|
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 |
5.37e-171 |
|
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: 529.75 E-value: 5.37e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1651 YTYEYQGNAPKLVYTPLTDKCYLTLTQAMKMGLGGNPYGPAGTGKTESVKALGGLLGRQVLVFNCDEGIDVKSMGRIFVG 1730
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1731 LVKCGAWGCFDEFNRLEEAVLSAVSMQIQTIQDALKNHRTVCELLGKEVEINANSGIFITMNPagkGYGGRQKLPDNLKQ 1810
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNP---GYAGRTELPDNLKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1811 LFRPVAMSRPDNDLIAEVILYSEGFKDAKELGRKLVAIFNLSRELLTPQQHYDWGLRALKTVLRGSGNllrqLKKNStkQ 1890
Cdd:pfam12774 158 LFRPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGS----LKRSN--P 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1891 DVNENHIVVQALRLNTMSKFTFADCTRFDALIKDVFPGIDFKEVEYDELSSALKQVFEEANYEVIPNQMKKALELYEQLR 1970
Cdd:pfam12774 232 NLNEDVLLLRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETML 311
|
330
....*....|....*.
gi 1720430018 1971 QRTGVVIVGPSGAGKS 1986
Cdd:pfam12774 312 VRHGVMLVGPTGSGKT 327
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1361-4022 |
3.12e-163 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 571.16 E-value: 3.12e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1361 LPKEQTRFNKVDEDFRsiMMDIRKDSRVTTLTT-HAGIRNTLLTILDQLQRCQKSLNEFLEEKRSAFPRFyfIGDDDLLE 1439
Cdd:COG5245 644 IPHAVHRKMSLVSGVR--GIYKRVVSGCEAINTiLEDVGDDLDLFYKEMDQVFMSIEKVLGLRWREVERA--SEVEELMD 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1440 ILGQSTNPSVIQSHLKKLFAGINSVCFDEEskHITAMKSLEGEVVPFKSKVLLSNNVEA--WLNDlalEMKQTLKQLLKE 1517
Cdd:COG5245 720 RVRELENRVYSYRFFVKKIAKEEMKTVFSS--RIQKKEPFSLDSEAYVGFFRLYEKSIVirGINR---SMGRVLSQYLES 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1518 CVTAGRSSQGAIDPSLFPSQILCLAEQiKFTEDVENAIkdhslhqiEAQLVaklERYTSVDTSSEDPGNSESGILELKLK 1597
Cdd:COG5245 795 VQEALEIEDGSFFVSRHRVRDGGLEKG-RGCDAWENCF--------DPPLS---EYFRILEKIFPSEEGYFFDEVLKRLD 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1598 ALILDIIHNIDIVKQLNQVQVHTTDDWAWKKQVRFYMKSDHTCYVQMVDSELQYTYEYQGNAPKLVYTPLTDKCYLTLTQ 1677
Cdd:COG5245 863 PGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMDTSQHQKLFE 942
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1678 AMKMGLGGNpygpAGTGKTESVKALGGLLGRQVlvfncdEGIDVKSmgRIFVGLVKCGAWGcFDEFNRLEEAVLsAVSMQ 1757
Cdd:COG5245 943 AVCDEVCRF----VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISR-TILVD 1008
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1758 IQTIQDALKNHRTVCELLGKEVEINANSGIFITMNPagkgyggRQKLPDNLKQLFRPVAMSRPDNdLIAEVilysegfkd 1837
Cdd:COG5245 1009 EYLNSDEFRMLEELNSAVVEHGLKSPSTPVEMIINE-------RNIVLEIGRRALDMFLSNIPFG-AIKSR--------- 1071
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1838 AKELGRKLVAIFNLSRELLTPQQHYDWglRALKTVLRGSGNLLRQLKKNSTKqdvnenhiVVQALRLNTMSkftfadctr 1917
Cdd:COG5245 1072 RESLDREIGAFNNEVDGIAREEDELMF--YPMFKSLKAKHRMLEEKTEYLNK--------ILSITGLPLIS--------- 1132
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1918 fDALIKDvfpgIDFKEVEYDELSS-ALKQVFEEANyEVIPNQMKKALELYEQLRQRTGVVIVGPSGAGKSTLWRmlrAAL 1996
Cdd:COG5245 1133 -DTLRER----IDTLDAEWDSFCRiSESLKKYESQ-QVSGLDVAQFVSFLRSVDTGAFHAEYFRVFLCKIKHYT---DAC 1203
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1997 CKIGKVVKQYTMNPKAMPRHQLLGHIDMDTREWSDGVLTNSARQVVREpqdvsswiicdgdidpEWIESLNSVLDDNRLL 2076
Cdd:COG5245 1204 DYLWHVKSPYVKKKYFDADMELRQFFLMFNREDMEARLADSKMEYEVE----------------RYVEKTKAEVSSLKLE 1267
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2077 TMPSGERiqfgpnvNFVFETHDlscASPATISRMGMIFLSDEETDLNSLIKSWL--RNQPLEyrSNLENWIGDYFSK--- 2151
Cdd:COG5245 1268 LSSVGEG-------QVVVSNLG---SIGDKVGRCLVEYDSISRLSTKGVFLDELgdTKRYLD--ECLDFFSCFEEVQkei 1335
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2152 -ALQWVLKQNDYVVETSLVGTVmnGLSHLHGCKYHDQFIINLI---RGLGGNLNMKSRLEFTKEVFN----WA------R 2217
Cdd:COG5245 1336 dELSMVFCADALRFSADLYHIV--KERRFSGVLAGSDASESLGgksIELAAILEHKDLIVEMKRGINdvlkLRifgdkcR 1413
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2218 ETPPDSHRPMDTYYDCDRGQLASY--MLKKPESLTADDFSNGHI-----------LP---VIQTPDMQRGLDYFKPWLSs 2281
Cdd:COG5245 1414 ESTPRFYLISDGDLIKDLNERSDYeeMLIMMFNISAVITNNGSIagfelrgervmLRkevVIPTSDTGFVDSFSNEALN- 1492
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2282 dTKQPFILVGPEGCGKGMLLRYAFSQLRSTEIATIHCSAQTTSRHLLQKLSQTcMVISTNTG--RVYRPKDCERLVLYLK 2359
Cdd:COG5245 1493 -TLRSYIYCGPPGSGKEMLMCPSLRSELITEVKYFNFSTCTMTPSKLSVLERE-TEYYPNTGvvRLYPKPVVKDLVLFCD 1570
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2360 DINLPKLDKWGTSTLVAFLQQVLTYQGFYDE-NLEWVGLENIQIVASMSAGGRLGRHKLTTRFTSIVRLCAIDYPEREQL 2438
Cdd:COG5245 1571 EINLPYGFEYYPPTVIVFLRPLVERQGFWSSiAVSWVTICGIILYGACNPGTDEGRVKYYERFIRKPVFVFCCYPELASL 1650
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2439 QTIYGAYLEAVLHKNLKNHSIwgssskIYLLAGSMVQVYEQVRAKFTVDEYSHYFFTPCILTQWVLGLFRYDLEGgsSNH 2518
Cdd:COG5245 1651 RNIYEAVLMGSYLCFDEFNRL------SEETMSASVELYLSSKDKTKFFLQMNYGYKPRELTRSLRAIFGYAETR--IDT 1722
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2519 PLDYVLEIVAYEARRLFRDKIVGVKELHLFDNILTSVLQGDWGSDILDNMADSFYVTWGAHHVSggktapgqplpphgkp 2598
Cdd:COG5245 1723 PDVSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREMIAGHIGEAEITFSMILFFG---------------- 1786
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2599 LGKLTSADLKDVIKKGLIHYGRDNQNLDILLFQEVLEYMSRIDRVLSFPGGSLLLAGRSGVGRRTVTSLVSHMHGAVLFS 2678
Cdd:COG5245 1787 MACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMRE 1866
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2679 PKISRGYEPKQFRNDLKHVLQLAGIEAQQVVLLLEDYQFVHPTFLEMINSLLASGEVPGLYTLEELEPLLLPLKDQASQD 2758
Cdd:COG5245 1867 IFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFEST 1946
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2759 GFF----GPVFNYFTYRIQQNLHIVL-IMDSANLNFIVNCESnPALHKKCQVLWMEGWSDSSMKKIPEMLFSET--DGEE 2831
Cdd:COG5245 1947 SLEkdteATLTRVFLVYMEENLPVVFsACCSQDTSVLAGIRS-PALKNRCFIDFKKLWDTEEMSQYANSVETLSrdGGRV 2025
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2832 KYEKKRKDEKKRNSVDPDFIKSFLLIHES-------CKAYGATPSRYMTFLHVYSAISSSKKKELLKRQSHLQAGVSKLN 2904
Cdd:COG5245 2026 FFINGELGVGKGALISEVFGDDAVVIEGRgfeismiEGSLGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYN 2105
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2905 EAKALVDELNRKAGEQSILLRIKQDEADSALQEITVSMQDASEQKTELERLKQRIAEEVVKIEERKSKIDDELKEVQPLV 2984
Cdd:COG5245 2106 EYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAV 2185
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2985 NEAKLAVGNIRPESLSEIRSLRMPPDVIRDILEGVLRLMGIFDTSWVSMKSFLAKRGVREDIATFD-ARNIPKEIRESVE 3063
Cdd:COG5245 2186 LEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLLGFEAKIWFGEQQSLRRDDFIRIIGKYPdEIEFDLEARRFRE 2265
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3064 ELLFKNkASFDPKNAKRASTAAAPLAAWVKANVQYSHVLERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSEL 3143
Cdd:COG5245 2266 ARECSD-PSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRR 2344
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3144 KEKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLDREHRRWNAQVAEIAEELATLPKRAQLAAAFITYLSAAPEGLR-- 3221
Cdd:COG5245 2345 RSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRai 2424
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3222 -KNCLEEWTKAAGLEKFDLRRFLCTESEQLIWKSEGLP-SDDLSIENALVIlqiiglKSWSRVCPFLIDPSSQATEWLKT 3299
Cdd:COG5245 2425 eFGMSFIRISKEFRDKEIRRRQFITEGVQKIEDFKEEAcSTDYGLENSRIR------KDLQDLTAVLNDPSSKIVTSQRQ 2498
