|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
89-415 |
0e+00 |
|
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: 651.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 89 YGYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSPKGPAGTGKTETVKDLGKALGIYVIVVNCSEGLDYKSMGRMYSG 168
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 169 LAQSGAWGCFDEFNRINIEVLSVVAQQILSILSALTANLTRFYFEGFEINLVWSCGIFITMNPGYAGRTELPENLKSMFR 248
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 249 PIAMVVPDSTLIAEIILFGEGFGNCKILAKKVYTLYSLAVQQLSRQDHYDFGLRALTSLLRYAGKKRRLQPDLSDEEVLL 328
Cdd:pfam12774 161 PVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 329 LSMRDMNIAKLTSVDVPLFNAIVQDLFPNIELPVIDYGKLRDTIEQEIREMGLQITPFTLTKVLQLYETKNSRHSTMIVG 408
Cdd:pfam12774 241 RALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVG 320
|
....*..
gi 1720366530 409 GTGSSKT 415
Cdd:pfam12774 321 PTGSGKT 327
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
2447-2747 |
9.22e-129 |
|
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: 407.01 E-value: 9.22e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 2447 ITEARTLFETLLSLQPQITPTRVGG-QSREEKVLELAADVKQKIPEMIDYE-GTRKLLALDPSPLNVVLLQEIQRYNKLM 2524
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGgSSREEIVLELAKDILEKLPEPFDIEeAEEKYPVGYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 2525 KTILFSLTDLEKGIQGLIVMSTSLEEIFNCIFDAHVPPLWGKV-YPSQKPLASWTRDLAVRVEQFETWASRARPPVLFWL 2603
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKsYPSLKPLGSWIRDLLERLKQLQDWLDDEGPPKVFWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 2604 SGFTFPTGFLTAVLQSAARQNNISVDSLSWEFIV-STVDDSNLVYPPKDGVWVRGLYLEGAGWDRKNSCLVEAEPMQLVC 2682
Cdd:pfam18199 161 SGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVtKKVSPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366530 2683 LMPTIHFRPAE-SRKKSAKGMYSCPCYYYPNRAGSTdrasFVIGIDLRSGsMTSDHWIKRGTALLM 2747
Cdd:pfam18199 241 PLPVIHLKPVEsDKKKLDENTYECPVYKTSERHSTN----FVFSVDLPTD-KPPDHWILRGVALLL 301
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
32-2432 |
6.40e-128 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 453.68 E-value: 6.40e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 32 KIVALVTIEIHARDVLEKLYKSGLMDVSSFDWLSQLRFYwEKDVDDCIIRQTNTQFQYGYEYLGNSGRLVITPLTDRCYM 111
Cdd:COG5245 860 RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELP-QGLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMDTSQHQ 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 112 TLTTALHLHRGGSpkgpAGTGKTETVKDLGKALGIYVivvncsEGLDYKSmgRMYSGLAQSGAWGcFDEFNRINIEVLSV 191
Cdd:COG5245 939 KLFEAVCDEVCRF----VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISRTI 1005
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 192 VA--QQILSILSALTANLTRFYFEGFeinLVWSCGIFITMNPgyagRTELPENLKSMFRPIAMVVPDSTlIAEIIlfgeg 269
Cdd:COG5245 1006 LVdeYLNSDEFRMLEELNSAVVEHGL---KSPSTPVEMIINE----RNIVLEIGRRALDMFLSNIPFGA-IKSRR----- 1072
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 270 fgncKILAKKVYTLYSLAVQQLSRQDHYDFglRALTSLLRyagKKRRLQPDLSDEEVLLLSmrdmnIAKLTSVDVPLFNA 349
Cdd:COG5245 1073 ----ESLDREIGAFNNEVDGIAREEDELMF--YPMFKSLK---AKHRMLEEKTEYLNKILS-----ITGLPLISDTLRER 1138
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 350 IvqDLFPNIELPVIdygklRDTIEQEIREMGlQITPFTLTKVLQLYETKNSRHSTMIVGGTGSSKTTSWKIlqasltslc 429
Cdd:COG5245 1139 I--DTLDAEWDSFC-----RISESLKKYESQ-QVSGLDVAQFVSFLRSVDTGAFHAEYFRVFLCKIKHYTD--------- 1201
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 430 ragepnyniVREFPLNPKALSLGELYGEYDLNTNEWTDGILSSVMRVACADEKpdeKWILFDGpvdtlWIESMNSVMDDN 509
Cdd:COG5245 1202 ---------ACDYLWHVKSPYVKKKYFDADMELRQFFLMFNREDMEARLADSK---MEYEVER-----YVEKTKAEVSSL 1264
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 510 KVLTLINGERIAMpeqvsllfeVENLAvASPATVSRCGMVYTDYVDLGWKPYVQSWL--EKRPKTEVEPLQRMFE----- 582
Cdd:COG5245 1265 KLELSSVGEGQVV---------VSNLG-SIGDKVGRCLVEYDSISRLSTKGVFLDELgdTKRYLDECLDFFSCFEevqke 1334
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 583 ------KFINKILSFKKDnCNELVPVPEYSGIISLCKLYTVLATPENGVNpADAENYSFMVEMTFVFSMIWSVCASVDED 656
Cdd:COG5245 1335 idelsmVFCADALRFSAD-LYHIVKERRFSGVLAGSDASESLGGKSIELA-AILEHKDLIVEMKRGINDVLKLRIFGDKC 1412
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 657 gRKKIDSYLREIEGSFPNKDTVYEYY---------VNPKMRTWTSFEEKLPKSWR--YPPNapfykIMVPTVDTVRYNYL 725
Cdd:COG5245 1413 -RESTPRFYLISDGDLIKDLNERSDYeemlimmfnISAVITNNGSIAGFELRGERvmLRKE-----VVIPTSDTGFVDSF 1486
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 726 VSTLVANQNPVLLVGPVGTGKTSIAQSVLQSlpSSQWSVLVVNMSAQTTSNNVQSIIESRVEK-RTKGVYVPFGG---KS 801
Cdd:COG5245 1487 SNEALNTLRSYIYCGPPGSGKEMLMCPSLRS--ELITEVKYFNFSTCTMTPSKLSVLERETEYyPNTGVVRLYPKpvvKD 1564
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 802 MITFMDDLNMPAKDMFGSQPPLELIR-LWIDYGFWYDrVKQSIKHIRDMFLMAAMGPPGG-GRTVISPRLQSRFNIINMT 879
Cdd:COG5245 1565 LVLFCDEINLPYGFEYYPPTVIVFLRpLVERQGFWSS-IAVSWVTICGIILYGACNPGTDeGRVKYYERFIRKPVFVFCC 1643
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 880 FPTESQIIRIFGTMINQKLQDFEEEVKPIGNVVTEATlDVYNTVVQRFlPTPAKIHYLFNLRDISKVFQGMLRANKDFHD 959
Cdd:COG5245 1644 YPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASV-ELYLSSKDKT-KFFLQMNYGYKPRELTRSLRAIFGYAETRID 1721
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 960 TK-ASITRLWIHECFRVFSDRLVDTADMEAFMGILSDKLGTFF-DLTFHHLcpNKRPPIFGDFLKEPKVYEDLVDLTVLk 1037
