|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
149-475 |
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: 648.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 149 YGYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSPKGPAGTGKTETVKDLGKALGTYVIVVNCSEGLDYKSMGRMYSG 228
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 229 LAQTGAWGCFDEFNRINIEVLSVVAQQILSILSALTANLTRFYFEGFEINLVWSCGIFITMNPGYAGRTELPENLKSMFR 308
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 309 PIAMVVPDSTLIAEIILFGEGFGNCKILAKKVYTLYSLAVQQLSRQDHYDFGLRALTSLLRYAGKKRRLQPDLTDEEVLL 388
Cdd:pfam12774 161 PVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 389 LSMRDMNIAKLTSVDVPLFNAIVQDLFPNIELPVIDYGKLRDTIEQEIREMGLQITPFTLTKVLQLYETKNSRHSTMIVG 468
Cdd:pfam12774 241 RALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVG 320
|
....*..
gi 1958663405 469 GTGSSKT 475
Cdd:pfam12774 321 PTGSGKT 327
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
2507-2807 |
7.93e-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: 7.93e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 2507 ITEARTLFETLLSLQPQITPTRIGG-QSREEKVLELAADVKQKIPEMIDYE-GTRKLLALDPSPLNVVLLQEIQRYNKLM 2584
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGgSSREEIVLELAKDILEKLPEPFDIEeAEEKYPVGYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 2585 KTILFSLTDLEKGIQGLIVMSTSLEEIFNCIFDAHVPPLWGKV-YPSQKPLASWTRDLAVRVEQFETWANRAHPPVLFWL 2663
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKsYPSLKPLGSWIRDLLERLKQLQDWLDDEGPPKVFWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 2664 SGFTFPTGFLTAVLQSAARQNNISVDSLSWEFIV-STVDDSNLVYPPKDGVWVRGLYLEGAGWDRKNSCLVEAEPMQLVC 2742
Cdd:pfam18199 161 SGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVtKKVSPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958663405 2743 LMPTIHFRPAE-SRKKSAKGMYSCPCYYYPNRAGSadraSFVIGIDLRSGaMTSDHWIKRGTALLM 2807
Cdd:pfam18199 241 PLPVIHLKPVEsDKKKLDENTYECPVYKTSERHST----NFVFSVDLPTD-KPPDHWILRGVALLL 301
|
|
| AAA_8 |
pfam12780 |
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
1116-1376 |
6.15e-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: 402.76 E-value: 6.15e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1116 MQLVLFREAIEHITRIVRVIGQPRGNMLLVGIGGSGRQSLARLASSICEYNTFQIEVTKHYRKQEFRDDIKRLYRQAGVE 1195
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1196 LQATSFLFVDTQIADESFLEDINNILSSGEVPNLYKADEFEEIQNQIIDQARAEQISESSDSLFAYLIERVRNNLHIVLC 1275
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1276 LSPVGDPFRNWIRQYPALVNCTTINWFSEWPREALLEVAEKYLvgVDLGTQENIHRKVAQIFVTMHWSVAQYSQKMLLEL 1355
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFL--EDIEIPEELKSNVVKVFVYVHSSVEDMSKKFYEEL 238
|
250 260
....*....|....*....|.
gi 1958663405 1356 RRHNYVTPTNYLELVSGYKKL 1376
Cdd:pfam12780 239 KRKNYVTPKSYLELLRLYKNL 259
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
92-2492 |
1.77e-127 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 452.52 E-value: 1.77e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 92 KIVALVTIEIHARDVLEKLYKGGLMDVNAFDWLSQLRFYwEKDVDDCIIRQTNTQFQYGYEYLGNSGRLVITPLTDRCYM 171
Cdd:COG5245 860 RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELP-QGLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMDTSQHQ 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 172 TLTTALHLHRGGSpkgpAGTGKTETVKDLGKALGTYVivvncsEGLDYKSmgRMYSGLAQTGAWGcFDEFNRINIEVLSV 251
Cdd:COG5245 939 KLFEAVCDEVCRF----VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISRTI 1005
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 252 VA--QQILSILSALTANLTRFYFEGFeinLVWSCGIFITMNPgyagRTELPENLKSMFRPIAMVVPDSTlIAEIIlfgeg 329
Cdd:COG5245 1006 LVdeYLNSDEFRMLEELNSAVVEHGL---KSPSTPVEMIINE----RNIVLEIGRRALDMFLSNIPFGA-IKSRR----- 1072