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3300 HLKDSHLEVINQQDSNFITALELAVRFGKTLIIQEMDGVEPVLYPLLRRDLVAQGPRYVVQIGDKIIDYNEDFRLFLSTR 3379
Cdd:COG5245 2499 MYDEKKAILGSFREMEFAFGLSQARREGSDKIIGDAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSE 2578
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3380 NPNPFIPPDAASIVTEVNFTTTRSGLRGQLLALTIQHEKPDLEEQKTKLLQQEEDKKIQLARLEESLLETLATSQGNILE 3459
Cdd:COG5245 2579 GRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQ 2658
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3460 NKDLIESLNQTKASSALIQDSLKESYKLQISLDQERDAYLPLAESASKMYFIISDLSKINNMYRFSLASFLRLFQRALqn 3539
Cdd:COG5245 2659 TDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFEKWR-- 2736
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3540 kqdseNTEERIQCLVNSLKHMVYEYI---CRCLF----------KADQLMFALHFVRGMHPELfqENEWDTFTGVVVgdm 3606
Cdd:COG5245 2737 -----RMKSKYLCAIRYMLMSSEWILdheDRSGFihrldvsfllRTKRFVSTLLEDKNYRQVL--SSCSLYGNDVIS--- 2806
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3607 lrkaDSQQRI-RDQLPSWIDQERSWAVATLKislpsLYQTLCLEDGAFWRTYYHHSMCEQEFPSILAKkvslFQQvlvvq 3685
Cdd:COG5245 2807 ----HSCDRFdRDVYRALKHQMDNRTHSTIL-----TSNSKTNPYKEYTYNDSWAEAFEVEDSGDLYK----FEE----- 2868
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3686 alrpdrlqsamalfackalGLKELSPLPLNLKRLYKETLEIEPIliiispgadpsqeLQELASAERSSecyhqvamgqgq 3765
Cdd:COG5245 2869 -------------------GLLELIVGHAPLIYAHKKSLENERN-------------VDRLGSKENEV------------ 2904
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3766 adLAIQMLKECARNGDWLCLKNLHLVVSWL-----PVLEKELNTLQPKDSFRLWLTAEVHPNFTPILLQSSLKITYESPP 3840
Cdd:COG5245 2905 --YAVLNSLFSRKEKSWFEVYNISLSFGWFkryveDVVYPIKASRVCGKVKNMWTSMVDADMLPIQLLIAIDSFVSSTYP 2982
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3841 GLKKNLMRTYES-WTPEQISKrdnIHRAHALFSLAWFHAACQERRNYIPQGWTKFYEFSLSDLRAGYHVIDRLF--DGTK 3917
Cdd:COG5245 2983 ETGCGYADLVEIdRYPFDYTL---VIACDDAFYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNILflNHLN 3059
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3918 DVQWEFVHGLLENSIYGGRVDNYFDLRVLQSYLKQFF----NSSIID--VLNQRNKKSIFPYSISLpnSCSILdyraVIE 3991
Cdd:COG5245 3060 ARKWGNNRDLIFTIVYGKKHSLMEDSKVVDKYCRGYGahetSSQILAsvPGGDPELVKFHMEEMCR--SSAFG----VIG 3133
|
2730 2740 2750
....*....|....*....|....*....|.
gi 1720430018 3992 KLPEDDKPSFFGLPANIARSSQRMISSQVIS 4022
Cdd:COG5245 3134 QLPDLALCAWLMGPCDSEYLKAIVYSSRIDM 3164
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1120-1518 |
1.21e-126 |
|
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: 405.87 E-value: 1.21e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1120 ISKDIESCAQIWALYEEFQQGLQDMAKEDWITyrAKIYLFEEFLINWHERLRKIE---EHSVMTVKLQSEVDRYKMIIPI 1196
Cdd:pfam08393 4 IKKELEPLKKLWDLVSEWQESLEEWKNGPFSD--LDVEELEEELEEFLKELKKLPkelRDWDVAEELKKKIDDFKKSLPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1197 LKYVRGEHLSPDHWLDLFRLLGLPRGTSLEKLLFGDLLRVadTIVEKASELKDLNSRAQGEVTIREALRELDLWGVGAVF 1276
Cdd:pfam08393 82 IEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDL--NLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1277 SLIDYEDSqnhTIKLIKDWKDIVNQVGDNRCLLQSLKDSPYYKGFEDKVSIWERKLAQLDEYLQNLNHIQRKWVYLEPIF 1356
Cdd:pfam08393 160 ELVPYKDT---GTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1357 G----RGALPKEQTRFNKVDEDFRSIMMDIRKDSRVTTLTTHAGIRNTLLTILDQLQRCQKSLNEFLEEKRSAFPRFYFI 1432
Cdd:pfam08393 237 SsediRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1433 GDDDLLEILGQSTNPSVIQSHLKKLFAGINSVCFDeESKHITAMKSLEGEVVPF-KSKVLLSNNVEAWLNDLALEMKQTL 1511
Cdd:pfam08393 317 SNDELLEILSQTKDPTRVQPHLKKCFEGIASLEFD-ENKEITGMISKEGEVVPFsKPPVEAKGNVEEWLNELEEEMRETL 395
|
....*..
gi 1720430018 1512 KQLLKEC 1518
Cdd:pfam08393 396 RDLLKEA 402
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3252-3477 |
3.93e-94 |
|
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: 304.75 E-value: 3.93e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3252 WKSEGLPSDDLSIENALVILQiiglkswSRVCPFLIDPSSQATEWLKTHLKDSHLEVINQQDSNFITALELAVRFGKTLI 3331
Cdd:pfam12781 3 WNIQGLPNDELSIENAIIVTN-------SRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3332 IQEM-DGVEPVLYPLLRRDLVAQGPRYVVQIGDKIIDYNEDFRLFLSTRNPNPFIPPDAASIVTEVNFTTTRSGLRGQLL 3410
Cdd:pfam12781 76 IEDVgEELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720430018 3411 ALTIQHEKPDLEEQKTKLLQQEEDKKIQLARLEESLLETLATSQGNILENKDLIESLNQTKASSALI 3477
Cdd:pfam12781 156 GIVVKKERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4017-4310 |
1.27e-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: 1.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 4017 SSQVISQLRILGRSVTAGCKFDREiwSNElSPVLNLWKKLNQ---NSNLIHQKVSPPNDRQGSPILSFIILEQFNAIRLV 4093
Cdd:pfam18199 4 TNELLSTLLSLQPRSDSGGGGGGS--SRE-EIVLELAKDILEklpEPFDIEEAEEKYPVGYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 4094 QSVHQSLAALSKVIRGTTLLSSEVQKLASALLNQKCPLTWQSRWEGPEDPL-QYLRGLVARTLAIQNWVEKAEKQVllad 4172
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLgSWIRDLLERLKQLQDWLDDEGPPK---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 4173 TLDLSELFHPDTFLNALRQETARATGCSVDSLKFVASWKGRLQEAKLQIK------ISGLLLEGCSFDG--NRLSEnQHD 4244
Cdd:pfam18199 157 VFWLSGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTKKVSPEEVTEPpedgvyVHGLFLEGARWDRknGCLVE-SEP 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720430018 4245 SPSVSSVLPCYMgwTPQGSYGPYSPDECISLPVYTSAERER--VVTNIDVPCGGNQDQWIQCGAALFL 4310
Cdd:pfam18199 236 KELFSPLPVIHL--KPVESDKKKLDENTYECPVYKTSERHStnFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
161-674 |
7.03e-22 |
|
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: 103.43 E-value: 7.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 161 LKEDDTRGILTPSDEFQFWIEQA--------HRGSKQISK-----ERA--SY---FKELFE-----------------TI 205
Cdd:pfam08385 19 LKEDSQGRNPGPLAEIEFWKSREanlssiyeQLKSPEVKKvleilEAAksSYlpaFKALDTeltdalneakdnvkylkTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 206 SREFYNLDSL-SLLEVVDLVETTRDVVDDVWRQTEHdhYPES-RMLHLLDVIGGSFGRFVQKKLGSLKLWEDPYYLVKEN 283
Cdd:pfam08385 99 ERPFEDLEELtDPPEIIEAIPPLMNTIRLIWSISRY--YNTSeRMTVLLEKISNQLIEQCKKYLSPEGIFDGDVEEALEK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 284 LKAGISICEQWVIVCSHLTGQVWQRYVPHPWK-SGKYFPETLDKLGKRLEEVLAIRTIHEKLLYFLPASEERIVCLSRVF 362
Cdd:pfam08385 177 LQECIELLEAWKEEYKKTREKLEESPRERPWDfSERYIFGRFDAFLERLEKILELFETIEQFSKLEKIGGTKGPELEGVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 363 EP--------FTGVNPVQYNP--YTEPLWKAAVSQYEKIIAPAEQKIAGKLKNYISEIQdSPQQLLQAFLKYKELVKRPT 432
Cdd:pfam08385 257 EEileefqeaYKVFKSKTYDIldVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDDAR-STESAFKLLRIFEFLLERPI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 433 ISKELMLERETLLARLGDSAKDFRLDFENRCRgipgDPSgpLSGKNLSEVVNNIVWVRQLELKVDDTIKIAEALLSDLSg 512
Cdd:pfam08385 336 IRGALEEKYTDLLQMFKKELDAVKKIFDKQKY----NPS--PIAKNMPPVAGAIIWARQLFRRIQEPMKRFKEELGLLK- 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 513 frsfHRSAEDLLDQF-------KLYEQEQFDDWSREVqsglsDSRSGLCIEANsrIMELDPNDGAL-KVHYSDRLVILLR 584
Cdd:pfam08385 409 ----HAEGKKVIKKYnelakklDEYERLIYEAWLKEV-----EEASEGNLKRP--LLVRHPETGKLlSVNFDPQLLALLR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 585 EVRQLSALGFVIPAKIQQVANVAQKFCKQAIILKQVAHFYNSIDQQMIQSQRPMMLQSALAFEQIIKNskagsgGKSQIT 664
Cdd:pfam08385 478 EVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEP------GLTTLT 551
|
570
....*....|
gi 1720430018 665 WDNpKELEGY 674
Cdd:pfam08385 552 WNS-LGIDEY 560