Cdd:COG5245 1722 TPdVSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIrEMIAGHI--GEAEITFSMILFFGMACLLKKDLAVF- 1798
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1038 taMETALNEYNLSPSVVPMqlVLFREAIEHITRIVRVIGQPRGNMLLVGIGGSGRQSLARLASSICDYNTFQIEVTKHYR 1117
Cdd:COG5245 1799 --VEEVRKIFGSSHLDVEA--VAYKDALLHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDEL 1874
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1118 KQEFRDDIKRLYRQAGVELQTTSFLFVDTQIADESFLEDINNILSSGEVPNLYKSDEFEEIQNHIIDQARAEQIP-ESSD 1196
Cdd:COG5245 1875 TGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFESTSLEkDTEA 1954
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1197 SLFAYLIERVRNNLHIVLCL-SPVGDPFRNWIRqYPALVNCTTINWFSEWPREALLEVAEKYI-----------IGVDLG 1264
Cdd:COG5245 1955 TLTRVFLVYMEENLPVVFSAcCSQDTSVLAGIR-SPALKNRCFIDFKKLWDTEEMSQYANSVEtlsrdggrvffINGELG 2033
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1265 TQE--NIHRKVAQIFVTMHWSVaqYSQKMLLELrryNYVTPTNYLELVSGYKKLLGEKRQELLDQANKLRTGLFKIDETR 1342
Cdd:COG5245 2034 VGKgaLISEVFGDDAVVIEGRG--FEISMIEGS---LGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYG 2108
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1343 EKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEEALPALEEA 1422
Cdd:COG5245 2109 RGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEA 2188
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1423 MRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMILRGNEPT-WAEAKRQLGEQNFIKSLINFDKD-NISDKVLKKIGA-Y 1499
Cdd:COG5245 2189 VLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLLGFEAKiWFGEQQSLRRDDFIRIIGKYPDEiEFDLEARRFREArE 2268
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1500 CAQPDFQPDIIGRVSLAAKSLCMWVRAMELYGRLYRVVEPKRIRMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQY 1579
Cdd:COG5245 2269 CSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYY 2348
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1580 DEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDLGYLVGDCLIAAAFLSYMGPFLTNYRDEIINQ 1659
Cdd:COG5245 2349 SLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGM 2428
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1660 IWIRKIRELQVPCSPRFA-IDNFLTNPTKVRDWNIQglpSDAFSTENGIIVTRGNRWALMIDPQGQALKWIKNMEGNQGL 1738
Cdd:COG5245 2429 SFIRISKEFRDKEIRRRQfITEGVQKIEDFKEEACS---TDYGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKA 2505
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1739 KIIDLQMHDYLRVLEHAIQFGFPVLLQnVQEYLDPTLNPVLNKSVARIGGRMLIRIGDKEVEYNPNFR-FYLTTKLSNPH 1817
Cdd:COG5245 2506 ILGSFREMEFAFGLSQARREGSDKIIG-DAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAvFWLSEGRSGDM 2584
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1818 YNPEtSAKTTIVNFAVKEQGLEAQLLGIVVRKERPELEEQKDSLVINIAAGKRKLKELEDEILRLLNEATGSLLDDVQLV 1897
Cdd:COG5245 2585 GSIE-WKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIA 2663
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1898 NTLQTSKITATEVTEQLETSETTEINIDLAREAYRPCAQRASVLFFVLNDMGRIDPMYQFSldayIGLFILSIDKSHRSN 1977
Cdd:COG5245 2664 VLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKS----ICELSSEFEKWRRMK 2739
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1978 KLE-DRIEYLNDYHTYAVYrYTCRTLFErHKLLFSFHMCAKIletsgklnmdeynfFLRGGVVLDREGQMDNPCTSWLAD 2056
Cdd:COG5245 2740 SKYlCAIRYMLMSSEWILD-HEDRSGFI-HRLDVSFLLRTKR--------------FVSTLLEDKNYRQVLSSCSLYGND 2803
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 2057 AYWDNITELDKLTNFhglMNSFEQYPRDWHLWYTNSSpekamlpgewenACNEMQRMLIVRSLRQ-DRVAFcvtsfivSN 2135
Cdd:COG5245 2804 VISHSCDRFDRDVYR---ALKHQMDNRTHSTILTSNS------------KTNPYKEYTYNDSWAEaFEVED-------SG 2861
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 2136 LGSRFieppvlnMKSVMEDSTPRSPLVFILSPGVDptsaLLQLAEHTGMAHRfhaLSLGQGQAPIAARllregvnQGHWV 2215
Cdd:COG5245 2862 DLYKF-------EEGLLELIVGHAPLIYAHKKSLE----NERNVDRLGSKEN---EVYAVLNSLFSRK-------EKSWF 2920
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 2216 FLANCHLSLSWMPN-LDKLVEQLQVEDPHPSF-RLWLSSSPHPDFPISILQASIKMTTEPPKGLKANMTRLYQLMteaQF 2293
Cdd:COG5245 2921 EVYNISLSFGWFKRyVEDVVYPIKASRVCGKVkNMWTSMVDADMLPIQLLIAIDSFVSSTYPETGCGYADLVEID---RY 2997
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 2294 THCSKPAKYKKLLFALCFFHSILLERKKFLQLGWNIIYGFNDSDFEVSENLLS--LYLDEYEETPWDALKYLIAGVNYGG 2371
Cdd:COG5245 2998 PFDYTLVIACDDAFYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKniLFLNHLNARKWGNNRDLIFTIVYGK 3077
|
2410 2420 2430 2440 2450 2460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720366530 2372 HVTDDWDRRLLTTYINDYFC--DLSLTTPFYRLS-VLDTYYIPKDGSLASYKEYISMLPSMDPP 2432
Cdd:COG5245 3078 KHSLMEDSKVVDKYCRGYGAheTSSQILASVPGGdPELVKFHMEEMCRSSAFGVIGQLPDLALC 3141
|
|
| AAA_8 |
pfam12780 |
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
1056-1316 |
9.75e-128 |
|
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: 401.99 E-value: 9.75e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1056 MQLVLFREAIEHITRIVRVIGQPRGNMLLVGIGGSGRQSLARLASSICDYNTFQIEVTKHYRKQEFRDDIKRLYRQAGVE 1135
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1136 LQTTSFLFVDTQIADESFLEDINNILSSGEVPNLYKSDEFEEIQNHIIDQARAEQIPESSDSLFAYLIERVRNNLHIVLC 1215
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1216 LSPVGDPFRNWIRQYPALVNCTTINWFSEWPREALLEVAEKYIigVDLGTQENIHRKVAQIFVTMHWSVAQYSQKMLLEL 1295
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFL--EDIEIPEELKSNVVKVFVYVHSSVEDMSKKFYEEL 238
|
250 260
....*....|....*....|.