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 330 fgncKILAKKVYTLYSLAVQQLSRQDHYDFglRALTSLLRyagKKRRLQPDLTDEEVLLLSmrdmnIAKLTSVDVPLFNA 409
Cdd:COG5245 1073 ----ESLDREIGAFNNEVDGIAREEDELMF--YPMFKSLK---AKHRMLEEKTEYLNKILS-----ITGLPLISDTLRER 1138
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 410 IvqDLFPNIELPVIdygklRDTIEQEIREMGlQITPFTLTKVLQLYETKNSRHSTMIVGGTGSSKTTSWrilqaslTSLC 489
Cdd:COG5245 1139 I--DTLDAEWDSFC-----RISESLKKYESQ-QVSGLDVAQFVSFLRSVDTGAFHAEYFRVFLCKIKHY-------TDAC 1203
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 490 ragepnfnivkEFPLNPKALSLGELYGEYDLNTNEWTDGILSSVMRAACADEKpdeKWILFDGpvdtlWIESMNSVMDDN 569
Cdd:COG5245 1204 -----------DYLWHVKSPYVKKKYFDADMELRQFFLMFNREDMEARLADSK---MEYEVER-----YVEKTKAEVSSL 1264
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 570 KVLTLINGERIAMpeqvsllfeVENLAvASPATVSRCGMVYtDYVDLGWTPYVQSWLEKRPKAEIEPLQRMFE------- 642
Cdd:COG5245 1265 KLELSSVGEGQVV---------VSNLG-SIGDKVGRCLVEY-DSISRLSTKGVFLDELGDTKRYLDECLDFFScfeevqk 1333
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 643 -------KFINKILTFKKDnCNELVPVTEYSGIISLCKLYTVLATPENGVNpADTENHAFMVEMTFVFSMIWSVCASVDE 715
Cdd:COG5245 1334 eidelsmVFCADALRFSAD-LYHIVKERRFSGVLAGSDASESLGGKSIELA-AILEHKDLIVEMKRGINDVLKLRIFGDK 1411
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 716 DgRKKIDSYLREIEGSFPNKDTVYEYY---------VNPKMRTWSSFEEQLPKSWR--YPPNapfykIMVPTVDTVRYNY 784
Cdd:COG5245 1412 C-RESTPRFYLISDGDLIKDLNERSDYeemlimmfnISAVITNNGSIAGFELRGERvmLRKE-----VVIPTSDTGFVDS 1485
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 785 LVSTLVANQNPVLLVGPVGTGKTSIAQSVLQSlpSSQWSVLVVNMSAQTTSNNVQSIIESRVEK-RTKGVYVPFGG---K 860
Cdd:COG5245 1486 FSNEALNTLRSYIYCGPPGSGKEMLMCPSLRS--ELITEVKYFNFSTCTMTPSKLSVLERETEYyPNTGVVRLYPKpvvK 1563
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 861 SMITFMDDLNMPAKDMFGSQPPLELIR-LWIDYGFWYDrVKQTIKHIRDMFLMAAMGPPGG-GRTVISPRLQSRFNIINM 938
Cdd:COG5245 1564 DLVLFCDEINLPYGFEYYPPTVIVFLRpLVERQGFWSS-IAVSWVTICGIILYGACNPGTDeGRVKYYERFIRKPVFVFC 1642
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 939 TFPTESQIIRIFGTMINQKLQDFEEEVKPIGNVVTEATlDVYNTVVQRFlPTPAKIHYLFNLRDISKVFQGMLRANKDFH 1018
Cdd:COG5245 1643 CYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASV-ELYLSSKDKT-KFFLQMNYGYKPRELTRSLRAIFGYAETRI 1720
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1019 DTK-ASITRLWIHECFRVFSDRLVDTTDMEAFIGILSDKLGTFFdltfhhlcpnkRPPIFGDFLKEPKVYEDLVDLS--- 1094
Cdd:COG5245 1721 DTPdVSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAI-----------REMIAGHIGEAEITFSMILFFGmac 1789
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1095 VLKTAMETALNE-----YNLSPSVvqmQLVLFREAIEHITRIVRVIGQPRGNMLLVGIGGSGRQSLARLASSICEYNTFQ 1169
Cdd:COG5245 1790 LLKKDLAVFVEEvrkifGSSHLDV---EAVAYKDALLHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMRE 1866
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1170 IEVTKHYRKQEFRDDIKRLYRQAGVELQATSFLFVDTQIADESFLEDINNILSSGEVPNLYKADEFEEIQNQIIDQARAE 1249
Cdd:COG5245 1867 IFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFEST 1946
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1250 QIS-ESSDSLFAYLIERVRNNLHIVLCL-SPVGDPFRNWIRqYPALVNCTTINWFSEWPREALLEVAEKYL--------- 1318
Cdd:COG5245 1947 SLEkDTEATLTRVFLVYMEENLPVVFSAcCSQDTSVLAGIR-SPALKNRCFIDFKKLWDTEEMSQYANSVEtlsrdggrv 2025
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1319 --VGVDLGTQE--NIHRKVAQIFVTMHWSVaqYSQKMLLELrrhNYVTPTNYLELVSGYKKLLGEKRQELLDQANKLRTG 1394
Cdd:COG5245 2026 ffINGELGVGKgaLISEVFGDDAVVIEGRG--FEISMIEGS---LGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVEG 2100
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1395 LFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEE 1474
Cdd:COG5245 2101 VRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSS 2180