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2885-3237 |
6.25e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 6.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2885 KKKELLKRQSHLQAGVSKLNEAKALVDELNRkageqsillrIKQDEADSALQEITVSMQDASEQKTELErlkqriaEEVV 2964
Cdd:PRK03918 346 KLKELEKRLEELEERHELYEEAKAKKEELER----------LKKRLTGLTPEKLEKELEELEKAKEEIE-------EEIS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2965 KIEERKSKIDDELKEVQPLVNEAKLAVG---------------NIRPESLSEIRSLRMPPDVIRDILEGVLRLMgifdts 3029
Cdd:PRK03918 409 KITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKEL------ 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3030 wVSMKSFLAKRgvREDIATfdaRNIPKEIRESVEELlfknkASFDPKNAKrastaaaplaawvKANVQYSHVLERIQPLE 3109
Cdd:PRK03918 483 -RELEKVLKKE--SELIKL---KELAEQLKELEEKL-----KKYNLEELE-------------KKAEEYEKLKEKLIKLK 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3110 TEQSGLELNLKKTEDRKRKLEdllnsvgqkvsELKEKFQSRTSEAAKLEAEVSK-AQETIKAAEVLISQLDREHRRWNA- 3187
Cdd:PRK03918 539 GEIKSLKKELEKLEELKKKLA-----------ELEKKLDELEEELAELLKELEElGFESVEELEERLKELEPFYNEYLEl 607
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1720430018 3188 -----QVAEIAEELATLPKRAQLAAAFITYLSAAPEGLRKNcLEEWTKAAGLEKF 3237
Cdd:PRK03918 608 kdaekELEREEKELKKLEEELDKAFEELAETEKRLEELRKE-LEELEKKYSEEEY 661
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2883-3223 |
5.46e-07 |
|
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: 56.23 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2883 SSKKKELLKRQSHLQAGVSKLNEAKALVDELNRK-----AGEQsilLRIKQDeadsaLQEITVSMQDASEQKTELERLKQ 2957
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKikdlgEEEQ---LRVKEK-----IGELEAEIASLERSIAEKERELE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2958 RIAEEVVKIEERKSKIDDELKEVqplvnEAKLAVGNIRPESLSEIrslrmppdvirdilegvlrlmgifdtswvsmksFL 3037
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEEL-----EREIEEERKRRDKLTEE---------------------------------YA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3038 AKRGVREDIATfDARNIPKEIRESVEELlfknkasfdpknakrastaaaplaawVKANVQYSHVLERIQPLETEQSGLEL 3117
Cdd:TIGR02169 361 ELKEELEDLRA-ELEEVDKEFAETRDEL--------------------------KDYREKLEKLKREINELKRELDRLQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3118 NLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLDREHRRWNAQVAEIAEELA 3197
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
330 340
....*....|....*....|....*.
gi 1720430018 3198 TLPKRAQLAAAFITYLSAAPEGLRKN 3223
Cdd:TIGR02169 494 EAEAQARASEERVRGGRAVEEVLKAS 519
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
1937-1988 |
8.36e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 43.93 E-value: 8.36e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1720430018 1937 DELSSALKQVFEEANYEVIPNQMKKAL---ELYEQLRQRTgVVIVGPSGAGKSTL 1988
Cdd:cd01854 48 DEELEELLEIYEKLGYPVLAVSAKTGEgldELRELLKGKT-SVLVGQSGVGKSTL 101
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1944-1996 |
4.98e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 41.87 E-value: 4.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1720430018 1944 KQVFEEANYEVIPNQMkkalelyeqlrqrtgVVIVGPSGAGKSTLWRMLRAAL 1996
Cdd:COG2401 43 RYVLRDLNLEIEPGEI---------------VLIVGASGSGKSTLLRLLAGAL 80
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
2878-3006 |
8.09e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.54 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2878 YSAISSSKKKELLKRQSHLQagvSKLNEAKALVDELNRkageqsillrIKQDEADSALQEITVSMQDASEQKTELERLKQ 2957
Cdd:smart00787 166 ELELLNSIKPKLRDRKDALE---EELRQLKQLEDELED----------CDPTELDRAKEKLKKLLQEIMIKVKKLEELEE 232
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1720430018 2958 RIAEEVVKIEERKSKID---DELKEVQPLVNEaklavgnIRPESLSEIRSLR 3006
Cdd:smart00787 233 ELQELESKIEDLTNKKSelnTEIAEAEKKLEQ-------CRGFTFKEIEKLK 277
|
|
| |
|
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 |
5.37e-171 |
|
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: 529.75 E-value: 5.37e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1651 YTYEYQGNAPKLVYTPLTDKCYLTLTQAMKMGLGGNPYGPAGTGKTESVKALGGLLGRQVLVFNCDEGIDVKSMGRIFVG 1730
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1731 LVKCGAWGCFDEFNRLEEAVLSAVSMQIQTIQDALKNHRTVCELLGKEVEINANSGIFITMNPagkGYGGRQKLPDNLKQ 1810
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNP---GYAGRTELPDNLKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1811 LFRPVAMSRPDNDLIAEVILYSEGFKDAKELGRKLVAIFNLSRELLTPQQHYDWGLRALKTVLRGSGNllrqLKKNStkQ 1890
Cdd:pfam12774 158 LFRPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGS----LKRSN--P 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1891 DVNENHIVVQALRLNTMSKFTFADCTRFDALIKDVFPGIDFKEVEYDELSSALKQVFEEANYEVIPNQMKKALELYEQLR 1970
Cdd:pfam12774 232 NLNEDVLLLRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETML 311
|
330
....*....|....*.
gi 1720430018 1971 QRTGVVIVGPSGAGKS 1986
Cdd:pfam12774 312 VRHGVMLVGPTGSGKT 327
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1361-4022 |
3.12e-163 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 571.16 E-value: 3.12e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1361 LPKEQTRFNKVDEDFRsiMMDIRKDSRVTTLTT-HAGIRNTLLTILDQLQRCQKSLNEFLEEKRSAFPRFyfIGDDDLLE 1439
Cdd:COG5245 644 IPHAVHRKMSLVSGVR--GIYKRVVSGCEAINTiLEDVGDDLDLFYKEMDQVFMSIEKVLGLRWREVERA--SEVEELMD 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1440 ILGQSTNPSVIQSHLKKLFAGINSVCFDEEskHITAMKSLEGEVVPFKSKVLLSNNVEA--WLNDlalEMKQTLKQLLKE 1517
Cdd:COG5245 720 RVRELENRVYSYRFFVKKIAKEEMKTVFSS--RIQKKEPFSLDSEAYVGFFRLYEKSIVirGINR---SMGRVLSQYLES 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1518 CVTAGRSSQGAIDPSLFPSQILCLAEQiKFTEDVENAIkdhslhqiEAQLVaklERYTSVDTSSEDPGNSESGILELKLK 1597
Cdd:COG5245 795 VQEALEIEDGSFFVSRHRVRDGGLEKG-RGCDAWENCF--------DPPLS---EYFRILEKIFPSEEGYFFDEVLKRLD 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1598 ALILDIIHNIDIVKQLNQVQVHTTDDWAWKKQVRFYMKSDHTCYVQMVDSELQYTYEYQGNAPKLVYTPLTDKCYLTLTQ 1677
Cdd:COG5245 863 PGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMDTSQHQKLFE 942
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1678 AMKMGLGGNpygpAGTGKTESVKALGGLLGRQVlvfncdEGIDVKSmgRIFVGLVKCGAWGcFDEFNRLEEAVLsAVSMQ 1757
Cdd:COG5245 943 AVCDEVCRF----VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISR-TILVD 1008
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1758 IQTIQDALKNHRTVCELLGKEVEINANSGIFITMNPagkgyggRQKLPDNLKQLFRPVAMSRPDNdLIAEVilysegfkd 1837
Cdd:COG5245 1009 EYLNSDEFRMLEELNSAVVEHGLKSPSTPVEMIINE-------RNIVLEIGRRALDMFLSNIPFG-AIKSR--------- 1071
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1838 AKELGRKLVAIFNLSRELLTPQQHYDWglRALKTVLRGSGNLLRQLKKNSTKqdvnenhiVVQALRLNTMSkftfadctr 1917
Cdd:COG5245 1072 RESLDREIGAFNNEVDGIAREEDELMF--YPMFKSLKAKHRMLEEKTEYLNK--------ILSITGLPLIS--------- 1132
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1918 fDALIKDvfpgIDFKEVEYDELSS-ALKQVFEEANyEVIPNQMKKALELYEQLRQRTGVVIVGPSGAGKSTLWRmlrAAL 1996
Cdd:COG5245 1133 -DTLRER----IDTLDAEWDSFCRiSESLKKYESQ-QVSGLDVAQFVSFLRSVDTGAFHAEYFRVFLCKIKHYT---DAC 1203
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1997 CKIGKVVKQYTMNPKAMPRHQLLGHIDMDTREWSDGVLTNSARQVVREpqdvsswiicdgdidpEWIESLNSVLDDNRLL 2076
Cdd:COG5245 1204 DYLWHVKSPYVKKKYFDADMELRQFFLMFNREDMEARLADSKMEYEVE----------------RYVEKTKAEVSSLKLE 1267
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2077 TMPSGERiqfgpnvNFVFETHDlscASPATISRMGMIFLSDEETDLNSLIKSWL--RNQPLEyrSNLENWIGDYFSK--- 2151
