII 405
Cdd:COG5245 1866 -EIFGHRDELTGDFRDSLKVQDLRRNI--HGGRECLFIFESiPVESSFLEDFNPLLDNNRFLCLFSGnERIRIPENLRFV 1942
|
410 420
....*....|....*....|..
gi 2462601207 406 FEPHNIDNASPATVSRNGMVFM 427
Cdd:COG5245 1943 FESTSLEKDTEATLTRVFLVYM 1964
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
286-421 |
1.15e-09 |
|
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: 58.84 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 286 GMMTLGPSGAGKTTCIHTLMRAMTDCGKphrEMRMNPKAITAPQMFGRLDVATND--WTDGIFstlwrkTLRAKKGehiW 363
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPV---FYVQLTRDTTEEDLFGRRNIDPGGasWVDGPL------VRAAREG---E 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462601207 364 IILDGPVDAI---WIENLNSVLDDNKTLTLANGDRIPMAPNC-KIIFEPHNID----NASPATVSR 421
Cdd:pfam07728 69 IAVLDEINRAnpdVLNSLLSLLDERRLLLPDGGELVKAAPDGfRLIATMNPLDrglnELSPALRSR 134
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
1208-1329 |
3.61e-07 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 52.65 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1208 LSFIQGYKFIYGEKHVEvRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQA-----AE 1282
Cdd:PRK07352 29 LAIVIGLLYYFGRGFLG-KILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAiraeiEK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462601207 1283 KVKAEVQKVKDRAQAIVDSiSKDKAIAEEKLEAAKPALEEAEAALQT 1329
Cdd:PRK07352 108 QAIEDMARLKQTAAADLSA-EQERVIAQLRREAAELAIAKAESQLPG 153
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1225-1346 |
7.16e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1225 VRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVandkadmvlkevtmKAQAAEKVKAEVQKVKDRAQAIVDSISK 1304
Cdd:COG3883 124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEA--------------LKAELEAAKAELEAQQAEQEALLAQLSA 189
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2462601207 1305 DKAIAEEKLEAAKPALEEAEAALQTIRPSDIATVRTLGRPPH 1346
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1237-1326 |
1.80e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 49.46 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1237 EKLKEASESVAALSKELEAKEKELQVANDKADmvlKEVTMKAQAAEKVKAEVQKVKDRAQAivdsisKDKAIAEEKLeAA 1316
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE---EEAKAKAAAEAKKKAEEAKKKAEAEA------KAKAEAEAKA-KA 191
|
90
....*....|
gi 2462601207 1317 KPALEEAEAA 1326
Cdd:TIGR02794 192 EEAKAKAEAA 201
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1220-1553 |
4.39e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1220 EKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRaqaiV 1299
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER----I 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1300 DSISKDKAIAEEKLEAAKPALEEAEAALQTIRpSDIATVRTlgrpphLIMRIMDCVLLL------FQRKVSAVKIDL-EK 1372
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAE-AEIEELEA------QIEQLKEELKALrealdeLRAELTLLNEEAaNL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1373 SCTMPSWQESLKLmtAGNFLQNLQQFPKDtiNEEVIEFLSPYFEMPDYNIETAKRvcgnvaGLCSWTKAMASFFSINKEV 1452
Cdd:TIGR02168 823 RERLESLERRIAA--TERRLEDLEEQIEE--LSEDIESLAAEIEELEELIEELES------ELEALLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1453 LPLKANLVVQENRHLLAMQDLQKAQAELDDKQAELDVVQAEYEQ-AMTEKQTLLEDAERcrhKMQTASTLISGLAGEKER 1531
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVrIDNLQERLSEEYSL---TLEEAEALENKIEDDEEE 969
|
330 340
....*....|....*....|..