gi 1720366530 1296 RRYNYVTPTNYLELVSGYKKL 1316
Cdd:pfam12780 239 KRKNYVTPKSYLELLRLYKNL 259
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
1689-1910 |
3.83e-126 |
|
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: 396.04 E-value: 3.83e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1689 RDWNIQGLPSDAFSTENGIIVTRGNRWALMIDPQGQALKWIKNMEGNQGLKIIDLQMHDYLRVLEHAIQFGFPVLLQNVQ 1768
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1769 EYLDPTLNPVLNKSVARIGGRMLIRIGDKEVEYNPNFRFYLTTKLSNPHYNPETSAKTTIVNFAVKEQGLEAQLLGIVVR 1848
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720366530 1849 KERPELEEQKDSLVINIAAGKRKLKELEDEILRLLNEATGSLLDDVQLVNTLQTSKITATEV 1910
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
703-881 |
1.34e-103 |
|
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: 329.35 E-value: 1.34e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 703 YPPNAPFYKIMVPTVDTVRYNYLVSTLVANQNPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSII 782
Cdd:pfam12775 1 IPPDVPFSEILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPLFINFSAQTTSNQTQDII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 783 ESRVEKRTKGVYVPFGGKSMITFMDDLNMPAKDMFGSQPPLELIRLWIDYGFWYDRVKQSIKHIRDMFLMAAMGPPGGGR 862
Cdd:pfam12775 81 ESKLEKRRKGVYGPPGGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKLTFKEIVDVQFVAAMGPPGGGR 160
|
170
....*....|....*....
gi 1720366530 863 TVISPRLQSRFNIINMTFP 881
Cdd:pfam12775 161 NDITPRLLRHFNVFNITFP 179
|
|
| AAA_lid_11 |
pfam18198 |
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the ... |
2302-2441 |
2.92e-73 |
|
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: 240.82 E-value: 2.92e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 2302 YKKLLFALCFFHSILLERKKFLQLGWNIIYGFNDSDFEVSENLLSLYLDEY-EETPWDALKYLIAGVNYGGHVTDDWDRR 2380
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLDEYdEKIPWDALRYLIGEINYGGRVTDDWDRR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720366530 2381 LLTTYINDYFCDlSLTTPFYRLSVlDTYYIPKDGSLASYKEYISMLPSMDPPEAFGQHPNA 2441
Cdd:pfam18198 81 LLNTYLEEFFNP-EVLEEDFKFSP-SLYYIPPDGDLEDYLEYIESLPLVDSPEVFGLHPNA 139
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
2156-2270 |
4.60e-64 |
|
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: 213.46 E-value: 4.60e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 2156 TPRSPLVFILSPGVDPTSALLQLAEHTGMAHRFHALSLGQGQAPIAARLLREGVNQGHWVFLANCHLSLSWMPNLDKLVE 2235
Cdd:pfam03028 1 SPTTPLIFILSPGSDPTADLEKLAKKLGFGGKLHSISLGQGQGPIAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKILE 80
|
90 100 110
....*....|....*....|....*....|....*
gi 1720366530 2236 QLQVEDPHPSFRLWLSSSPHPDFPISILQASIKMT 2270
Cdd:pfam03028 81 ELPEETLHPDFRLWLTSEPSPKFPISILQNSIKIT 115
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
1330-1662 |
1.82e-57 |
|
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: 203.77 E-value: 1.82e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1330 KLRTGLFKIDETREKVEvmsleleDAKKKVA----EFQKQCE--EYLVIIVQQKREADEQQKAVTANSE-KIAIEEVKCQ 1402
Cdd:pfam12777 2 RLENGLLKLHSTAAQVD-------DLKAKLAaqeaELKQKNEdaDKLIQVVGIEADKVSKEKAIADEEEqKVAVIMKEVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1403 ALADNAQKDLEEALPALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMIL---RGNEP---TWAEAKRQLGE-QN 1475
Cdd:pfam12777 75 EKQKACEEDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILmapGGKIPkdkSWKAAKIMMAKvDG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1476 FIKSLINFDKDNISDKVLKKIGAYCAQPDFQPDIIGRVSLAAKSLCMWVRAMELYGRLYRVVEPKRIRMNAAMAQLQEKQ 1555
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1556 AALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDLGYLVGDC 1635
Cdd:pfam12777 235 EKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDI 314
|
330 340
....*....|....*....|....*..
gi 1720366530 1636 LIAAAFLSYMGPFLTNYRDEIINQIWI 1662
Cdd:pfam12777 315 LLISAFISYLGFFTKKYRNELLDKFWI 341
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
577-695 |
9.62e-32 |
|
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA domain 5 in the dynein heavy chain. This domain is composed of 8 alpha helices.
Pssm-ID: 465532 [Multi-domain] Cd Length: 126 Bit Score: 121.62 E-value: 9.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 577 LQRMFEKFINKILSFKKDNCNELVPVPEYSGIISLCKLYTVLATP---ENGVNPADAENYSFMVEMTFVFSMIWSVCASV 653
Cdd:pfam17852 1 LEPLFEWLVPPALEFVRKNCKEIVPTSDLNLVQSLCRLLESLLDEvleYNGVHPLSPDKLKEYLEKLFLFALVWSIGGTL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1720366530 654 DEDGRKKIDSYLREIEGS----FPNKDTVYEYYVNPKMRTWTSFEE 695
Cdd:pfam17852 81 DEDSRKKFDEFLRELFSGldlpPPEKGTVYDYFVDLEKGEWVPWSD 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
735-873 |
3.39e-25 |
|
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: 103.14 E-value: 3.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 735 PVLLVGPVGTGKTSIAQSVLQSLpsSQWSVLVVNMSAQTTSNNVQSIIESRVE--KRTKGVYVPFGGKSMITFMDDLNMP 812
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAL--SNRPVFYVQLTRDTTEEDLFGRRNIDPGgaSWVDGPLVRAAREGEIAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720366530 813 AKDMFGSQ-PPLELIRLWIDYGFWYDRVKQSikhirDMFLMAAMGPPGGGRTVISPRLQSRF 873
Cdd:pfam07728 79 NPDVLNSLlSLLDERRLLLPDGGELVKAAPD-----GFRLIATMNPLDRGLNELSPALRSRF 135
|
|
| AAA_lid_1 |
pfam17857 |
AAA+ lid domain; This domain represents the AAA lid domain from dynein heavy chain D3. |
914-1002 |
2.04e-17 |
|
AAA+ lid domain; This domain represents the AAA lid domain from dynein heavy chain D3.