Cdd:COG5245 1268 LSSVGEG-------QVVVSNLG---SIGDKVGRCLVEYDSISRLSTKGVFLDELgdTKRYLD--ECLDFFSCFEEVQkei 1335
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2152 -ALQWVLKQNDYVVETSLVGTVmnGLSHLHGCKYHDQFIINLI---RGLGGNLNMKSRLEFTKEVFN----WA------R 2217
Cdd:COG5245 1336 dELSMVFCADALRFSADLYHIV--KERRFSGVLAGSDASESLGgksIELAAILEHKDLIVEMKRGINdvlkLRifgdkcR 1413
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2218 ETPPDSHRPMDTYYDCDRGQLASY--MLKKPESLTADDFSNGHI-----------LP---VIQTPDMQRGLDYFKPWLSs 2281
Cdd:COG5245 1414 ESTPRFYLISDGDLIKDLNERSDYeeMLIMMFNISAVITNNGSIagfelrgervmLRkevVIPTSDTGFVDSFSNEALN- 1492
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2282 dTKQPFILVGPEGCGKGMLLRYAFSQLRSTEIATIHCSAQTTSRHLLQKLSQTcMVISTNTG--RVYRPKDCERLVLYLK 2359
Cdd:COG5245 1493 -TLRSYIYCGPPGSGKEMLMCPSLRSELITEVKYFNFSTCTMTPSKLSVLERE-TEYYPNTGvvRLYPKPVVKDLVLFCD 1570
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2360 DINLPKLDKWGTSTLVAFLQQVLTYQGFYDE-NLEWVGLENIQIVASMSAGGRLGRHKLTTRFTSIVRLCAIDYPEREQL 2438
Cdd:COG5245 1571 EINLPYGFEYYPPTVIVFLRPLVERQGFWSSiAVSWVTICGIILYGACNPGTDEGRVKYYERFIRKPVFVFCCYPELASL 1650
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2439 QTIYGAYLEAVLHKNLKNHSIwgssskIYLLAGSMVQVYEQVRAKFTVDEYSHYFFTPCILTQWVLGLFRYDLEGgsSNH 2518
Cdd:COG5245 1651 RNIYEAVLMGSYLCFDEFNRL------SEETMSASVELYLSSKDKTKFFLQMNYGYKPRELTRSLRAIFGYAETR--IDT 1722
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2519 PLDYVLEIVAYEARRLFRDKIVGVKELHLFDNILTSVLQGDWGSDILDNMADSFYVTWGAHHVSggktapgqplpphgkp 2598
Cdd:COG5245 1723 PDVSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREMIAGHIGEAEITFSMILFFG---------------- 1786
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2599 LGKLTSADLKDVIKKGLIHYGRDNQNLDILLFQEVLEYMSRIDRVLSFPGGSLLLAGRSGVGRRTVTSLVSHMHGAVLFS 2678
Cdd:COG5245 1787 MACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMRE 1866
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2679 PKISRGYEPKQFRNDLKHVLQLAGIEAQQVVLLLEDYQFVHPTFLEMINSLLASGEVPGLYTLEELEPLLLPLKDQASQD 2758
Cdd:COG5245 1867 IFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFEST 1946
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2759 GFF----GPVFNYFTYRIQQNLHIVL-IMDSANLNFIVNCESnPALHKKCQVLWMEGWSDSSMKKIPEMLFSET--DGEE 2831
Cdd:COG5245 1947 SLEkdteATLTRVFLVYMEENLPVVFsACCSQDTSVLAGIRS-PALKNRCFIDFKKLWDTEEMSQYANSVETLSrdGGRV 2025
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2832 KYEKKRKDEKKRNSVDPDFIKSFLLIHES-------CKAYGATPSRYMTFLHVYSAISSSKKKELLKRQSHLQAGVSKLN 2904
Cdd:COG5245 2026 FFINGELGVGKGALISEVFGDDAVVIEGRgfeismiEGSLGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYN 2105
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2905 EAKALVDELNRKAGEQSILLRIKQDEADSALQEITVSMQDASEQKTELERLKQRIAEEVVKIEERKSKIDDELKEVQPLV 2984
Cdd:COG5245 2106 EYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAV 2185
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2985 NEAKLAVGNIRPESLSEIRSLRMPPDVIRDILEGVLRLMGIFDTSWVSMKSFLAKRGVREDIATFD-ARNIPKEIRESVE 3063
Cdd:COG5245 2186 LEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLLGFEAKIWFGEQQSLRRDDFIRIIGKYPdEIEFDLEARRFRE 2265
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3064 ELLFKNkASFDPKNAKRASTAAAPLAAWVKANVQYSHVLERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSEL 3143
Cdd:COG5245 2266 ARECSD-PSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRR 2344
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3144 KEKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLDREHRRWNAQVAEIAEELATLPKRAQLAAAFITYLSAAPEGLR-- 3221
Cdd:COG5245 2345 RSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRai 2424
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3222 -KNCLEEWTKAAGLEKFDLRRFLCTESEQLIWKSEGLP-SDDLSIENALVIlqiiglKSWSRVCPFLIDPSSQATEWLKT 3299
Cdd:COG5245 2425 eFGMSFIRISKEFRDKEIRRRQFITEGVQKIEDFKEEAcSTDYGLENSRIR------KDLQDLTAVLNDPSSKIVTSQRQ 2498
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3300 HLKDSHLEVINQQDSNFITALELAVRFGKTLIIQEMDGVEPVLYPLLRRDLVAQGPRYVVQIGDKIIDYNEDFRLFLSTR 3379
Cdd:COG5245 2499 MYDEKKAILGSFREMEFAFGLSQARREGSDKIIGDAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSE 2578
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3380 NPNPFIPPDAASIVTEVNFTTTRSGLRGQLLALTIQHEKPDLEEQKTKLLQQEEDKKIQLARLEESLLETLATSQGNILE 3459
Cdd:COG5245 2579 GRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQ 2658
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3460 NKDLIESLNQTKASSALIQDSLKESYKLQISLDQERDAYLPLAESASKMYFIISDLSKINNMYRFSLASFLRLFQRALqn 3539
Cdd:COG5245 2659 TDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFEKWR-- 2736
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3540 kqdseNTEERIQCLVNSLKHMVYEYI---CRCLF----------KADQLMFALHFVRGMHPELfqENEWDTFTGVVVgdm 3606
Cdd:COG5245 2737 -----RMKSKYLCAIRYMLMSSEWILdheDRSGFihrldvsfllRTKRFVSTLLEDKNYRQVL--SSCSLYGNDVIS--- 2806
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3607 lrkaDSQQRI-RDQLPSWIDQERSWAVATLKislpsLYQTLCLEDGAFWRTYYHHSMCEQEFPSILAKkvslFQQvlvvq 3685
Cdd:COG5245 2807 ----HSCDRFdRDVYRALKHQMDNRTHSTIL-----TSNSKTNPYKEYTYNDSWAEAFEVEDSGDLYK----FEE----- 2868
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3686 alrpdrlqsamalfackalGLKELSPLPLNLKRLYKETLEIEPIliiispgadpsqeLQELASAERSSecyhqvamgqgq 3765
Cdd:COG5245 2869 -------------------GLLELIVGHAPLIYAHKKSLENERN-------------VDRLGSKENEV------------ 2904
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3766 adLAIQMLKECARNGDWLCLKNLHLVVSWL-----PVLEKELNTLQPKDSFRLWLTAEVHPNFTPILLQSSLKITYESPP 3840
Cdd:COG5245 2905 --YAVLNSLFSRKEKSWFEVYNISLSFGWFkryveDVVYPIKASRVCGKVKNMWTSMVDADMLPIQLLIAIDSFVSSTYP 2982
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3841 GLKKNLMRTYES-WTPEQISKrdnIHRAHALFSLAWFHAACQERRNYIPQGWTKFYEFSLSDLRAGYHVIDRLF--DGTK 3917
Cdd:COG5245 2983 ETGCGYADLVEIdRYPFDYTL---VIACDDAFYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNILflNHLN 3059
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3918 DVQWEFVHGLLENSIYGGRVDNYFDLRVLQSYLKQFF----NSSIID--VLNQRNKKSIFPYSISLpnSCSILdyraVIE 3991
Cdd:COG5245 3060 ARKWGNNRDLIFTIVYGKKHSLMEDSKVVDKYCRGYGahetSSQILAsvPGGDPELVKFHMEEMCR--SSAFG----VIG 3133
|
2730 2740 2750
....*....|....*....|....*....|.
gi 1720430018 3992 KLPEDDKPSFFGLPANIARSSQRMISSQVIS 4022
Cdd:COG5245 3134 QLPDLALCAWLMGPCDSEYLKAIVYSSRIDM 3164
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1120-1518 |
1.21e-126 |
|
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: 405.87 E-value: 1.21e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1120 ISKDIESCAQIWALYEEFQQGLQDMAKEDWITyrAKIYLFEEFLINWHERLRKIE---EHSVMTVKLQSEVDRYKMIIPI 1196
Cdd:pfam08393 4 IKKELEPLKKLWDLVSEWQESLEEWKNGPFSD--LDVEELEEELEEFLKELKKLPkelRDWDVAEELKKKIDDFKKSLPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1197 LKYVRGEHLSPDHWLDLFRLLGLPRGTSLEKLLFGDLLRVadTIVEKASELKDLNSRAQGEVTIREALRELDLWGVGAVF 1276
Cdd:pfam08393 82 IEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDL--NLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1277 SLIDYEDSqnhTIKLIKDWKDIVNQVGDNRCLLQSLKDSPYYKGFEDKVSIWERKLAQLDEYLQNLNHIQRKWVYLEPIF 1356
Cdd:pfam08393 160 ELVPYKDT---GTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1357 G----RGALPKEQTRFNKVDEDFRSIMMDIRKDSRVTTLTTHAGIRNTLLTILDQLQRCQKSLNEFLEEKRSAFPRFYFI 1432
Cdd:pfam08393 237 SsediRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1433 GDDDLLEILGQSTNPSVIQSHLKKLFAGINSVCFDeESKHITAMKSLEGEVVPF-KSKVLLSNNVEAWLNDLALEMKQTL 1511
Cdd:pfam08393 317 SNDELLEILSQTKDPTRVQPHLKKCFEGIASLEFD-ENKEITGMISKEGEVVPFsKPPVEAKGNVEEWLNELEEEMRETL 395
|
....*..