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1475 ALPALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMILRGNEPT-WAEAKRQLGEQNFIKSLI-YFDKDNISDKV 1552
Cdd:COG5245 2181 KKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLLGFEAKiWFGEQQSLRRDDFIRIIGkYPDEIEFDLEA 2260
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1553 LKKIGA-YCAQPDFQPDIIGRVSLAAKSLCMWVRAMELYGRLYRVVEPKRIRMNAAIAQLQEKQAALAEAQEKLREVAEK 1631
Cdd:COG5245 2261 RRFREArECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTF 2340
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1632 LEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDLGYLVGDCLIAAAFLSYMGPflTN 1711
Cdd:COG5245 2341 KLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGT--LG 2418
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1712 YRDEIVNQIWIKKIWELQVPCSpRFAIDNFLTN-PTKVRDWNIQGLPSDSFSTENGIIVTRGNRWALMIDPQAQALKWIK 1790
Cdd:COG5245 2419 FLCRAIEFGMSFIRISKEFRDK-EIRRRQFITEgVQKIEDFKEEACSTDYGLENSRIRKDLQDLTAVLNDPSSKIVTSQR 2497
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1791 NMEGNQGLKIIDLQMHDYLRVLEHAIQFGFPVLLQnVQEYLDPSLNPVLNKSVARIGGRMLMRIADKEVEYNPNFR-FYL 1869
Cdd:COG5245 2498 QMYDEKKAILGSFREMEFAFGLSQARREGSDKIIG-DAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAvFWL 2576
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1870 TTKLSNPHYSPEtSAKTTIVNFAVKEQGLEAQLLGIVVRKERPELEEQKDSLVINIAAGKRKLKELEDEILRLLNEATGS 1949
Cdd:COG5245 2577 SEGRSGDMGSIE-WKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISN 2655
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1950 LLDDVQLVNTLQTSKITATEVTEQLETSETTEINIDLAREAYRPCAQRASVLFFVLNDMGRIDPMYQFSLDAYISLF-IL 2028
Cdd:COG5245 2656 MEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFeKW 2735
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 2029 SIDKSHRSNKLEDRIEYLNDYhtyavyrytcrtLFERHKLLFSFhmcakILETSGKLNMDEynfFLRGGVVLDREGQMDN 2108
Cdd:COG5245 2736 RRMKSKYLCAIRYMLMSSEWI------------LDHEDRSGFIH-----RLDVSFLLRTKR---FVSTLLEDKNYRQVLS 2795
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 2109 PCTSWLADAYWDNITELDKLTNFhglMNSFEQYPRDwHLWYTNSNpekamlpgeweNACNEMQRMLIVRSLRQ-DRVAFc 2187
Cdd:COG5245 2796 SCSLYGNDVISHSCDRFDRDVYR---ALKHQMDNRT-HSTILTSN-----------SKTNPYKEYTYNDSWAEaFEVED- 2859
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 2188 vtsfivSNLGSRFieppvlnMKLVMEDSTPRSPLVFILSPGVDptsaLLQLAEHTGMAHRfhaLSLGQGQAPIAARllre 2267
Cdd:COG5245 2860 ------SGDLYKF-------EEGLLELIVGHAPLIYAHKKSLE----NERNVDRLGSKEN---EVYAVLNSLFSRK---- 2915
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 2268 gvnQGHWVFLANCHLSLSWMPN-LDKLVEQLQVEDPHPSF-RLWLSSSPHPDFPISILQASIKMTTEPPKGLKANMTRLY 2345
Cdd:COG5245 2916 ---EKSWFEVYNISLSFGWFKRyVEDVVYPIKASRVCGKVkNMWTSMVDADMLPIQLLIAIDSFVSSTYPETGCGYADLV 2992
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 2346 qlmtEAQFThcskPTKYK-----KLLFALCFFHSILLERKKFLQLGWNIIYGFNDSDFEVSENLLS--LYLDEYEETPWD 2418
Cdd:COG5245 2993 ----EIDRY----PFDYTlviacDDAFYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKniLFLNHLNARKWG 3064
|
2410 2420 2430 2440 2450 2460 2470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958663405 2419 ALKYLIAGVNYGGHVTDDWDRRLLTTYINDYFC--DLSLTTPSYRLS-VLDTYYIPKDGSLASYKEYISLLPSMDPP 2492
Cdd:COG5245 3065 NNRDLIFTIVYGKKHSLMEDSKVVDKYCRGYGAheTSSQILASVPGGdPELVKFHMEEMCRSSAFGVIGQLPDLALC 3141
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
1749-1970 |
1.50e-124 |
|
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: 391.42 E-value: 1.50e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1749 RDWNIQGLPSDSFSTENGIIVTRGNRWALMIDPQAQALKWIKNMEGNQGLKIIDLQMHDYLRVLEHAIQFGFPVLLQNVQ 1828
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1829 EYLDPSLNPVLNKSVARIGGRMLMRIADKEVEYNPNFRFYLTTKLSNPHYSPETSAKTTIVNFAVKEQGLEAQLLGIVVR 1908
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958663405 1909 KERPELEEQKDSLVINIAAGKRKLKELEDEILRLLNEATGSLLDDVQLVNTLQTSKITATEV 1970