Pssm-ID: 465535 [Multi-domain] Cd Length: 100 Bit Score: 79.59 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 914 EATLDVYNTVVQRFLPTPAKIHYLFNLRDISKVFQGMLRANKDFHDTKASITRLWIHECFRVFSDRLVDTADMEAFMGIL 993
Cdd:pfam17857 3 AAALAFHQKIAATFLPTAIKFHYIFNLRDFANIFQGILFSSAECLKSPLDLIRLWLHESERVYGDKMVDEKDFDLFDKIQ 82
|
....*....
gi 1720366530 994 SDKLGTFFD 1002
Cdd:pfam17857 83 MASLKKFFD 91
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
734-876 |
4.30e-09 |
|
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: 57.54 E-value: 4.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 734 NPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKGVYVPfgGKSMITFMDDLNMPA 813
Cdd:cd00009 20 KNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEK--AKPGVLFIDEIDSLS 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720366530 814 KDMFGSQppLELIRLWIDYGFWYDRVKqsikhirdmFLMAAMGPPGGGrtvISPRLQSRFNII 876
Cdd:cd00009 98 RGAQNAL--LRVLETLNDLRIDRENVR---------VIGATNRPLLGD---LDRALYDRLDIR 146
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1337-1627 |
1.76e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1337 KIDETREKVEVMSLELEDAKKKVAEFQKQCEEylviivqqKREADEQQKavTANSEKIAIEEVKCQAL----ADNAQKDL 1412
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE--------KKKADEAKK--KAEEDKKKADELKKAAAakkkADEAKKKA 1427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1413 EEALPAlEEAMRALESLNKKDigEIKSYGRPPAQVEivmqavmilrgNEPTWAEAKRQLGEqnfIKSliNFDKDNISDKV 1492
Cdd:PTZ00121 1428 EEKKKA-DEAKKKAEEAKKAD--EAKKKAEEAKKAE-----------EAKKKAEEAKKADE---AKK--KAEEAKKADEA 1488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1493 LKKigayCAQPDFQPDIIGRVSLAAKslcmwvRAMELygrlyRVVEPKRIRMNAAMAQLQEKQAALAEAQEKLR-EVAEK 1571
Cdd:PTZ00121 1489 KKK----AEEAKKKADEAKKAAEAKK------KADEA-----KKAEEAKKADEAKKAEEAKKADEAKKAEEKKKaDELKK 1553
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366530 1572 LEMLKKQydEKLAQKEELRKKSEEMELKLERAGMLVSglaGEKARWEETVQGLEED 1627
Cdd:PTZ00121 1554 AEELKKA--EEKKKAEEAKKAEEDKNMALRKAEEAKK---AEEARIEEVMKLYEEE 1604
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1262-1595 |
1.78e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.04 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1262 DLGTQ-ENihRKVAQIFVTMHwsvaqySQKMLLELRRYNYVTPTNYLELvsgykkllgEKRQELLDQANKLRTGLFKIDE 1340
Cdd:pfam05483 475 DLKTElEK--EKLKNIELTAH------CDKLLLENKELTQEASDMTLEL---------KKHQEDIINCKKQEERMLKQIE 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1341 TREKVEvMSL--ELEDAKKkvaEFQKQCEEYLVIIVQQKREADEQQKAVTANSEKIAIEEVKCqalaDNAQKDLEEALPA 1418
Cdd:pfam05483 538 NLEEKE-MNLrdELESVRE---EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC----NNLKKQIENKNKN 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1419 LEEAMRALESLNKKDIGEIKsygrppaQVEIVMQAVMILrgnEPTWAEAKRQLGE--QNFIKSLInfDKDNISDKVLKKI 1496
Cdd:pfam05483 610 IEELHQENKALKKKGSAENK-------QLNAYEIKVNKL---ELELASAKQKFEEiiDNYQKEIE--DKKISEEKLLEEV 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1497 GAYCAQPD----FQPDIIGRVSlaaKSLCMWVRAMELYGRLY-RVVEPKRIRMNAAMAQLQEKQAALAEAQEKLREVAEK 1571
Cdd:pfam05483 678 EKAKAIADeavkLQKEIDKRCQ---HKIAEMVALMEKHKHQYdKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAE 754
|
330 340
....*....|....*....|....
gi 1720366530 1572 LEMLKKQYDEKLAQKEELRKKSEE 1595
Cdd:pfam05483 755 LLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1337-1628 |
3.55e-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: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1337 KIDETREKVEVMSLELEDAKKkVAEFQKQCEEY-LVIIVQQKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEEA 1415
Cdd:TIGR02169 192 IIDEKRQQLERLRREREKAER-YQALLKEKREYeGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1416 LPALEEAMRALESLN-------KKDIGEIKsygrppAQVEivmQAVMILRGNEptwAEAKRQLGEQNFIKSLINFDKDNI 1488
Cdd:TIGR02169 271 EQLLEELNKKIKDLGeeeqlrvKEKIGELE------AEIA---SLERSIAEKE---RELEDAEERLAKLEAEIDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1489 sDKVLKKIGAYCAQpdfqpdiigRVSLAAKslcmwvramelygrlyrvVEPKRIRMNAAMAQLQEKQAALAEAQEKLREV 1568
Cdd:TIGR02169 339 -EELEREIEEERKR---------RDKLTEE------------------YAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1569 AEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDL 1628
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1317-1631 |
2.93e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1317 LGEKRQELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL--VIIVQQKREADEQQKAVTANSEKI 1394
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkrLEELEERHELYEEAKAKKEELERL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1395 AiEEVKCQALaDNAQKDLEEALPALEEAMRALESLNKKdIGEIKSygrppaQVEIVMQAVMILRGNEPTWAEAKRQLGEQ 1474
Cdd:PRK03918 378 K-KRLTGLTP-EKLEKELEELEKAKEEIEEEISKITAR-IGELKK------EIKELKKAIEELKKAKGKCPVCGRELTEE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1475 nfikslinfDKDNISDKVLKKIGaycaqpDFQPDIIgrvSLAAKSLCMWVRAMELYGRLYRvvEPKRIRMNAAMAQLQEK 1554
Cdd:PRK03918 449 ---------HRKELLEEYTAELK------RIEKELK---EIEEKERKLRKELRELEKVLKK--ESELIKLKELAEQLKEL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1555 QAALAEAQ-EKLREVAEKLEMLKKQYD----------EKLAQKEELRKKSEEMELKLERAGMLVSGLAGE-KARWEETVQ 1622
Cdd:PRK03918 509 EEKLKKYNlEELEKKAEEYEKLKEKLIklkgeikslkKELEKLEELKKKLAELEKKLDELEEELAELLKElEELGFESVE 588
|
....*....