gi 1720430018 1512 KQLLKEC 1518
Cdd:pfam08393 396 RDLLKEA 402
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3252-3477 |
3.93e-94 |
|
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: 304.75 E-value: 3.93e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3252 WKSEGLPSDDLSIENALVILQiiglkswSRVCPFLIDPSSQATEWLKTHLKDSHLEVINQQDSNFITALELAVRFGKTLI 3331
Cdd:pfam12781 3 WNIQGLPNDELSIENAIIVTN-------SRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3332 IQEM-DGVEPVLYPLLRRDLVAQGPRYVVQIGDKIIDYNEDFRLFLSTRNPNPFIPPDAASIVTEVNFTTTRSGLRGQLL 3410
Cdd:pfam12781 76 IEDVgEELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720430018 3411 ALTIQHEKPDLEEQKTKLLQQEEDKKIQLARLEESLLETLATSQGNILENKDLIESLNQTKASSALI 3477
Cdd:pfam12781 156 GIVVKKERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4017-4310 |
1.27e-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: 1.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 4017 SSQVISQLRILGRSVTAGCKFDREiwSNElSPVLNLWKKLNQ---NSNLIHQKVSPPNDRQGSPILSFIILEQFNAIRLV 4093
Cdd:pfam18199 4 TNELLSTLLSLQPRSDSGGGGGGS--SRE-EIVLELAKDILEklpEPFDIEEAEEKYPVGYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 4094 QSVHQSLAALSKVIRGTTLLSSEVQKLASALLNQKCPLTWQSRWEGPEDPL-QYLRGLVARTLAIQNWVEKAEKQVllad 4172
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLgSWIRDLLERLKQLQDWLDDEGPPK---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 4173 TLDLSELFHPDTFLNALRQETARATGCSVDSLKFVASWKGRLQEAKLQIK------ISGLLLEGCSFDG--NRLSEnQHD 4244
Cdd:pfam18199 157 VFWLSGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTKKVSPEEVTEPpedgvyVHGLFLEGARWDRknGCLVE-SEP 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720430018 4245 SPSVSSVLPCYMgwTPQGSYGPYSPDECISLPVYTSAERER--VVTNIDVPCGGNQDQWIQCGAALFL 4310
Cdd:pfam18199 236 KELFSPLPVIHL--KPVESDKKKLDENTYECPVYKTSERHStnFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| AAA_lid_11 |
pfam18198 |
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the ... |
3870-4008 |
4.83e-50 |
|
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: 174.95 E-value: 4.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3870 LFSLAWFHAACQERRNYIPQGWTKFYEFSLSDLRAGYHVIDRLFDGTKD-VQWEFVHGLLENSIYGGRVDNYFDLRVLQS 3948
Cdd:pfam18198 5 LFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLDEYDEkIPWDALRYLIGEINYGGRVTDDWDRRLLNT 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3949 YLKQFFNSSIIDvlnqrNKKSIFPYSISLPNSCSILDYRAVIEKLPEDDKPSFFGLPANI 4008
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 |
1.25e-43 |
|
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: 161.24 E-value: 1.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2625 LDILLFQEVLEYMSRIDRVLSFPGGSLLLAGRSGVGRRTVTSLVSHMHGAVLFSPKISRGYEPKQFRNDLKHVLQLAGIE 2704
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2705 AQQVVLLLEDYQFVHPTFLEMINSLLASGEVPGLYTLEELEPLLLPLKDQASQDGFFGP---VFNYFTYRIQQNLHIVLI 2781
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSreaVYNYFVKRCRNNLHIVLC 160
|
170 180 190
....*....|....*....|....*....|
gi 1720430018 2782 MDSANLNFIVNCESNPALHKKCQVLWMEGW 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 ... |
3736-3835 |
2.33e-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: 143.35 E-value: 2.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3736 GADPSQELQELASAERSSECYHQVAMGQGQADLAIQMLKECARNGDWLCLKNLHLVVSWLPVLEKELNTLQPK---DSFR 3812
Cdd:pfam03028 13 GSDPTADLEKLAKKLGFGGKLHSISLGQGQGPIAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKILEELPEEtlhPDFR 92
|
90 100
....*....|....*....|...
gi 1720430018 3813 LWLTAEVHPNFTPILLQSSLKIT 3835
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 |
9.11e-30 |
|
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: 117.01 E-value: 9.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1974 GVVIVGPSGAGKSTLWRMLRAALCKigkVVKQYTMNPKAMPRHQLLGHIDMDTR--EWSDGVLTNSARqvvrepqdvSSW 2051
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSN---RPVFYVQLTRDTTEEDLFGRRNIDPGgaSWVDGPLVRAAR---------EGE 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720430018 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 ... |
2896-3228 |
1.51e-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: 114.40 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2896 LQAGVSKLNEAKALVDELNRKAGEQSILLRIKQDEADSALQEITVSMQDASEQKTELERLKQRIAEEVVKIEERKSKIDD 2975
Cdd:pfam12777 3 LENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKACEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2976 ELKEVQPLVNEAKLAVGNIRPESLSEIRSLRMPPDVIRDILEGVLRLMGIF-----DTSWVSMKSFLAK-RGVREDIATF 3049
Cdd:pfam12777 83 DLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMAPGgkipkDKSWKAAKIMMAKvDGFLDSLIKF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3050 DARNIPKEIRESVEEllFKNKASFDPKNAKRASTAAAPLAAWVKANVQYSHVLERIQPLETEQSGLELNLKKTEDRKRKL 3129
Cdd:pfam12777 163 DKEHIHEACLKAFKP--YLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQEKLAAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3130 EDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLDREHRRWNAQVAEIAEELATLPKRAQLAAAF 3209
Cdd:pfam12777 241 KAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDILLISAF 320
|
330 340
....*....|....*....|
gi 1720430018 3210 ITYLSAAPEGLRKNCLEE-W 3228
Cdd:pfam12777 321 ISYLGFFTKKYRNELLDKfW 340
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
161-674 |
7.03e-22 |
|
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: 103.43 E-value: 7.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 161 LKEDDTRGILTPSDEFQFWIEQA--------HRGSKQISK-----ERA--SY---FKELFE-----------------TI 205
Cdd:pfam08385 19 LKEDSQGRNPGPLAEIEFWKSREanlssiyeQLKSPEVKKvleilEAAksSYlpaFKALDTeltdalneakdnvkylkTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 206 SREFYNLDSL-SLLEVVDLVETTRDVVDDVWRQTEHdhYPES-RMLHLLDVIGGSFGRFVQKKLGSLKLWEDPYYLVKEN 283
Cdd:pfam08385 99 ERPFEDLEELtDPPEIIEAIPPLMNTIRLIWSISRY--YNTSeRMTVLLEKISNQLIEQCKKYLSPEGIFDGDVEEALEK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 284 LKAGISICEQWVIVCSHLTGQVWQRYVPHPWK-SGKYFPETLDKLGKRLEEVLAIRTIHEKLLYFLPASEERIVCLSRVF 362
Cdd:pfam08385 177 LQECIELLEAWKEEYKKTREKLEESPRERPWDfSERYIFGRFDAFLERLEKILELFETIEQFSKLEKIGGTKGPELEGVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 363 EP--------FTGVNPVQYNP--YTEPLWKAAVSQYEKIIAPAEQKIAGKLKNYISEIQdSPQQLLQAFLKYKELVKRPT 432
Cdd:pfam08385 257 EEileefqeaYKVFKSKTYDIldVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDDAR-STESAFKLLRIFEFLLERPI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 433 ISKELMLERETLLARLGDSAKDFRLDFENRCRgipgDPSgpLSGKNLSEVVNNIVWVRQLELKVDDTIKIAEALLSDLSg 512
Cdd:pfam08385 336 IRGALEEKYTDLLQMFKKELDAVKKIFDKQKY----NPS--PIAKNMPPVAGAIIWARQLFRRIQEPMKRFKEELGLLK- 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 513 frsfHRSAEDLLDQF-------KLYEQEQFDDWSREVqsglsDSRSGLCIEANsrIMELDPNDGAL-KVHYSDRLVILLR 584
Cdd:pfam08385 409 ----HAEGKKVIKKYnelakklDEYERLIYEAWLKEV-----EEASEGNLKRP--LLVRHPETGKLlSVNFDPQLLALLR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 585 EVRQLSALGFVIPAKIQQVANVAQKFCKQAIILKQVAHFYNSIDQQMIQSQRPMMLQSALAFEQIIKNskagsgGKSQIT 664
Cdd:pfam08385 478 EVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEP------GLTTLT 551
|
570
....*....|
gi 1720430018 665 WDNpKELEGY 674
Cdd:pfam08385 552 WNS-LGIDEY 560
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2284-2423 |
1.65e-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: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2284 KQPFILVGPEGCGKGMLLRYAFSQLRSTE--IATIHCSAQTTSrhllqklSQTCMVISTN----TGRVYRPKDCERLVLY 2357
Cdd:pfam12775 31 GKPVLLVGPTGTGKTVIIQNLLRKLDKEKylPLFINFSAQTTS-------NQTQDIIESKlekrRKGVYGPPGGKKLVVF 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720430018 2358 LKDINLPKLDKWGTSTLVAFLQQVLTYQGFYD-ENLEWVGLENIQIVASMS-AGGrlGRHKLTTRFTS 2423
Cdd:pfam12775 104 IDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDrKKLTFKEIVDVQFVAAMGpPGG--GRNDITPRLLR 169
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2885-3237 |
6.25e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 6.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2885 KKKELLKRQSHLQAGVSKLNEAKALVDELNRkageqsillrIKQDEADSALQEITVSMQDASEQKTELErlkqriaEEVV 2964
Cdd:PRK03918 346 KLKELEKRLEELEERHELYEEAKAKKEELER----------LKKRLTGLTPEKLEKELEELEKAKEEIE-------EEIS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2965 KIEERKSKIDDELKEVQPLVNEAKLAVG---------------NIRPESLSEIRSLRMPPDVIRDILEGVLRLMgifdts 3029
Cdd:PRK03918 409 KITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKEL------ 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3030 wVSMKSFLAKRgvREDIATfdaRNIPKEIRESVEELlfknkASFDPKNAKrastaaaplaawvKANVQYSHVLERIQPLE 3109
Cdd:PRK03918 483 -RELEKVLKKE--SELIKL---KELAEQLKELEEKL-----KKYNLEELE-------------KKAEEYEKLKEKLIKLK 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3110 TEQSGLELNLKKTEDRKRKLEdllnsvgqkvsELKEKFQSRTSEAAKLEAEVSK-AQETIKAAEVLISQLDREHRRWNA- 3187
Cdd:PRK03918 539 GEIKSLKKELEKLEELKKKLA-----------ELEKKLDELEEELAELLKELEElGFESVEELEERLKELEPFYNEYLEl 607
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1720430018 3188 -----QVAEIAEELATLPKRAQLAAAFITYLSAAPEGLRKNcLEEWTKAAGLEKF 3237
Cdd:PRK03918 608 kdaekELEREEKELKKLEEELDKAFEELAETEKRLEELRKE-LEELEKKYSEEEY 661
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3091-3208 |
1.36e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3091 WVKANVQYSHVLERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKA 3170
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110
....*....|....*....|....*....|....*...