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
794-936 |
4.32e-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: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 794 NPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKGVYVPfgGKSMITFMDDLNMPA 873
Cdd:cd00009 20 KNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEK--AKPGVLFIDEIDSLS 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958663405 874 KDMFGSQppLELIRLWIDYGFWYDRVKqtikhirdmFLMAAMGPPGGGrtvISPRLQSRFNII 936
Cdd:cd00009 98 RGAQNAL--LRVLETLNDLRIDRENVR---------VIGATNRPLLGD---LDRALYDRLDIR 146
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1397-1687 |
2.76e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1397 KIDETREKVEVMSLELEDAKKKVAEFQKQCEEylviivqqKREADEQQKavTANSEKIAIEEVKCQAL----ADNAQKDL 1472
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE--------KKKADEAKK--KAEEDKKKADELKKAAAakkkADEAKKKA 1427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1473 EEALPAlEEAMRALESLNKKDigEIKSYGRPPAQVEIVMQAVMILRGNEptwaEAKRQLGEQnfiksliyfdkdNISDKV 1552
Cdd:PTZ00121 1428 EEKKKA-DEAKKKAEEAKKAD--EAKKKAEEAKKAEEAKKKAEEAKKAD----EAKKKAEEA------------KKADEA 1488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1553 LKKigayCAQPDFQPDIIGRVSLAAKslcmwvRAMELygrlyRVVEPKRIRMNAAIAQLQEKQAALAEAQEKLR-EVAEK 1631
Cdd:PTZ00121 1489 KKK----AEEAKKKADEAKKAAEAKK------KADEA-----KKAEEAKKADEAKKAEEAKKADEAKKAEEKKKaDELKK 1553
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958663405 1632 LEMLKKQydEKLAQKEELRKKSEEMELKLERAGMLVSglaGEKARWEETVQGLEED 1687
Cdd:PTZ00121 1554 AEELKKA--EEKKKAEEAKKAEEDKNMALRKAEEAKK---AEEARIEEVMKLYEEE 1604
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1397-1688 |
1.73e-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: 53.92 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1397 KIDETREKVEVMSLELEDAKKkVAEFQKQCEEY-LVIIVQQKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEEA 1475
Cdd:TIGR02169 192 IIDEKRQQLERLRREREKAER-YQALLKEKREYeGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1476 LPALEEAMRALESLN-------KKDIGEIKsygrppAQVEivmQAVMILRGNEptwAEAKRQLGEQNFIKSLIYFDKDNI 1548
Cdd:TIGR02169 271 EQLLEELNKKIKDLGeeeqlrvKEKIGELE------AEIA---SLERSIAEKE---RELEDAEERLAKLEAEIDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1549 sDKVLKKIGAYCAQpdfqpdiigRVSLAAKslcmwvramelygrlyrvVEPKRIRMNAAIAQLQEKQAALAEAQEKLREV 1628
Cdd:TIGR02169 339 -EELEREIEEERKR---------RDKLTEE------------------YAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1629 AEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDL 1688
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
794-852 |
1.66e-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: 1.66e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958663405 794 NPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKG 852
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASG 61
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
149-475 |
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: 648.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 149 YGYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSPKGPAGTGKTETVKDLGKALGTYVIVVNCSEGLDYKSMGRMYSG 228
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 229 LAQTGAWGCFDEFNRINIEVLSVVAQQILSILSALTANLTRFYFEGFEINLVWSCGIFITMNPGYAGRTELPENLKSMFR 308
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 309 PIAMVVPDSTLIAEIILFGEGFGNCKILAKKVYTLYSLAVQQLSRQDHYDFGLRALTSLLRYAGKKRRLQPDLTDEEVLL 388
Cdd:pfam12774 161 PVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 389 LSMRDMNIAKLTSVDVPLFNAIVQDLFPNIELPVIDYGKLRDTIEQEIREMGLQITPFTLTKVLQLYETKNSRHSTMIVG 468
Cdd:pfam12774 241 RALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVG 320
|
....*..