gi 2462601207 1532 WTEQSQEFAAQTKRLvGDVLLA 1553
Cdd:TIGR02168 970 ARRRLKRLENKIKEL-GPVNLA 990
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1224-1510 |
5.87e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1224 EVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSIS 1303
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1304 KDKAiAEEKLEAAKPALEEAEAALQTIRPSDIATVRTLGRPphlIMRImdcvlllfQRKVSAVKIDLEKSCTMPSWQESL 1383
Cdd:COG4372 119 ELQK-ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ---LESL--------QEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1384 KLMTAGNFLQNLQQFPKDTINEEVIEFLSPYFEMPDYNIETAKRVCGNVAGLcswtkamasffsINKEVLPLKANLVVQE 1463
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL------------LDALELEEDKEELLEE 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2462601207 1464 NRHLLAMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDAER 1510
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALL 301
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1236-1555 |
8.35e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 8.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1236 LEKLKEASESVAALSKELEAKEKELQVANDKADMV-----------LKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSISK 1304
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELleqlslateeeLQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1305 DKAIAEEKLEAAKPA--LEEAE---------AALQTIRPSDIATVRTLGRPPHLIMRIMdCVLLLFQRKVSAVKIDLEKS 1373
Cdd:COG4717 228 ELEQLENELEAAALEerLKEARlllliaaalLALLGLGGSLLSLILTIAGVLFLVLGLL-ALLFLLLAREKASLGKEAEE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1374 CTMPSWQESLKLMTAGNFLQNLqQFPKDTINEEVIEFLSpyfempdyNIETAKRVCGNVAGLcswtkamasffsiNKEvl 1453
Cdd:COG4717 307 LQALPALEELEEEELEELLAAL-GLPPDLSPEELLELLD--------RIEELQELLREAEEL-------------EEE-- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1454 pLKANLVVQENRHLLAMQD---------LQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLE--DAERCRHKMQTASTLI 1522
Cdd:COG4717 363 -LQLEELEQEIAALLAEAGvedeeelraALEQAEEYQELKEELEELEEQLEELLGELEELLEalDEEELEEELEELEEEL 441
|
330 340 350
....*....|....*....|....*....|...
gi 2462601207 1523 SGLAGEKERWTEQSQEFAAQTKRLVGDVLLATA 1555
Cdd:COG4717 442 EELEEELEELREELAELEAELEQLEEDGELAEL 474
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1214-1328 |
9.31e-05 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 44.35 E-value: 9.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1214 YKFIYgeKHVeVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKE-----VTMKAQAAEKVKAEV 1288
Cdd:cd06503 17 KKFLW--KPI-LKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEarkeaEKIKEEILAEAKEEA 93
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2462601207 1289 QKVKDRAQAIVDSiSKDKAIAEEKLEAAKPALEEAEAALQ 1328
Cdd:cd06503 94 ERILEQAKAEIEQ-EKEKALAELRKEVADLAVEAAEKILG 132
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1238-1325 |
1.06e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.15 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1238 KLKEAsesvAALSKELEAKEKELQVANDKADMVLK----EVTMKAQAAEKVKAEVQKVKDRAqaivdsiSKDKAIAE--E 1311
Cdd:TIGR02794 143 KAKEE----AAKQAEEEAKAKAAAEAKKKAEEAKKkaeaEAKAKAEAEAKAKAEEAKAKAEA-------AKAKAAAEaaA 211
|
90
....*....|....
gi 2462601207 1312 KLEAAKPALEEAEA 1325
Cdd:TIGR02794 212 KAEAEAAAAAAAEA 225
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1220-1331 |
1.25e-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: 46.07 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1220 EKHVEVRTLANRmntgLEKLKEASESVA------ALSKELEAKEKELQVANDKadmvLKEVTMKAQAAEKVKAEVQKVKD 1293
Cdd:COG1579 63 RLELEIEEVEAR----IKKYEEQLGNVRnnkeyeALQKEIESLKRRISDLEDE----ILELMERIEELEEELAELEAELA 134
|
90 100 110
....*....|....*....|....*....|....*...
gi 2462601207 1294 RAQAIVDSiskdkaiAEEKLEAAKPALEEAEAALQTIR 1331
Cdd:COG1579 135 ELEAELEE-------KKAELDEELAELEAELEELEAER 165
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1469-1542 |
1.39e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.39e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462601207 1469 AMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDAERcrhKMQTASTLISGLAGEKERWTEQSQEFAAQ 1542
Cdd:COG3883 134 LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA---QQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1238-1326 |
1.53e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1238 KLKEASES--VAALSK--ELEAKEKELQVANDKADMVLKEvtmKAQAAEKVKAEV---QKVKDRAQAIVDSISKDKAIAE 1310
Cdd:PRK09510 146 KAKAEAEAkrAAAAAKkaAAEAKKKAEAEAAKKAAAEAKK---KAEAEAAAKAAAeakKKAEAEAKKKAAAEAKKKAAAE 222
|
90
....*....|....*.
gi 2462601207 1311 EKLEAAKPALEEAEAA 1326
Cdd:PRK09510 223 AKAAAAKAAAEAKAAA 238
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1238-1326 |
3.42e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.57 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1238 KLKEASESVAALSKEL--EAKEKELQVANDKAD---MVLKEVTMKAQAAEKVKAEVQ---KVKDRAQAIVDSISKDKAIA 1309
Cdd:PRK09510 118 KQAEEAAKQAALKQKQaeEAAAKAAAAAKAKAEaeaKRAAAAAKKAAAEAKKKAEAEaakKAAAEAKKKAEAEAAAKAAA 197
|
90
....*....|....*..