gi 1720430018 3171 AEVLISQLDREHRRWNAQVAEIAEELATLpkRAQLAAA 3208
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEEL--EEELEEA 349
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2883-3223 |
5.46e-07 |
|
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: 56.23 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2883 SSKKKELLKRQSHLQAGVSKLNEAKALVDELNRK-----AGEQsilLRIKQDeadsaLQEITVSMQDASEQKTELERLKQ 2957
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKikdlgEEEQ---LRVKEK-----IGELEAEIASLERSIAEKERELE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2958 RIAEEVVKIEERKSKIDDELKEVqplvnEAKLAVGNIRPESLSEIrslrmppdvirdilegvlrlmgifdtswvsmksFL 3037
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEEL-----EREIEEERKRRDKLTEE---------------------------------YA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3038 AKRGVREDIATfDARNIPKEIRESVEELlfknkasfdpknakrastaaaplaawVKANVQYSHVLERIQPLETEQSGLEL 3117
Cdd:TIGR02169 361 ELKEELEDLRA-ELEEVDKEFAETRDEL--------------------------KDYREKLEKLKREINELKRELDRLQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3118 NLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLDREHRRWNAQVAEIAEELA 3197
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
330 340
....*....|....*....|....*.
gi 1720430018 3198 TLPKRAQLAAAFITYLSAAPEGLRKN 3223
Cdd:TIGR02169 494 EAEAQARASEERVRGGRAVEEVLKAS 519
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2885-3202 |
1.31e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2885 KKKELLKRQSHLQAGVSKLNEAKALVDELNRKAGEQSILLRIKqDEADSALQEITVSMQDASEQKTELERLKQRIAEEVV 2964
Cdd:PRK03918 260 KIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFY-EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2965 KIEERKSKIDD------ELKEVQPLVNEAKLAVGNIrpESLSEIRSLRMPPDVIRDILEgvlrlmgifdtswvsMKSflA 3038
Cdd:PRK03918 339 RLEELKKKLKElekrleELEERHELYEEAKAKKEEL--ERLKKRLTGLTPEKLEKELEE---------------LEK--A 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3039 KRGVREDIATFDAR-----NIPKEIRESVEELlfkNKASFDPKNAKRASTAAAPLAAWVKANVQYSHVLERIQPLETEQS 3113
Cdd:PRK03918 400 KEEIEEEISKITARigelkKEIKELKKAIEEL---KKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3114 GLELNLKKTE----------------DRKRKLEDLLNSVG-QKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLIS 3176
Cdd:PRK03918 477 KLRKELRELEkvlkkeseliklkelaEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK 556
|
330 340
....*....|....*....|....*.
gi 1720430018 3177 QLdrehRRWNAQVAEIAEELATLPKR 3202
Cdd:PRK03918 557 KL----AELEKKLDELEEELAELLKE 578
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2885-3206 |
2.19e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2885 KKKELLKRQSHLQagvSKLNEAKALVDELNRKAGEQSillriKQDEADSALQEITVSMQDASEQKTELERLKQriAEEVV 2964
Cdd:PTZ00121 1477 KKAEEAKKADEAK---KKAEEAKKKADEAKKAAEAKK-----KADEAKKAEEAKKADEAKKAEEAKKADEAKK--AEEKK 1546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2965 KIEERKSKidDELKEVqplvnEAKLAVGNIRPESLSEIRSLRMPpDVIRDILEGVLRLMGIFDTSWVSMKSFLAKRGVRE 3044
Cdd:PTZ00121 1547 KADELKKA--EELKKA-----EEKKKAEEAKKAEEDKNMALRKA-EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3045 DIATFDARNiPKEIRESVEELlfKNKASFDPKNA----KRASTAAAPLAAWVKANVQYSHVLERIQPLETEQSGLELNLK 3120
Cdd:PTZ00121 1619 KIKAEELKK-AEEEKKKVEQL--KKKEAEEKKKAeelkKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3121 KTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLisQLDREHRRWNAQVAEIAEELATLP 3200
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA--KKDEEEKKKIAHLKKEEEKKAEEI 1773
|
....*.
gi 1720430018 3201 KRAQLA 3206
Cdd:PTZ00121 1774 RKEKEA 1779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2886-3507 |
3.62e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2886 KKELLKRQSHLQAGVSKLNEAKALVDELNRKAGEQSILLRIKQDEADSALQEITVSMQDASEQKTELERLKQRIAEEVVK 2965
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2966 IEERKSKIDDELKEVQPLVNEAKLAvgnirpeslseirslrmppdvirdilegvlrlmgifdtswvsmksflakrgvred 3045
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEA------------------------------------------------------- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3046 iatfdarnipKEIRESVEELLFKNKASFDPKNAKrastaaaplaaWVKANVQYSHVLERIQPLETEQSGLELNLKKTEDR 3125
Cdd:COG1196 357 ----------EAELAEAEEALLEAEAELAEAEEE-----------LEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3126 KRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLDREHRRWNAQVAEIAEELATLPKRAQL 3205
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3206 AAAfityLSAAPEGLrkncLEEWTKAAGLEKFDLrrfLCTESEQLIWKSEGLPSDDLSIENALviLQIIGLKSWSRVcpf 3285
Cdd:COG1196 496 LLE----AEADYEGF----LEGVKAALLLAGLRG---LAGAVAVLIGVEAAYEAALEAALAAA--LQNIVVEDDEVA--- 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3286 lidpsSQATEWLKTHLK----DSHLEVINQQDSNFITALELAVRFGKTLIIQEMDGVEPVLYPLLRRDLVAQGPRYVVQI 3361
Cdd:COG1196 560 -----AAAIEYLKAAKAgratFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3362 GDKIIDYNEDFRLFLSTRnpnpfippdaasiVTEVNFTTTRSGLRGQLLALTIQHEKPDLEEQKTKLLQQEEDKKIQLAR 3441
Cdd:COG1196 635 ALRRAVTLAGRLREVTLE-------------GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720430018 3442 LEESLLETLATSQGNILENKDLIESLNQTKASSALIQDSLKESYKLQISLDQERDAYLPLAESASK 3507
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2889-3201 |
6.72e-06 |
|
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: 52.76 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2889 LLKRQSHLQagvSKLNEAKALVDELNRKAGEQSILLRIKQDEADSALQEITVSMQDASEQKTELERLKQRIAEEVVKIEE 2968
Cdd:TIGR02169 693 LQSELRRIE---NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2969 RKSKIDDELKEVQPLvnEAKLAvGNIRPESLSEIRSLRmppDVIRDIlEGVLRlmgifdtswvSMKSFLAKRGVREDIAt 3048
Cdd:TIGR02169 770 LEEDLHKLEEALNDL--EARLS-HSRIPEIQAELSKLE---EEVSRI-EARLR----------EIEQKLNRLTLEKEYL- 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3049 fdarnipkeiRESVEELLFKNKASFDPKNAKRastaaaplaawvkanvqyshvlERIQPLETEQSGLELNLKKTEDRKRK 3128
Cdd:TIGR02169 832 ----------EKEIQELQEQRIDLKEQIKSIE----------------------KEIENLNGKKEELEEELEELEAALRD 879
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720430018 3129 LEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIK----AAEVLISQLDrEHRRWNAQVAEIAEELATLPK 3201
Cdd:TIGR02169 880 LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSelkaKLEALEEELS-EIEDPKGEDEEIPEEELSLED 955
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2884-3236 |
9.43e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 9.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2884 SKKKELLKRQSHLQAGVSKLNEAKALVDELNRKAGEQSillriKQDEADSALQEI---TVSMQDASEQKTELERLKQRiA 2960
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK-----KADEAKKKAEEDkkkADELKKAAAAKKKADEAKKK-A 1427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2961 EEVVKIEERKSKIDDELK--EVQPLVNEAKLAvgnirpESLSEIRSLRMPPDVIRDILEGVLRlmgifdTSWVSMKSFLA 3038
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKadEAKKKAEEAKKA------EEAKKKAEEAKKADEAKKKAEEAKK------ADEAKKKAEEA 1495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3039 KRGVREDIATFDARNIPKEIRESVE----ELLFKNKASFDPKNAKRASTAAAPLAAWVKANVQYSHVLERIQPLETEQSG 3114
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKAEEakkaDEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3115 LELNLKKTEDrKRKLEDLLNSVGQKVSELKEKF---QSRTSEAAKLEAE-VSKAQETIKAAEVLISQLDREHRRwnAQVA 3190
Cdd:PTZ00121 1576 KNMALRKAEE-AKKAEEARIEEVMKLYEEEKKMkaeEAKKAEEAKIKAEeLKKAEEEKKKVEQLKKKEAEEKKK--AEEL 1652
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1720430018 3191 EIAEELATLpKRAQLAAAFITYLSAAPEgLRKNCLEEWTKAAGLEK 3236
Cdd:PTZ00121 1653 KKAEEENKI-KAAEEAKKAEEDKKKAEE-AKKAEEDEKKAAEALKK 1696
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2887-3208 |
1.01e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2887 KELLKRQSHLQAGVSKLNEAKALVDELNRKAGEqsiLLRIKQDEADSALQEITVSMQDASEQKTELERLKQRIAEEvvkI 2966
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEE---LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE---L 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2967 EERKSKIDDELKEVQPLVNEAKLAVGNIRPESLSEIRSLRMPPDVIRDILE---GVLRLMG--IFDTSWVSMKSFLAKRG 3041
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILtiaGVLFLVLglLALLFLLLAREKASLGK 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3042 VREDIATFDARNI--PKEIRESVEELLFKNKASfdpknAKRASTAAAPLAAWVKANVQYSHVLER--IQPLETEQSGLeL 3117
Cdd:COG4717 303 EAEELQALPALEEleEEELEELLAALGLPPDLS-----PEELLELLDRIEELQELLREAEELEEElqLEELEQEIAAL-L 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3118 NLKKTED---------RKRKLEDLLnsvgQKVSELKEKFQSRTSEAAKLEAEVSKAQ--ETIKAAEVLISQLDREHRRWN 3186
Cdd:COG4717 377 AEAGVEDeeelraaleQAEEYQELK----EELEELEEQLEELLGELEELLEALDEEEleEELEELEEELEELEEELEELR 452
|
330 340
....*....|....*....|..