gi 1720366530 1623 GLEEDLGYL 1631
Cdd:PRK03918 589 ELEERLKEL 597
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1338-1602 |
3.84e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1338 IDETREKVEVMSLELEDAKKKVAEFQKQCE--EYLVII------VQQKREADEQ---QKAVTANSEKIAIEEVKCQA--L 1404
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLEraEDLVEAedrierLEERREDLEEliaERRETIEEKRERAEELRERAaeL 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1405 ADNAQKDLEEALPALEEAMRALE---SLNKKdIGEIKSYGRPPAQVEIVMQAVMILRGNEPTWAEAKRQLGEQNfiksli 1481
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREevaELNSK-LAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELN------ 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1482 NFDKDNISDKVLKKigaycaqpdfqpdiigrVSLAAKslcmwvramelygrlyrvVEPKRIrmNAAMAQLQEKQAALAEA 1561
Cdd:PRK02224 623 DERRERLAEKRERK-----------------RELEAE------------------FDEARI--EEAREDKERAEEYLEQV 665
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1720366530 1562 QEKLREVAEKLEMLKKQ---YDEKLAQKEELRKKSEEMELKLER 1602
Cdd:PRK02224 666 EEKLDELREERDDLQAEigaVENELEELEELRERREALENRVEA 709
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1294-1438 |
5.02e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1294 ELRRYNYVTPTNYLELVSGYKKLLGE---KRQELLDQANKLRtglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL 1370
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEeakKAEEAKIKAEELK----KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366530 1371 VIIVQQKREADEQQKAVtansekiaiEEVKcqaLADNAQKDLEEALPALEEAMRALESLNKKDIGEIK 1438
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKA---------EEAK---KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1322-1432 |
9.17e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.29 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1322 QELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQQKAVTANSEKIaieeVKC 1401
Cdd:COG1340 146 EKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEI----VEA 221
|
90 100 110
....*....|....*....|....*....|.
gi 1720366530 1402 QALADNAQKDLEEALPALEEAMRALESLNKK 1432
Cdd:COG1340 222 QEKADELHEEIIELQKELRELRKELKKLRKK 252
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
126-247 |
9.90e-06 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 47.29 E-value: 9.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 126 KGPAGTGKTETVKDLGKALGIY-VIVVNCSE---------GLDYKSMG--RMYSGL---AQSGAWGCFDEFNRINIEVLS 190
Cdd:pfam07728 5 VGPPGTGKTELAERLAAALSNRpVFYVQLTRdtteedlfgRRNIDPGGasWVDGPLvraAREGEIAVLDEINRANPDVLN 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720366530 191 VVaqqiLSILSA----LTANLTRFYFEGFEINLVwscgifITMNPGYAGRTELPENLKSMF 247
Cdd:pfam07728 85 SL----LSLLDErrllLPDGGELVKAAPDGFRLI------ATMNPLDRGLNELSPALRSRF 135
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1317-1610 |
1.16e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1317 LGEKRQELLDQANKLRTGLF----KIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVII---VQQKREADEQQKAVTA 1389
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEeltaELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsrlEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1390 NSEKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKKdigeiksygrppaqveivmqavmiLRGNEPTWAEAKR 1469
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE------------------------LEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1470 QLGEQNfiKSLINFDKDniSDKVLKKIGAycaqpdfqpdIIGRVSLAAKSLCMWVRAMElygRLYRVVE-----PKRIRM 1544
Cdd:TIGR02168 373 RLEELE--EQLETLRSK--VAQLELQIAS----------LNNEIERLEARLERLEDRRE---RLQQEIEellkkLEEAEL 435
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366530 1545 NAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKlaqKEELRKKSEEMELKLERAGMLVSGL 1610
Cdd:TIGR02168 436 KELQAELEELEEELEELQEELERLEEALEELREELEEA---EQALDAAERELAQLQARLDSLERLQ 498
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
1543-1603 |
1.29e-05 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 46.42 E-value: 1.29e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720366530 1543 RMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYD---EKLA-QKEELRKKSEEMELKLERA 1603
Cdd:pfam18595 51 KLEEAKKKLKELRDALEEKEIELRELERREERLQRQLEnaqEKLErLREQAEEKREAAQARLEEL 115
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1307-1637 |
1.85e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1307 LELVSGYKKLLGEKRQELLDQANKLRTglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL-VIIVQQKREADEQQK 1385
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEA---ELEELRLELEELELELEEAQAEEYELLAELARLEqDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1386 AVTANSEKIAIEEV--KCQALADNAQKDLEEALPALEEAMRALESLNKkdigeiksygrppAQVEIVMQAVMILRGNEPT 1463
Cdd:COG1196 318 LEELEEELAELEEEleELEEELEELEEELEEAEEELEEAEAELAEAEE-------------ALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1464 WAEAKRQLGEQNFIKSLINFDKDNISDKVLKKIgaycaqpdfqpdiigrvslaakslcmwvRAMELYGRLYRVVEPKRIR 1543
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLE----------------------------RLEEELEELEEALAELEEE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1544 MNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQG 1623
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
330
....*....|....
gi 1720366530 1624 LEEDLGYLVGDCLI 1637
Cdd:COG1196 517 AGLRGLAGAVAVLI 530
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1543-1601 |
1.96e-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: 48.38 E-value: 1.96e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720366530 1543 RMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLA----QKEELRKKSEEMELKLE 1601
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAeleaELEELEAEREELAAKIP 173
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1319-1627 |
3.24e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1319 EKRQELLDQANKLRTGlfKIDETREKVEVMSlELEDAKK-----------KVAEFQKQCEEYLVII---VQQKREADEQQ 1384
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETG--KAEEARKAEEAKK-KAEDARKaeearkaedarKAEEARKAEDAKRVEIarkAEDARKAEEAR 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1385 KAVTA---NSEKIAIEEVKCQAL--ADNAQKdLEEALPA-----LEEAMRALESlnkKDIGEIKSYGRPPAQVEIVMQAV 1454
Cdd:PTZ00121 1171 KAEDAkkaEAARKAEEVRKAEELrkAEDARK-AEAARKAeeerkAEEARKAEDA---KKAEAVKKAEEAKKDAEEAKKAE 1246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1455 MIlRGNEPTWAEAKRQLGEQNFIKSLINFDKDNISDKVLKKIGAYCAQPDFQPDIIGRVSLAAKSLCMWVRAMELYGRly 1534
Cdd:PTZ00121 1247 EE-RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKK-- 1323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1535 rvVEPKRIRMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLEragmlvsglagEK 1614
Cdd:PTZ00121 1324 --AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-----------EK 1390
|
330
....*....|...