gi 1958663405 469 GTGSSKT 475
Cdd:pfam12774 321 PTGSGKT 327
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
2507-2807 |
7.93e-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: 7.93e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 2507 ITEARTLFETLLSLQPQITPTRIGG-QSREEKVLELAADVKQKIPEMIDYE-GTRKLLALDPSPLNVVLLQEIQRYNKLM 2584
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGgSSREEIVLELAKDILEKLPEPFDIEeAEEKYPVGYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 2585 KTILFSLTDLEKGIQGLIVMSTSLEEIFNCIFDAHVPPLWGKV-YPSQKPLASWTRDLAVRVEQFETWANRAHPPVLFWL 2663
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKsYPSLKPLGSWIRDLLERLKQLQDWLDDEGPPKVFWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 2664 SGFTFPTGFLTAVLQSAARQNNISVDSLSWEFIV-STVDDSNLVYPPKDGVWVRGLYLEGAGWDRKNSCLVEAEPMQLVC 2742
Cdd:pfam18199 161 SGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVtKKVSPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958663405 2743 LMPTIHFRPAE-SRKKSAKGMYSCPCYYYPNRAGSadraSFVIGIDLRSGaMTSDHWIKRGTALLM 2807
Cdd:pfam18199 241 PLPVIHLKPVEsDKKKLDENTYECPVYKTSERHST----NFVFSVDLPTD-KPPDHWILRGVALLL 301
|
|
| AAA_8 |
pfam12780 |
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
1116-1376 |
6.15e-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: 402.76 E-value: 6.15e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1116 MQLVLFREAIEHITRIVRVIGQPRGNMLLVGIGGSGRQSLARLASSICEYNTFQIEVTKHYRKQEFRDDIKRLYRQAGVE 1195
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1196 LQATSFLFVDTQIADESFLEDINNILSSGEVPNLYKADEFEEIQNQIIDQARAEQISESSDSLFAYLIERVRNNLHIVLC 1275
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1276 LSPVGDPFRNWIRQYPALVNCTTINWFSEWPREALLEVAEKYLvgVDLGTQENIHRKVAQIFVTMHWSVAQYSQKMLLEL 1355
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFL--EDIEIPEELKSNVVKVFVYVHSSVEDMSKKFYEEL 238
|
250 260
....*....|....*....|.
gi 1958663405 1356 RRHNYVTPTNYLELVSGYKKL 1376
Cdd:pfam12780 239 KRKNYVTPKSYLELLRLYKNL 259
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
92-2492 |
1.77e-127 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 452.52 E-value: 1.77e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 92 KIVALVTIEIHARDVLEKLYKGGLMDVNAFDWLSQLRFYwEKDVDDCIIRQTNTQFQYGYEYLGNSGRLVITPLTDRCYM 171
Cdd:COG5245 860 RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELP-QGLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMDTSQHQ 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 172 TLTTALHLHRGGSpkgpAGTGKTETVKDLGKALGTYVivvncsEGLDYKSmgRMYSGLAQTGAWGcFDEFNRINIEVLSV 251
Cdd:COG5245 939 KLFEAVCDEVCRF----VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISRTI 1005
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 252 VA--QQILSILSALTANLTRFYFEGFeinLVWSCGIFITMNPgyagRTELPENLKSMFRPIAMVVPDSTlIAEIIlfgeg 329
Cdd:COG5245 1006 LVdeYLNSDEFRMLEELNSAVVEHGL---KSPSTPVEMIINE----RNIVLEIGRRALDMFLSNIPFGA-IKSRR----- 1072
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 330 fgncKILAKKVYTLYSLAVQQLSRQDHYDFglRALTSLLRyagKKRRLQPDLTDEEVLLLSmrdmnIAKLTSVDVPLFNA 409
Cdd:COG5245 1073 ----ESLDREIGAFNNEVDGIAREEDELMF--YPMFKSLK---AKHRMLEEKTEYLNKILS-----ITGLPLISDTLRER 1138
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 410 IvqDLFPNIELPVIdygklRDTIEQEIREMGlQITPFTLTKVLQLYETKNSRHSTMIVGGTGSSKTTSWrilqaslTSLC 489
Cdd:COG5245 1139 I--DTLDAEWDSFC-----RISESLKKYESQ-QVSGLDVAQFVSFLRSVDTGAFHAEYFRVFLCKIKHY-------TDAC 1203
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 490 ragepnfnivkEFPLNPKALSLGELYGEYDLNTNEWTDGILSSVMRAACADEKpdeKWILFDGpvdtlWIESMNSVMDDN 569
Cdd:COG5245 1204 -----------DYLWHVKSPYVKKKYFDADMELRQFFLMFNREDMEARLADSK---MEYEVER-----YVEKTKAEVSSL 1264
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 570 KVLTLINGERIAMpeqvsllfeVENLAvASPATVSRCGMVYtDYVDLGWTPYVQSWLEKRPKAEIEPLQRMFE------- 642