gi 1720430018 3187 AQVAEIAEELATLPKRAQLAAA 3208
Cdd:COG4717 453 EELAELEAELEQLEEDGELAEL 474
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3103-3334 |
3.05e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3103 ERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLDREH 3182
Cdd:COG4372 73 SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3183 RRWNAQVAEIAEELATLPKRAQ--LAAAFITYLSAAPEGLRKNCLEEWTKAAGLEKFDLRRFLCTESEQLIWKSEGLPSD 3260
Cdd:COG4372 153 KELEEQLESLQEELAALEQELQalSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720430018 3261 DLSIENAL-VILQIIGLKSWSRVCPFLIDPSSQATEWLKTHLKDSHLEVINQQDSNFITALELAVRFGKTLIIQE 3334
Cdd:COG4372 233 LALSALLDaLELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAAL 307
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2943-3200 |
3.97e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2943 QDASEQKTELERLKQRIAEEVVKIEERKSKIDDELKEVQPLvnEAKLAvgnirpESLSEIRSLRMPPDVIRDILEGVLRL 3022
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--ERRIA------ALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3023 MGIFDTSWVSMKSFLAKRgvrediatfdARNIPKEIRESVEELLFKNKasfDPKNAKRASTaaaplaaWVKANVQYshVL 3102
Cdd:COG4942 92 IAELRAELEAQKEELAEL----------LRALYRLGRQPPLALLLSPE---DFLDAVRRLQ-------YLKYLAPA--RR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3103 ERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLDREH 3182
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|....*...
gi 1720430018 3183 RRWNAQVAEIAEELATLP 3200
Cdd:COG4942 230 ARLEAEAAAAAERTPAAG 247
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3093-3223 |
4.95e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3093 KANVQYSHVLERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVG---------QKVSELKEKFQSRTSEAAKLEAEVSK 3163
Cdd:COG1579 42 ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyealqKEIESLKRRISDLEDEILELMERIEE 121
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720430018 3164 AQETIKAAEVLIS----QLDREHRRWNAQVAEIAEELATLP-KRAQLAAAFITYLSAAPEGLRKN 3223
Cdd:COG1579 122 LEEELAELEAELAeleaELEEKKAELDEELAELEAELEELEaEREELAAKIPPELLALYERIRKR 186
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2853-3199 |
1.22e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 48.03 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2853 SFLLIHESCKAYGATPSRYMTFLHVYSaISSSKKKELLKRQSHLQagvsKLNEAKALVDELNRKAGEQSILLRIKQDEAD 2932
Cdd:COG5185 193 SELKKAEPSGTVNSIKESETGNLGSES-TLLEKAKEIINIEEALK----GFQDPESELEDLAQTSDKLEKLVEQNTDLRL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2933 SALQEITVSMQDASEQKTEL----ERLKQRIAEEVVKIEERKSkIDDELKEVQPLVNEAKLAvgnirpESLSEIRSlrmp 3008
Cdd:COG5185 268 EKLGENAESSKRLNENANNLikqfENTKEKIAEYTKSIDIKKA-TESLEEQLAAAEAEQELE------ESKRETET---- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3009 pdVIRDILEGVLRLMGIFDTSWVSMKSFLAKRGVREDIATFDAR--NIPKEIRESVEELLFKNKasfDPKNAKRAstaaa 3086
Cdd:COG5185 337 --GIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEEldSFKDTIESTKESLDEIPQ---NQRGYAQE----- 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3087 plaawVKANVQySHVLERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKlEAEVSKAQE 3166
Cdd:COG5185 407 -----ILATLE-DTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYD-EINRSVRSK 479
|
330 340 350
....*....|....*....|....*....|...
gi 1720430018 3167 TIKaaevlisqLDREHRRWNAQVAEIAEELATL 3199
Cdd:COG5185 480 KED--------LNEELTQIESRVSTLKATLEKL 504
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3103-3208 |
2.90e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3103 ERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAA----KLEAEVSKAQETIKAAEVLISQL 3178
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAalleALEEELEALEEALAEAEAALRDL 417
|
90 100 110
....*....|....*....|....*....|....*..
gi 1720430018 3179 DREHRRWNAQVAE-------IAEELATLpkRAQLAAA 3208
Cdd:COG4913 418 RRELRELEAEIASlerrksnIPARLLAL--RDALAEA 452
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2877-3204 |
2.96e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2877 VYSAISSSKKKELLKRQSHLQagvSKLNEAKALVDELNrkagEQSILLRIKQDEADSALQEitvsmqdASEQKTELERLK 2956
Cdd:PRK02224 192 LKAQIEEKEEKDLHERLNGLE---SELAELDEEIERYE----EQREQARETRDEADEVLEE-------HEERREELETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2957 QRIAEEVVKIEE---RKSKIDDELKEVQPLVNE---------AKLAVGNIRPESLSEIRS-LRMPPDVIRDILEgvlrlm 3023
Cdd:PRK02224 258 AEIEDLRETIAEterEREELAEEVRDLRERLEEleeerddllAEAGLDDADAEAVEARREeLEDRDEELRDRLE------ 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3024 gifdTSWVSMKSFLAK-RGVREDIATFDARNipKEIRESVEEL---LFKNKASFDPKNAKRA---STAAAPLAAWVKANV 3096
Cdd:PRK02224 332 ----ECRVAAQAHNEEaESLREDADDLEERA--EELREEAAELeseLEEAREAVEDRREEIEeleEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3097 QYSHVLERIQPLETEQSG-------LELNLKKTEDRKRKLEDLLNS-----VGQKV---------SELKEKFQSRTSEAA 3155
Cdd:PRK02224 406 DLGNAEDFLEELREERDElrereaeLEATLRTARERVEEAEALLEAgkcpeCGQPVegsphvetiEEDRERVEELEAELE 485
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720430018 3156 KLEAEVSKAQETIKAAEVLISQLDR----EHRRWNAQ---------VAEIAEELATLPKRAQ 3204
Cdd:PRK02224 486 DLEEEVEEVEERLERAEDLVEAEDRierlEERREDLEeliaerretIEEKRERAEELRERAA 547
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2945-3202 |
5.18e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2945 ASEQKTELERLKQRIAEEVvkieERKSKIDDELKEVQPLVNEAKLAVGNIRPEslseIRSLRMPPDVIRDILEGVLRLMG 3024
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFI----KRTENIEELIKEKEKELEEVLREINEISSE----LPELREELEKLEKEVKELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3025 IFDTSWVSMKSFLA-KRGVREDIatfdarnipKEIRESVEELlfKNKASFDPKNAKRastaaaplaawvkanvqyshvLE 3103
Cdd:PRK03918 239 EIEELEKELESLEGsKRKLEEKI---------RELEERIEEL--KKEIEELEEKVKE---------------------LK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3104 RIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELKEKFqsrtSEAAKLEAEVSKAQETIKAAEVLISQLDREHR 3183
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI----KELEEKEERLEELKKKLKELEKRLEELEERHE 362
|
250
....*....|....*....