gi 1720366530 1615 ARWEETVQGLEED 1627
Cdd:PTZ00121 1391 KKADEAKKKAEED 1403
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1317-1628 |
3.26e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1317 LGEKRQELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEyLVIIVQQKREADEQQKAVTANSEKIAI 1396
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS-LERLQENLEGFSEGVKALLKNQSGLSG 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1397 EEvkcQALAD--NAQKDLEEALP-ALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMILRGNEPTWAEAKRQLGE 1473
Cdd:TIGR02168 521 IL---GVLSEliSVDEGYEAAIEaALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNI 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1474 QNFIKSLINFDKdnisdkvlkkigaycAQPDFQPDIIGRVS--LAAKSLcmwVRAMELYGRL---YRVVEP--KRIRMNA 1546
Cdd:TIGR02168 598 EGFLGVAKDLVK---------------FDPKLRKALSYLLGgvLVVDDL---DNALELAKKLrpgYRIVTLdgDLVRPGG 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1547 AMAQLQEKQAALAEAQEK-LREVAEKLEMLKKQYDEKLAQKEELRKKSEEME-------LKLERAGMLVSGLAGEKARWE 1618
Cdd:TIGR02168 660 VITGGSAKTNSSILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEeeleqlrKELEELSRQISALRKDLARLE 739
|
330
....*....|
gi 1720366530 1619 ETVQGLEEDL 1628
Cdd:TIGR02168 740 AEVEQLEERI 749
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1319-1425 |
3.58e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.03 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1319 EKRQELLDQANKLRtglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQ-KREADEQQKAVTANSEKIAiE 1397
Cdd:PRK09510 91 ELQQKQAAEQERLK----QLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAaKAKAEAEAKRAAAAAKKAA-A 165
|
90 100
....*....|....*....|....*...
gi 1720366530 1398 EVKCQALADNAQKDLEEALPALEEAMRA 1425
Cdd:PRK09510 166 EAKKKAEAEAAKKAAAEAKKKAEAEAAA 193
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1337-1622 |
5.02e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1337 KIDETREKVEVMSLELEDAKKKVAEFQKQceeylviIVQQKREADEQQKAVTANSEKIaieevkcqalaDNAQKDLEEAL 1416
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAE-------LEELNEEYNELQAELEALQAEI-----------DKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1417 PALEEAMRALeslnKKDIGEIKSYGRPPAQVEIVMQAvmilrgneptwaeakrqlgeqnfikslinfdkDNISDkVLKKI 1496
Cdd:COG3883 79 AEIEERREEL----GERARALYRSGGSVSYLDVLLGS--------------------------------ESFSD-FLDRL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1497 GAYCAQPDFQPDIIGRVslaakslcmwvramelygrlyrvvepkrirmNAAMAQLQEKQAALAEAQEKLREVAEKLEMLK 1576
Cdd:COG3883 122 SALSKIADADADLLEEL-------------------------------KADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1720366530 1577 KQYDEKLAQKEELRK--KSEEMELKLERAGMLVSGLAGEKARWEETVQ 1622
Cdd:COG3883 171 AELEAQQAEQEALLAqlSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1543-1628 |
5.69e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1543 RMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQ 1622
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE 160
|
....*.
gi 1720366530 1623 GLEEDL 1628
Cdd:COG4372 161 SLQEEL 166
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1546-1628 |
6.27e-05 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 44.94 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1546 AAMAQLQE---KQAALA-EAQEKL-REV------AEKLEMLKKQYdeklaqkEELRKKSEEMELKLERAgmlVSGLAGEK 1614
Cdd:pfam07926 22 AQLQKLQEdleKQAEIArEAQQNYeRELvlhaedIKALQALREEL-------NELKAEIAELKAEAESA---KAELEESE 91
|
90
....*....|....
gi 1720366530 1615 ARWEETVQGLEEDL 1628
Cdd:pfam07926 92 ESWEEQKKELEKEL 105
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1319-1619 |
9.75e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 9.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1319 EKRQELLDQANKLRTglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYlviivqqKREADEQQKAVTANSEKIaiEE 1398
Cdd:COG1340 29 EKRDELNEELKELAE---KRDELNAQVKELREEAQELREKRDELNEKVKEL-------KEERDELNEKLNELREEL--DE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1399 VKcqALADNAQKDLEEaLPALEEAMRALE------SLNKKD----IGEIKSYGRppaQVEIVMQAVmilrgneptwaEAK 1468
Cdd:COG1340 97 LR--KELAELNKAGGS-IDKLRKEIERLEwrqqteVLSPEEekelVEKIKELEK---ELEKAKKAL-----------EKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1469 RQLGE-QNFIKSLinfdKDNISDkVLKKIGAYCAQpdfqpdiIGRVSLAAKSLcmwvramelygrlYRVVEPKRIRMNAA 1547
Cdd:COG1340 160 EKLKElRAELKEL----RKEAEE-IHKKIKELAEE-------AQELHEEMIEL-------------YKEADELRKEADEL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1548 MAQLQEKQAALAE-------AQEKLREVAEKLEMLKKQYD--EKLAQKEELRKKSEEMELKLERagmlvsglaGEKARWE 1618
Cdd:COG1340 215 HKEIVEAQEKADElheeiieLQKELRELRKELKKLRKKQRalKREKEKEELEEKAEEIFEKLKK---------GEKLTTE 285
|
.
gi 1720366530 1619 E 1619
Cdd:COG1340 286 E 286
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1376-1628 |
9.78e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 9.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1376 QKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKkdigEIKSygrppAQVEIvmqavm 1455
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA----EIAE-----AEAEI------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1456 ilrgneptwAEAKRQLGEQnfIKSLinfdkdNISDKVLKKIGAYCAQPDFQpDIIGRVSLaakslcmwvramelygrLYR 1535
Cdd:COG3883 82 ---------EERREELGER--ARAL------YRSGGSVSYLDVLLGSESFS-DFLDRLSA-----------------LSK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1536 VVEpkriRMNAAMAQLQEKQAALAEAQEKLREVAEKLEmlkkqydeklAQKEELRKKSEEMELKLERAGMLVSGLAGEKA 1615
Cdd:COG3883 127 IAD----ADADLLEELKADKAELEAKKAELEAKLAELE----------ALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
250
....*....|...
gi 1720366530 1616 RWEETVQGLEEDL 1628
Cdd:COG3883 193 AAEAQLAELEAEL 205
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1543-1628 |
1.00e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1543 RMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQ 1622
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
....*.
gi 1720366530 1623 GLEEDL 1628
Cdd:COG1196 313 ELEERL 318
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
734-792 |
1.70e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 44.29 E-value: 1.70e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366530 734 NPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKG 792
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASG 61
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1315-1601 |
1.72e-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: 46.87 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1315 KLLGEKRQELLDQANKLRTGLFkiDETREKVEVMSLELEDAKKKVAEFQKQCEEYL--VIIVQQKREADEQQKAVTANSE 1392
Cdd:COG5185 249 AQTSDKLEKLVEQNTDLRLEKL--GENAESSKRLNENANNLIKQFENTKEKIAEYTksIDIKKATESLEEQLAAAEAEQE 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1393 KI-AIEEV-----KCQALADNAQKDLEEALPALEEAMRALE-----SLNKKDIGEIKSygrppaQVEIVMQAVMILRGNe 1461
Cdd:COG5185 327 LEeSKRETetgiqNLTAEIEQGQESLTENLEAIKEEIENIVgevelSKSSEELDSFKD------TIESTKESLDEIPQN- 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1462 ptwAEAKRQLGEQNFIKSLINFDKDnisdkvLKKIGAYCAQPDFQPDIIGRVSLAAKSlcmwvramelygrlyRVVEPKR 1541
Cdd:COG5185 400 ---QRGYAQEILATLEDTLKAADRQ------IEELQRQIEQATSSNEEVSKLLNELIS---------------ELNKVMR 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720366530 1542 IRMNAAMAQLQEKQAALA-EAQEKLREVAEKLEMLKkqyDEKLAQKEELRKKSEEMELKLE 1601
Cdd:COG5185 456 EADEESQSRLEEAYDEINrSVRSKKEDLNEELTQIE---SRVSTLKATLEKLRAKLERQLE 513
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1541-1619 |
2.83e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.68 E-value: 2.83e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366530 1541 RIRMNAAMAQLQEKQaaLAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAgmlvsglAGEKARWEE 1619
Cdd:pfam13868 100 REQMDEIVERIQEED--QAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEY-------LKEKAEREE 169
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1522-1604 |
3.37e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 45.80 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1522 MWVRAMELY-GRLYRVVEPKRIRMNAAMAQLQEKQAALAEAQEKLREvaEKLE------MLKKQYDEK-LAQKEELRKK- 1592
Cdd:pfam15558 62 QWQAEKEQRkARLGREERRRADRREKQVIEKESRWREQAEDQENQRQ--EKLErarqeaEQRKQCQEQrLKEKEEELQAl 139
|
90
....*....|....*.