Cdd:COG5245 1265 KLELSSVGEGQVV---------VSNLG-SIGDKVGRCLVEY-DSISRLSTKGVFLDELGDTKRYLDECLDFFScfeevqk 1333
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 643 -------KFINKILTFKKDnCNELVPVTEYSGIISLCKLYTVLATPENGVNpADTENHAFMVEMTFVFSMIWSVCASVDE 715
Cdd:COG5245 1334 eidelsmVFCADALRFSAD-LYHIVKERRFSGVLAGSDASESLGGKSIELA-AILEHKDLIVEMKRGINDVLKLRIFGDK 1411
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 716 DgRKKIDSYLREIEGSFPNKDTVYEYY---------VNPKMRTWSSFEEQLPKSWR--YPPNapfykIMVPTVDTVRYNY 784
Cdd:COG5245 1412 C-RESTPRFYLISDGDLIKDLNERSDYeemlimmfnISAVITNNGSIAGFELRGERvmLRKE-----VVIPTSDTGFVDS 1485
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 785 LVSTLVANQNPVLLVGPVGTGKTSIAQSVLQSlpSSQWSVLVVNMSAQTTSNNVQSIIESRVEK-RTKGVYVPFGG---K 860
Cdd:COG5245 1486 FSNEALNTLRSYIYCGPPGSGKEMLMCPSLRS--ELITEVKYFNFSTCTMTPSKLSVLERETEYyPNTGVVRLYPKpvvK 1563
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 861 SMITFMDDLNMPAKDMFGSQPPLELIR-LWIDYGFWYDrVKQTIKHIRDMFLMAAMGPPGG-GRTVISPRLQSRFNIINM 938
Cdd:COG5245 1564 DLVLFCDEINLPYGFEYYPPTVIVFLRpLVERQGFWSS-IAVSWVTICGIILYGACNPGTDeGRVKYYERFIRKPVFVFC 1642
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 939 TFPTESQIIRIFGTMINQKLQDFEEEVKPIGNVVTEATlDVYNTVVQRFlPTPAKIHYLFNLRDISKVFQGMLRANKDFH 1018
Cdd:COG5245 1643 CYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASV-ELYLSSKDKT-KFFLQMNYGYKPRELTRSLRAIFGYAETRI 1720
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1019 DTK-ASITRLWIHECFRVFSDRLVDTTDMEAFIGILSDKLGTFFdltfhhlcpnkRPPIFGDFLKEPKVYEDLVDLS--- 1094
Cdd:COG5245 1721 DTPdVSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAI-----------REMIAGHIGEAEITFSMILFFGmac 1789
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1095 VLKTAMETALNE-----YNLSPSVvqmQLVLFREAIEHITRIVRVIGQPRGNMLLVGIGGSGRQSLARLASSICEYNTFQ 1169
Cdd:COG5245 1790 LLKKDLAVFVEEvrkifGSSHLDV---EAVAYKDALLHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMRE 1866
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1170 IEVTKHYRKQEFRDDIKRLYRQAGVELQATSFLFVDTQIADESFLEDINNILSSGEVPNLYKADEFEEIQNQIIDQARAE 1249
Cdd:COG5245 1867 IFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFEST 1946
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1250 QIS-ESSDSLFAYLIERVRNNLHIVLCL-SPVGDPFRNWIRqYPALVNCTTINWFSEWPREALLEVAEKYL--------- 1318
Cdd:COG5245 1947 SLEkDTEATLTRVFLVYMEENLPVVFSAcCSQDTSVLAGIR-SPALKNRCFIDFKKLWDTEEMSQYANSVEtlsrdggrv 2025
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1319 --VGVDLGTQE--NIHRKVAQIFVTMHWSVaqYSQKMLLELrrhNYVTPTNYLELVSGYKKLLGEKRQELLDQANKLRTG 1394
Cdd:COG5245 2026 ffINGELGVGKgaLISEVFGDDAVVIEGRG--FEISMIEGS---LGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVEG 2100
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1395 LFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEE 1474
Cdd:COG5245 2101 VRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSS 2180
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1475 ALPALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMILRGNEPT-WAEAKRQLGEQNFIKSLI-YFDKDNISDKV 1552
Cdd:COG5245 2181 KKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLLGFEAKiWFGEQQSLRRDDFIRIIGkYPDEIEFDLEA 2260
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1553 LKKIGA-YCAQPDFQPDIIGRVSLAAKSLCMWVRAMELYGRLYRVVEPKRIRMNAAIAQLQEKQAALAEAQEKLREVAEK 1631
Cdd:COG5245 2261 RRFREArECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTF 2340
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1632 LEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDLGYLVGDCLIAAAFLSYMGPflTN 1711
Cdd:COG5245 2341 KLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGT--LG 2418
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1712 YRDEIVNQIWIKKIWELQVPCSpRFAIDNFLTN-PTKVRDWNIQGLPSDSFSTENGIIVTRGNRWALMIDPQAQALKWIK 1790