gi 2462601207 1310 EEKLEAAKPALEEAEAA 1326
Cdd:PRK09510 198 EAKKKAEAEAKKKAAAE 214
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1237-1326 |
3.56e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 45.79 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1237 EKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSISKDKAIAEEKLEAA 1316
Cdd:pfam05701 370 AKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAI 449
|
90
....*....|
gi 2462601207 1317 KpALEEAEAA 1326
Cdd:pfam05701 450 K-ALQESESS 458
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1223-1330 |
4.93e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 44.33 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1223 VEVRTLANRMNTGLEKLKEASESVA-ALSKELEAKEKELQVANDkadmVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDS 1301
Cdd:pfam06008 151 KAAQDLLSRIQTWFQSPQEENKALAnALRDSLAEYEAKLSDLRE----LLREAAAKTRDANRLNLANQANLREFQRKKEE 226
|
90 100
....*....|....*....|....*....
gi 2462601207 1302 ISKDKAIAEEKLEAAKPALEEAEAALQTI 1330
Cdd:pfam06008 227 VSEQKNQLEETLKTARDSLDAANLLLQEI 255
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1214-1328 |
5.32e-04 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 42.85 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1214 YKFIYgeKHVeVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVT-----MKAQAAEKVKAEV 1288
Cdd:COG0711 18 KKFAW--PPI-LKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARkeaeaIAEEAKAEAEAEA 94
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2462601207 1289 QKVKDRAQAIVDSIsKDKAIAEEKLEAAKPALEEAEAALQ 1328
Cdd:COG0711 95 ERIIAQAEAEIEQE-RAKALAELRAEVADLAVAIAEKILG 133
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
615-753 |
7.47e-04 |
|
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: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 615 VLLIGEQGTAKTVIIKGFMSKYDP-ECHMIkslNFSSATTP--LMFQRTIESYVDKRMGTTYGPPAGKKMTVFIDDVNMP 691
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNrPVFYV---QLTRDTTEedLFGRRNIDPGGASWVDGPLVRAAREGEIAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462601207 692 ---IINEWgDQVTNEIVRQLMEqNGFYNLEKPGEFtsivdiQFLAAMIHPGGGRNDIPQRLKRQF 753
Cdd:pfam07728 79 npdVLNSL-LSLLDERRLLLPD-GGELVKAAPDGF------RLIATMNPLDRGLNELSPALRSRF 135
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1236-1325 |
8.54e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.41 E-value: 8.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1236 LEKLKEASES----VAALSKELEAKEKELQVANDKADmvlKEVTMKAQAAEKVKAEVQ---KVKDRAQAIVDSISKDKAI 1308
Cdd:PRK09510 128 ALKQKQAEEAaakaAAAAKAKAEAEAKRAAAAAKKAA---AEAKKKAEAEAAKKAAAEakkKAEAEAAAKAAAEAKKKAE 204
|
90
....*....|....*..
gi 2462601207 1309 AEEKLEAAKPALEEAEA 1325
Cdd:PRK09510 205 AEAKKKAAAEAKKKAAA 221
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1220-1331 |
9.79e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 9.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1220 EKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDR--AQA 1297
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeYEA 93
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462601207 1298 I---VDSISKDKAIAEEKLEAAKPALEEAEAALQTIR 1331
Cdd:COG1579 94 LqkeIESLKRRISDLEDEILELMERIEELEEELAELE 130
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1214-1329 |
1.01e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1214 YKFIYGE-KHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKadmvLKEVTMKAQAAEKVKAEVQKVK 1292
Cdd:TIGR02168 215 YKELKAElRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK----LEELRLEVSELEEEIEELQKEL 290
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462601207 1293 DRAQAIVDSISKDKAIAEEKLEAAKPALEEAEAALQT 1329
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1241-1331 |
1.26e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1241 EASESVAALSKELEAKEKELQVANDKADMVLKEvtmkaqaAEKVKAEVQKVKDRAQAIVDS-ISKDKAIAEEKLEAAKpa 1319
Cdd:PRK00409 513 EDKEKLNELIASLEELERELEQKAEEAEALLKE-------AEKLKEELEEKKEKLQEEEDKlLEEAEKEAQQAIKEAK-- 583
|
90
....*....|..
gi 2462601207 1320 lEEAEAALQTIR 1331
Cdd:PRK00409 584 -KEADEIIKELR 594
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1224-1327 |
1.71e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1224 EVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKdraqaivdsis 1303
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE----------- 764
|
90 100
....*....|....*....|....