gi 1720366530 1593 --SEEMEL--KLERAG 1604
Cdd:pfam15558 140 reQNSLQLqeRLEEAC 155
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1549-1628 |
4.02e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1549 AQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDL 1628
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1314-1432 |
5.34e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 44.84 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1314 KKLLGEKRQELLDQANKLRtglfKIDETREKV--EVMSLELEDAKKKVAEFQKQCEEylviivQQKREADEQQKAVTANS 1391
Cdd:TIGR02794 71 KKLEQQAEEAEKQRAAEQA----RQKELEQRAaaEKAAKQAEQAAKQAEEKQKQAEE------AKAKQAAEAKAKAEAEA 140
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1720366530 1392 EKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKK 1432
Cdd:TIGR02794 141 ERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKA 181
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1540-1667 |
5.68e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.91 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1540 KRIRMNAAMAQLQEKQAAL---AEAQEKLREVAEKLEMLKKQ-YDEKLAQKEELRKKSEEMELKLERAGMLVsglAGEKA 1615
Cdd:pfam13868 229 KKARQRQELQQAREEQIELkerRLAEEAEREEEEFERMLRKQaEDEEIEQEEAEKRRMKRLEHRRELEKQIE---EREEQ 305
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1720366530 1616 RWEETVQGLEEdlgylvGDCLIAAAflsymgpfltNYRDEIINQIWIRKIRE 1667
Cdd:pfam13868 306 RAAEREEELEE------GERLREEE----------AERRERIEEERQKKLKE 341
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1319-1628 |
5.87e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1319 EKRQELLDQANKLRTGLFKIDETREKVEvmslELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQ-QKAVTANSEKIAIE 1397
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEE----ELEELEAELAELQEELEELLEQLSLATEEELQDlAEELEELQQRLAEL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1398 EVKcQALADNAQKDLEEALPALEEAMRALESLNKKD---------------IGEIKSYGRPPAQVEIVMQAVMILRGNEP 1462
Cdd:COG4717 212 EEE-LEEAQEELEELEEELEQLENELEAAALEERLKearlllliaaallalLGLGGSLLSLILTIAGVLFLVLGLLALLF 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1463 TWAEAKRQLGEQNFIKSLINFDKDNISDKVLKKI-GAYCAQPDFQPDiigrvslaakslcmwvRAMELYGRLYRVVEpKR 1541
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEELEELlAALGLPPDLSPE----------------ELLELLDRIEELQE-LL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1542 IRMNAAMAQLQEKQaALAEAQEKLREV-AEKLEMLKKQYdEKLAQKEELRKKSEEMELKLERA--GMLVSGLAGEKARWE 1618
Cdd:COG4717 354 REAEELEEELQLEE-LEQEIAALLAEAgVEDEEELRAAL-EQAEEYQELKEELEELEEQLEELlgELEELLEALDEEELE 431
|
330
....*....|
gi 1720366530 1619 ETVQGLEEDL 1628
Cdd:COG4717 432 EELEELEEEL 441
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1322-1432 |
6.88e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 45.07 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1322 QELLDQANKLRTGLfkidET-----REKVEVMSLELEDAKKKVAEFQKQCEEYlviiVQQKREADEQQKAVT-ANSE--- 1392
Cdd:pfam05622 310 QQLLEDANRRKNEL----ETqnrlaNQRILELQQQVEELQKALQEQGSKAEDS----SLLKQKLEEHLEKLHeAQSElqk 381
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1720366530 1393 -KIAIEEVKCQALADNAQK--DLEEALPALEEAMRALESLNKK 1432
Cdd:pfam05622 382 kKEQIEELEPKQDSNLAQKidELQEALRKKDEDMKAMEERYKK 424
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1537-1628 |
7.04e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1537 VEPKRIRMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKAR 1616
Cdd:COG4372 54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133
|
90
....*....|..
gi 1720366530 1617 WEETVQGLEEDL 1628
Cdd:COG4372 134 LEAQIAELQSEI 145
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1319-1585 |
8.08e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1319 EKRQELLDQANK-LRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCE--------------EYLVIIVQQKREADEQ 1383
Cdd:COG4372 76 EQLEEELEELNEqLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQdleqqrkqleaqiaELQSEIAEREEELKEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1384 QKAVTANSEKIA-IEEVKCQALADNAQKDLEEalpALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMILRgnep 1462
Cdd:COG4372 156 EEQLESLQEELAaLEQELQALSEAEAEQALDE---LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE---- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1463 twAEAKRQLGEQNFIKSLINFDKDNISDKVLKKIGAYcAQPDFQPDIIGRVSLAAKSLCMWVRAMELYGRLYRVVEPKRI 1542
Cdd:COG4372 229 --AKLGLALSALLDALELEEDKEELLEEVILKEIEEL-ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLA 305
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1720366530 1543 RMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQ 1585
Cdd:COG4372 306 ALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1314-1642 |
1.04e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1314 KKLLGEKRQELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEylviIVQQKREADEQQKAVTANSEK 1393
Cdd:COG4372 51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES----LQEEAEELQEELEELQKERQD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1394 IAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKKdIGEIKSYGRPPAQVEIVMQAVMILRG-NEPTWAEAKRQLG 1472
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE-LAALEQELQALSEAEAEQALDELLKEaNRNAEKEEELAEA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1473 EQNFIKSLINFDKDNISDKVLKKIGaYCAQPDFQPDIIGRVSLAAKSLCMWVRAMELYGRLYRVVEPKRIRMNAAMAQLQ 1552
Cdd:COG4372 206 EKLIESLPRELAEELLEAKDSLEAK-LGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1553 EkqaaLAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDLGYLV 1632
Cdd:COG4372 285 L----EALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLS 360
|
330
....*....|
gi 1720366530 1633 GDCLIAAAFL 1642
Cdd:COG4372 361 KGAEAGVADG 370
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1549-1632 |
1.17e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1549 AQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDL 1628
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
....