Cdd:COG5245 2419 FLCRAIEFGMSFIRISKEFRDK-EIRRRQFITEgVQKIEDFKEEACSTDYGLENSRIRKDLQDLTAVLNDPSSKIVTSQR 2497
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1791 NMEGNQGLKIIDLQMHDYLRVLEHAIQFGFPVLLQnVQEYLDPSLNPVLNKSVARIGGRMLMRIADKEVEYNPNFR-FYL 1869
Cdd:COG5245 2498 QMYDEKKAILGSFREMEFAFGLSQARREGSDKIIG-DAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAvFWL 2576
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1870 TTKLSNPHYSPEtSAKTTIVNFAVKEQGLEAQLLGIVVRKERPELEEQKDSLVINIAAGKRKLKELEDEILRLLNEATGS 1949
Cdd:COG5245 2577 SEGRSGDMGSIE-WKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISN 2655
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1950 LLDDVQLVNTLQTSKITATEVTEQLETSETTEINIDLAREAYRPCAQRASVLFFVLNDMGRIDPMYQFSLDAYISLF-IL 2028
Cdd:COG5245 2656 MEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFeKW 2735
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 2029 SIDKSHRSNKLEDRIEYLNDYhtyavyrytcrtLFERHKLLFSFhmcakILETSGKLNMDEynfFLRGGVVLDREGQMDN 2108
Cdd:COG5245 2736 RRMKSKYLCAIRYMLMSSEWI------------LDHEDRSGFIH-----RLDVSFLLRTKR---FVSTLLEDKNYRQVLS 2795
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 2109 PCTSWLADAYWDNITELDKLTNFhglMNSFEQYPRDwHLWYTNSNpekamlpgeweNACNEMQRMLIVRSLRQ-DRVAFc 2187
Cdd:COG5245 2796 SCSLYGNDVISHSCDRFDRDVYR---ALKHQMDNRT-HSTILTSN-----------SKTNPYKEYTYNDSWAEaFEVED- 2859
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 2188 vtsfivSNLGSRFieppvlnMKLVMEDSTPRSPLVFILSPGVDptsaLLQLAEHTGMAHRfhaLSLGQGQAPIAARllre 2267
Cdd:COG5245 2860 ------SGDLYKF-------EEGLLELIVGHAPLIYAHKKSLE----NERNVDRLGSKEN---EVYAVLNSLFSRK---- 2915
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 2268 gvnQGHWVFLANCHLSLSWMPN-LDKLVEQLQVEDPHPSF-RLWLSSSPHPDFPISILQASIKMTTEPPKGLKANMTRLY 2345
Cdd:COG5245 2916 ---EKSWFEVYNISLSFGWFKRyVEDVVYPIKASRVCGKVkNMWTSMVDADMLPIQLLIAIDSFVSSTYPETGCGYADLV 2992
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 2346 qlmtEAQFThcskPTKYK-----KLLFALCFFHSILLERKKFLQLGWNIIYGFNDSDFEVSENLLS--LYLDEYEETPWD 2418
Cdd:COG5245 2993 ----EIDRY----PFDYTlviacDDAFYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKniLFLNHLNARKWG 3064
|
2410 2420 2430 2440 2450 2460 2470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958663405 2419 ALKYLIAGVNYGGHVTDDWDRRLLTTYINDYFC--DLSLTTPSYRLS-VLDTYYIPKDGSLASYKEYISLLPSMDPP 2492
Cdd:COG5245 3065 NNRDLIFTIVYGKKHSLMEDSKVVDKYCRGYGAheTSSQILASVPGGdPELVKFHMEEMCRSSAFGVIGQLPDLALC 3141
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
1749-1970 |
1.50e-124 |
|
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: 391.42 E-value: 1.50e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1749 RDWNIQGLPSDSFSTENGIIVTRGNRWALMIDPQAQALKWIKNMEGNQGLKIIDLQMHDYLRVLEHAIQFGFPVLLQNVQ 1828
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1829 EYLDPSLNPVLNKSVARIGGRMLMRIADKEVEYNPNFRFYLTTKLSNPHYSPETSAKTTIVNFAVKEQGLEAQLLGIVVR 1908
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958663405 1909 KERPELEEQKDSLVINIAAGKRKLKELEDEILRLLNEATGSLLDDVQLVNTLQTSKITATEV 1970
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
763-941 |
7.98e-104 |
|
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: 330.12 E-value: 7.98e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 763 YPPNAPFYKIMVPTVDTVRYNYLVSTLVANQNPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSII 842
Cdd:pfam12775 1 IPPDVPFSEILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPLFINFSAQTTSNQTQDII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 843 ESRVEKRTKGVYVPFGGKSMITFMDDLNMPAKDMFGSQPPLELIRLWIDYGFWYDRVKQTIKHIRDMFLMAAMGPPGGGR 922
Cdd:pfam12775 81 ESKLEKRRKGVYGPPGGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKLTFKEIVDVQFVAAMGPPGGGR 160
|
170
....*....|....*....