gi 2462601207 1304 KDKAIAEEKLEAAKPALEEAEAAL 1327
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARL 788
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
1236-1325 |
1.80e-03 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 40.26 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1236 LEKLKEASESVAALSKELEAKEKELqvandkadmvlKEVTMKAQAAEKvkaEVQKVKDRaqaivdsISKDKAIAEEKLEA 1315
Cdd:pfam18595 49 LAKLEEAKKKLKELRDALEEKEIEL-----------RELERREERLQR---QLENAQEK-------LERLREQAEEKREA 107
|
90
....*....|
gi 2462601207 1316 AKPALEEAEA 1325
Cdd:pfam18595 108 AQARLEELRE 117
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
9-127 |
2.10e-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: 40.74 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 9 GPAGTGKTETTKDMGRCLGKY-VVVFNCSDQM---DFRGlGRIFKGL------------AQSGSWGCFDEFNRIDlpvLS 72
Cdd:pfam07728 6 GPPGTGKTELAERLAAALSNRpVFYVQLTRDTteeDLFG-RRNIDPGgaswvdgplvraAREGEIAVLDEINRAN---PD 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462601207 73 VAAQQISIIltckkEHKKsFIFTDGDNVTM--NPEFGLFLTMNPGYAGRQELPENLK 127
Cdd:pfam07728 82 VLNSLLSLL-----DERR-LLLPDGGELVKaaPDGFRLIATMNPLDRGLNELSPALR 132
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1224-1330 |
2.33e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1224 EVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLK------------EVTMKAQ----AAEKVKAe 1287
Cdd:COG3883 45 ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARalyrsggsvsylDVLLGSEsfsdFLDRLSA- 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1288 VQKVKDRAQAIVDSISKDKAI-------AEEKLEAAKPALEEAEAALQTI 1330
Cdd:COG3883 124 LSKIADADADLLEELKADKAEleakkaeLEAKLAELEALKAELEAAKAEL 173
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1236-1329 |
2.48e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 40.31 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1236 LEKLKEASESVAALSKELEAKEKELQVANDKADmvlKEVTMKAQAAE---KVKAEVQKVKDRAQAivdsiskdkaiAEEK 1312
Cdd:pfam07926 14 KEEAADAEAQLQKLQEDLEKQAEIAREAQQNYE---RELVLHAEDIKalqALREELNELKAEIAE-----------LKAE 79
|
90
....*....|....*..
gi 2462601207 1313 LEAAKPALEEAEAALQT 1329
Cdd:pfam07926 80 AESAKAELEESEESWEE 96
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1224-1326 |
2.49e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1224 EVRTLANRMNTgLEKLKEASES---VAALSKELEAKEKELQvANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVD 1300
Cdd:COG4913 639 ELDALQERREA-LQRLAEYSWDeidVASAEREIAELEAELE-RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIG 716
|
90 100
....*....|....*....|....*.
gi 2462601207 1301 SISKDKAIAEEKLEAAKPALEEAEAA 1326
Cdd:COG4913 717 RLEKELEQAEEELDELQDRLEAAEDL 742
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1245-1329 |
3.49e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 42.41 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1245 SVAALSKELEAKEKEL---QVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAI--------VDSISKDKAIAEEKL 1313
Cdd:TIGR04320 255 SLAALQAKLATAQADLaaaQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQalqtaqnnLATAQAALANAEARL 334
|
90
....*....|....*.
gi 2462601207 1314 EAAKPALEEAEAALQT 1329
Cdd:TIGR04320 335 AKAKEALANLNADLAK 350
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1236-1340 |
3.73e-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: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1236 LEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSISK-DKAIAEEKLE 1314
Cdd:COG4913 677 LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLRALLEERFA 756
|
90 100
....*....|....*....|....*.
gi 2462601207 1315 AAkpALEEAEAALQTIRPSDIATVRT 1340
Cdd:COG4913 757 AA--LGDAVERELRENLEERIDALRA 780
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1220-1331 |
5.44e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1220 EKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDK---ADMVLKEVTMKAQAAEKVKAEVQKVKDRAQ 1296
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERrreLEERLEELEEELAELEEELEELEEELEELE 343
|
90 100 110
....*....|....*....|....*....|....*
gi 2462601207 1297 AIVDSISKDKAIAEEKLEAAKPALEEAEAALQTIR 1331
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1214-1328 |
6.83e-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: 41.97 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1214 YKFIYGEKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQ-VANDKADMV---------LKEVTMKAQAAEK 1283
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYaLANEISRLEqqkqilrerLANLERQLEELEA 323
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2462601207 1284 VKAEVQKVKDRAQAIVDSISKDKAIAEEKLEAAKPALEEAEAALQ 1328
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1440-1546 |
7.06e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601207 1440 KAMASFFSINKEVLPLKANLVVQENRHLLAMQDLQK----AQAELDDKQAELDVVQAEYEQAMTEKQTLLEDAERCRHKM 1515
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEeleqLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110
....*....|....*....|....*....|.
gi 2462601207 1516 QTASTLISGLAGEKERWTEQSQEFAAQTKRL 1546
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
|
| |