gi 1720366530 1629 GYLV 1632
Cdd:TIGR02168 312 ANLE 315
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1546-1613 |
1.30e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 44.25 E-value: 1.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366530 1546 AAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGE 1613
Cdd:pfam05701 121 AAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIE 188
|
|
| FliJ |
COG2882 |
Flagellar biosynthesis chaperone FliJ [Cell motility]; |
1548-1588 |
1.69e-03 |
|
Flagellar biosynthesis chaperone FliJ [Cell motility];
Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 41.04 E-value: 1.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1720366530 1548 MAQLQEKQAA--LAEAQEKLREVAEKLEMLKKQYDEKLAQKEE 1588
Cdd:COG2882 13 LAEKEEDEAAreLGQAQQALEQAEEQLEQLEQYREEYEQRLQQ 55
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1307-1631 |
1.69e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1307 LELVSGYKKLLGEKRQELLDQANKLRTglfKIDETREKVEvmslELEDAKKK-------VAEFQKQ--CEEY---LVIIV 1374
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKK---EIKELKKAIE----ELKKAKGKcpvcgreLTEEHRKelLEEYtaeLKRIE 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1375 QQKREADEQQKAVTANSEKIAIEEVKCQALAdnAQKDLEEALPALEEamraleSLNKKDIGEIKSYGRppaQVEIVMQAV 1454
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESELI--KLKELAEQLKELEE------KLKKYNLEELEKKAE---EYEKLKEKL 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1455 MILRGNEPTWAEAKRQLGEQNFIKSLINFDKDNISDK---VLKKIGaycaqpDFQPDIIGRVSLAAKSLcmwvraMELYG 1531
Cdd:PRK03918 535 IKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEElaeLLKELE------ELGFESVEELEERLKEL------EPFYN 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1532 RLYRVVE-PKRI-----RMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEklaqkEELRKKSEEMeLKLERAgm 1605
Cdd:PRK03918 603 EYLELKDaEKELereekELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE-----EEYEELREEY-LELSRE-- 674
|
330 340
....*....|....*....|....*.
gi 1720366530 1606 lVSGLAGEKARWEETVQGLEEDLGYL 1631
Cdd:PRK03918 675 -LAGLRAELEELEKRREEIKKTLEKL 699
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1319-1616 |
2.15e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 43.10 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1319 EKRQELLDQAN------KLRTGLFKIDETREKvevmsleledaKKKVAEFQKQCEEYLViivQQKREADEQQKAVTANSE 1392
Cdd:pfam15558 21 QRMRELQQQAAlaweelRRRDQKRQETLERER-----------RLLLQQSQEQWQAEKE---QRKARLGREERRRADRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1393 KIAIE-EVKCQALADNAQKDLEEAL--PALEEAMRALES-LNKKDIGEIKSYGRppAQVEIVMQAVMilrgnepTWAEAK 1468
Cdd:pfam15558 87 KQVIEkESRWREQAEDQENQRQEKLerARQEAEQRKQCQeQRLKEKEEELQALR--EQNSLQLQERL-------EEACHK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1469 RQLGE--------QNFIKSLINFDKdnisdkvLKKIGAYCAQPDfqpDIIGRVSLAAKSLcmwvRAMELYgrlYRVVEpK 1540
Cdd:pfam15558 158 RQLKEreeqkkvqENNLSELLNHQA-------RKVLVDCQAKAE---ELLRRLSLEQSLQ----RSQENY---EQLVE-E 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366530 1541 RIRmnaamaQLQEKqaALAEAQ--EKLREVAEKLEMLKKQYDEKLAqkeelrkksEEMELKLERAGMLVSGLAGEKAR 1616
Cdd:pfam15558 220 RHR------ELREK--AQKEEEqfQRAKWRAEEKEEERQEHKEALA---------ELADRKIQQARQVAHKTVQDKAQ 280
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
127-212 |
2.92e-03 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 40.27 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 127 GPAGTGKTETVKDLGKALGIYVIVVNCSEgLDYKSMGRMYSGL------AQSGAWGC--FDEFNRI-------NIEVLSV 191
Cdd:pfam00004 5 GPPGTGKTTLAKAVAKELGAPFIEISGSE-LVSKYVGESEKRLrelfeaAKKLAPCVifIDEIDALagsrgsgGDSESRR 83
|
90 100
....*....|....*....|.
gi 1720366530 192 VAQQILSILSALTANLTRFYF 212
Cdd:pfam00004 84 VVNQLLTELDGFTSSNSKVIV 104
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1544-1628 |
3.35e-03 |
|
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: 41.83 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1544 MNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERA-GMLVSGLAGEKARWEETVQ 1622
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEElAELEAELEELEAEREELAA 170
|
....*.
gi 1720366530 1623 GLEEDL 1628
Cdd:COG1579 171 KIPPEL 176
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1527-1628 |
3.38e-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: 39.90 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1527 MELYGRLYRVVEPKRIRMNAamaqLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELR-------KKSEEMELK 1599
Cdd:pfam20492 9 QELEERLKQYEEETKKAQEE----LEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEesaemeaEEKEQLEAE 84
|
90 100
....*....|....*....|....*....
gi 1720366530 1600 LERAGMLVSGLAGEKARWEETVQGLEEDL 1628
Cdd:pfam20492 85 LAEAQEEIARLEEEVERKEEEARRLQEEL 113
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1543-1603 |
3.73e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.35 E-value: 3.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1543 RMNAAMAQLQEK-QAALAEAQEKL-REVAEK-------LEMLKKQYDEKLAQKEELRKKSEEMELKLERA 1603
Cdd:COG1842 62 ELEAEAEKWEEKaRLALEKGREDLaREALERkaeleaqAEALEAQLAQLEEQVEKLKEALRQLESKLEEL 131
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1543-1631 |
5.91e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1543 RMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQ 1622
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
....*....
gi 1720366530 1623 GLEEDLGYL 1631
Cdd:COG4372 119 ELQKERQDL 127
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1549-1628 |
6.37e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1549 AQLQEKQAALAEAQEKLREVAEKLEMLKKQYDE-KLAQKEELRKKSEEMELKLERagmlvsgLAGEKARWEETVQGLEED 1627
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEE-------RERRRARLEALLAALGLP 374
|
.
gi 1720366530 1628 L 1628
Cdd:COG4913 375 L 375
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1551-1631 |
9.85e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366530 1551 LQEKQAALAEAQEKLREVAEKLEMLkKQYDEKLAQK-EELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDLG 1629
Cdd:TIGR02169 704 LDELSQELSDASRKIGEIEKEIEQL-EQEEEKLKERlEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN 782
|
..
gi 1720366530 1630 YL 1631
Cdd:TIGR02169 783 DL 784
|
|
| |