gi 1720430018 3184 RWNaQVAEIAEELATLPKR 3202
Cdd:PRK03918 363 LYE-EAKAKKEELERLKKR 380
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
1937-1988 |
8.36e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 43.93 E-value: 8.36e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1720430018 1937 DELSSALKQVFEEANYEVIPNQMKKAL---ELYEQLRQRTgVVIVGPSGAGKSTL 1988
Cdd:cd01854 48 DEELEELLEIYEKLGYPVLAVSAKTGEgldELRELLKGKT-SVLVGQSGVGKSTL 101
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3119-3223 |
9.25e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3119 LKKTEDRKRKLEDLLNSVGQKVSELKEKfqsrtseAAKLEAEVSKAQETIKAAEVLISQLDREHRRWNAQVAEIAEELAT 3198
Cdd:COG3883 135 LEELKADKAELEAKKAELEAKLAELEAL-------KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
90 100
....*....|....*....|....*
gi 1720430018 3199 LPKRAQLAAAFITYLSAAPEGLRKN 3223
Cdd:COG3883 208 AEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3056-3223 |
2.01e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3056 KEIRESVEELlFKNKASFDPKNAKRASTAAAPLAAWVKANVQYSHVLERIQPLETEQSGLELNLKKTEDRKRKLEDL--- 3132
Cdd:COG4717 49 ERLEKEADEL-FKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlql 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3133 -------------LNSVGQKVSELKEKFQSRTS---EAAKLEAEVSKAQETIKAAEVL--------ISQLDREHRRWNAQ 3188
Cdd:COG4717 128 lplyqelealeaeLAELPERLEELEERLEELREleeELEELEAELAELQEELEELLEQlslateeeLQDLAEELEELQQR 207
|
170 180 190
....*....|....*....|....*....|....*
gi 1720430018 3189 VAEIAEELATLPKRAQLAAAFITYLSAAPEGLRKN 3223
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1689-1812 |
2.52e-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: 41.12 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1689 GPAGTGKTESVKALGGLL-GRQVLVFNCDE---------GIDVKSMGRIFVGLV-----KCGAWGCFDEFNRLEEAVLSA 1753
Cdd:pfam07728 6 GPPGTGKTELAERLAAALsNRPVFYVQLTRdtteedlfgRRNIDPGGASWVDGPlvraaREGEIAVLDEINRANPDVLNS 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720430018 1754 VSMQIQTiqdalkNHRTVCELLGKEVEINANSGIFITMNPAGKgygGRQKLPDNLKQLF 1812
Cdd:pfam07728 86 LLSLLDE------RRLLLPDGGELVKAAPDGFRLIATMNPLDR---GLNELSPALRSRF 135
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1688-1771 |
2.83e-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: 41.36 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 1688 YGPAGTGKTESVKALGGLLGRQ---VLVFNC--------DEGIDVKSMGRIFVGLVKCGAWGC--FDEFNRLEEAVLSAV 1754
Cdd:cd00009 25 YGPPGTGKTTLARAIANELFRPgapFLYLNAsdlleglvVAELFGHFLVRLLFELAEKAKPGVlfIDEIDSLSRGAQNAL 104
|
90
....*....|....*..
gi 1720430018 1755 SMQIQTIQDALKNHRTV 1771
Cdd:cd00009 105 LRVLETLNDLRIDRENV 121
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3109-3181 |
2.92e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 2.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720430018 3109 ETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLDRE 3181
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
1688-1728 |
3.17e-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: 41.11 E-value: 3.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720430018 1688 YGPAGTGKTESVKALGGLLGRQVLVFNCDEGIDV------KSMGRIF 1728
Cdd:cd19481 32 YGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKyvgeseKNLRKIF 78
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2933-3203 |
3.52e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2933 SALQEITVSMQDASEQKTEL----ERLKQRIAEEVVKIEERKSKIDDELKEVQPLVNEAKlAVGNIRPESLSEIRSLRmp 3008
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELreeiEELKEKRDELNEELKELAEKRDELNAQVKELREEAQ-ELREKRDELNEKVKELK-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3009 pDVIRDILEGVLRLMGIFDTswvsmksflakrgVREDIATFDARNIP-KEIRESVEELLFKNK-ASFDPKNAKRastaaa 3086
Cdd:COG1340 78 -EERDELNEKLNELREELDE-------------LRKELAELNKAGGSiDKLRKEIERLEWRQQtEVLSPEEEKE------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3087 plaawvkanvqyshVLERIQPLETE----QSGLELNLKKTEDRK--RKLEDLLNSVGQKVSELKEKFQ-------SRTSE 3153
Cdd:COG1340 138 --------------LVEKIKELEKElekaKKALEKNEKLKELRAelKELRKEAEEIHKKIKELAEEAQelheemiELYKE 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3154 AAKLEAEVSKAQETIKAAEVLISQLDREHRRWNAQVAEIAEELATLPKRA 3203
Cdd:COG1340 204 ADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQ 253
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1975-2013 |
3.94e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 42.91 E-value: 3.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1720430018 1975 VVIVGPSGAGKSTLWRMLrAALCKI--------GKVVKQytMNPK----AM 2013
Cdd:PRK11650 33 IVLVGPSGCGKSTLLRMV-AGLERItsgeiwigGRVVNE--LEPAdrdiAM 80
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3116-3215 |
4.12e-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: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3116 ELNLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLdrehrrwNAQVAEIAEE 3195
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-------EAEIEERREE 87
|
90 100
....*....|....*....|
gi 1720430018 3196 LATLPKRAQLAAAFITYLSA 3215
Cdd:COG3883 88 LGERARALYRSGGSVSYLDV 107
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1944-1996 |
4.98e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 41.87 E-value: 4.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1720430018 1944 KQVFEEANYEVIPNQMkkalelyeqlrqrtgVVIVGPSGAGKSTLWRMLRAAL 1996
Cdd:COG2401 43 RYVLRDLNLEIEPGEI---------------VLIVGASGSGKSTLLRLLAGAL 80
|
|
| 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
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
2885-2990 |
5.72e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.52 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2885 KKKELLKRQSHLQAGVSKLNEA-------KALVDELNRKAGEQSILLRIKQDEADSALQEITVSmqdASEQKTELERLKQ 2957
Cdd:pfam20492 7 EKQELEERLKQYEEETKKAQEEleeseetAEELEEERRQAEEEAERLEQKRQEAEEEKERLEES---AEMEAEEKEQLEA 83
|
90 100 110
....*....|....*....|....*....|....*.
gi 1720430018 2958 RIAE---EVVKIEERKSKIDDELKEVQPLVNEAKLA 2990
Cdd:pfam20492 84 ELAEaqeEIARLEEEVERKEEEARRLQEELEEAREE 119
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
3095-3172 |
6.29e-03 |
|
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: 41.11 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3095 NVQysHVLERIQPL----------ETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSEL-------KEKFQSRTSEAAKL 3157
Cdd:pfam05266 86 DVK--APQSRINKLlslkdrqtklLEELKKLEKKIAEEESEKRKLEEEIDELEKKILELerqlalaKEKKEAADKEIARL 163
|
90
....*....|....*
gi 1720430018 3158 EAEVSKAQETIKAAE 3172
Cdd:pfam05266 164 KSEAEKLEQEIQDVE 178
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2915-3209 |
7.05e-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: 42.74 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2915 RKAGEQSILLRikQDEADSALQEITVSMQDASEQKTELERLKQRIAEevvkIEERKSKIDDELKEVQPLVNEAKLAVGNI 2994
Cdd:TIGR02168 665 SAKTNSSILER--RREIEELEEKIEELEEKIAELEKALAELRKELEE----LEEELEQLRKELEELSRQISALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2995 RPES---LSEIRSLRMPPDVIRDILEGVLRLMGIFDTSWVSMKSFLAKrgVREDIATF-DARNIPKEIRESVEELLFKNK 3070
Cdd:TIGR02168 739 EAEVeqlEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE--LEAQIEQLkEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3071 ASFDpKNAKRASTAAAPLAAWVKANVQyshVLERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELKEkfqsr 3150
Cdd:TIGR02168 817 EEAA-NLRERLESLERRIAATERRLED---LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE----- 887
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3151 tsEAAKLEAEVSKAQETIKAAEVLISQLDREHRRWNAQVAEIAEELATLP-KRAQLAAAF 3209
Cdd:TIGR02168 888 --ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEvRIDNLQERL 945
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
2878-3006 |
8.09e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.54 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 2878 YSAISSSKKKELLKRQSHLQagvSKLNEAKALVDELNRkageqsillrIKQDEADSALQEITVSMQDASEQKTELERLKQ 2957
Cdd:smart00787 166 ELELLNSIKPKLRDRKDALE---EELRQLKQLEDELED----------CDPTELDRAKEKLKKLLQEIMIKVKKLEELEE 232
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1720430018 2958 RIAEEVVKIEERKSKID---DELKEVQPLVNEaklavgnIRPESLSEIRSLR 3006
Cdd:smart00787 233 ELQELESKIEDLTNKKSelnTEIAEAEKKLEQ-------CRGFTFKEIEKLK 277
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3076-3222 |
8.69e-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: 42.35 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3076 KNAKRASTAAAPLAAWVKANVQYSHVLERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAA 3155
Cdd:TIGR02168 219 KAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720430018 3156 KLEAEVSKAQETIKAAEVLISQLDREHRRWNAQVAEIAEELATLPKRAQLAAAFITYLSAAPEGLRK 3222
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3093-3278 |
9.78e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 9.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3093 KANVQYSHVLERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAE 3172
Cdd:COG4372 91 AAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430018 3173 VLISQLDREHRrwNAQVAEIAEELATLPKRAQLAAAFITYLSAAPEGLRKncLEEWTKAAGLEKFDLRRFLCTESEQLIW 3252
Cdd:COG4372 171 QELQALSEAEA--EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAE--ELLEAKDSLEAKLGLALSALLDALELEE 246
|
170 180
....*....|....*....|....*.
gi 1720430018 3253 KSEGLPSDDLSIENALVILQIIGLKS 3278
Cdd:COG4372 247 DKEELLEEVILKEIEELELAILVEKD 272
|
|
| |