gi 1958663405 923 TVISPRLQSRFNIINMTFP 941
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 ... |
2362-2501 |
5.29e-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: 240.05 E-value: 5.29e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 2362 YKKLLFALCFFHSILLERKKFLQLGWNIIYGFNDSDFEVSENLLSLYLDEY-EETPWDALKYLIAGVNYGGHVTDDWDRR 2440
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLDEYdEKIPWDALRYLIGEINYGGRVTDDWDRR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958663405 2441 LLTTYINDYFCDlSLTTPSYRLSVlDTYYIPKDGSLASYKEYISLLPSMDPPEAFGQHPNA 2501
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 ... |
2216-2330 |
5.38e-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: 5.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 2216 TPRSPLVFILSPGVDPTSALLQLAEHTGMAHRFHALSLGQGQAPIAARLLREGVNQGHWVFLANCHLSLSWMPNLDKLVE 2295
Cdd:pfam03028 1 SPTTPLIFILSPGSDPTADLEKLAKKLGFGGKLHSISLGQGQGPIAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKILE 80
|
90 100 110
....*....|....*....|....*....|....*
gi 1958663405 2296 QLQVEDPHPSFRLWLSSSPHPDFPISILQASIKMT 2330
Cdd:pfam03028 81 ELPEETLHPDFRLWLTSEPSPKFPISILQNSIKIT 115
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
1390-1725 |
2.32e-56 |
|
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: 200.68 E-value: 2.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1390 KLRTGLFKIDETREKVEvmsleleDAKKKVA----EFQKQCE--EYLVIIVQQKREADEQQKAVTANSE-KIAIEEVKCQ 1462
Cdd:pfam12777 2 RLENGLLKLHSTAAQVD-------DLKAKLAaqeaELKQKNEdaDKLIQVVGIEADKVSKEKAIADEEEqKVAVIMKEVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1463 ALADNAQKDLEEALPALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMIL---RGNEP---TWAEAKRQLGE-QN 1535
Cdd:pfam12777 75 EKQKACEEDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILmapGGKIPkdkSWKAAKIMMAKvDG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1536 FIKSLIYFDKDNISDKVLKKIGAYCAQPDFQPDIIGRVSLAAKSLCMWVRAMELYGRLYRVVEPKRIRMNAAIAQLQEKQ 1615
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1616 AALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDLGYLVGDC 1695
Cdd:pfam12777 235 EKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDI 314
|
330 340 350
....*....|....*....|....*....|
gi 1958663405 1696 LIAAAFLSYMGPFLTNYRDEIVNQIWIKKI 1725
Cdd:pfam12777 315 LLISAFISYLGFFTKKYRNELLDKFWIPYI 344
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
637-755 |
2.10e-31 |
|
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: 120.46 E-value: 2.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 637 LQRMFEKFINKILTFKKDNCNELVPVTEYSGIISLCKLYTVLATP---ENGVNPADTENHAFMVEMTFVFSMIWSVCASV 713
Cdd:pfam17852 1 LEPLFEWLVPPALEFVRKNCKEIVPTSDLNLVQSLCRLLESLLDEvleYNGVHPLSPDKLKEYLEKLFLFALVWSIGGTL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1958663405 714 DEDGRKKIDSYLREIEGS----FPNKDTVYEYYVNPKMRTWSSFEE 755
Cdd:pfam17852 81 DEDSRKKFDEFLRELFSGldlpPPEKGTVYDYFVDLEKGEWVPWSD 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
795-933 |
1.71e-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: 103.91 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 795 PVLLVGPVGTGKTSIAQSVLQSLpsSQWSVLVVNMSAQTTSNNVQSIIESRVE--KRTKGVYVPFGGKSMITFMDDLNMP 872
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAL--SNRPVFYVQLTRDTTEEDLFGRRNIDPGgaSWVDGPLVRAAREGEIAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958663405 873 AKDMFGSQ-PPLELIRLWIDYGFWYDRVKQTikhirDMFLMAAMGPPGGGRTVISPRLQSRF 933
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. |
974-1062 |
3.26e-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: 79.21 E-value: 3.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 974 EATLDVYNTVVQRFLPTPAKIHYLFNLRDISKVFQGMLRANKDFHDTKASITRLWIHECFRVFSDRLVDTTDMEAFIGIL 1053
Cdd:pfam17857 3 AAALAFHQKIAATFLPTAIKFHYIFNLRDFANIFQGILFSSAECLKSPLDLIRLWLHESERVYGDKMVDEKDFDLFDKIQ 82
|
....*....
gi 1958663405 1054 SDKLGTFFD 1062
Cdd:pfam17857 83 MASLKKFFD 91
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
794-936 |
4.32e-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: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 794 NPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKGVYVPfgGKSMITFMDDLNMPA 873
Cdd:cd00009 20 KNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEK--AKPGVLFIDEIDSLS 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958663405 874 KDMFGSQppLELIRLWIDYGFWYDRVKqtikhirdmFLMAAMGPPGGGrtvISPRLQSRFNII 936
Cdd:cd00009 98 RGAQNAL--LRVLETLNDLRIDRENVR---------VIGATNRPLLGD---LDRALYDRLDIR 146
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
465-606 |
8.26e-08 |
|
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: 53.45 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 465 MIVGGTGSSKTTSWRILqASLtsLCRAgepNFNIVkefpLNPKALSLGELYGEYDLNTN--EWTDGILssvMRAAcadek 542
Cdd:pfam07728 3 LLVGPPGTGKTELAERL-AAA--LSNR---PVFYV----QLTRDTTEEDLFGRRNIDPGgaSWVDGPL---VRAA----- 64
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958663405 543 pDEKWILFDGPVDTL---WIESMNSVMDDNKVLTLINGERI-AMPEQVSLLFEVENL----AVASPATVSRC 606
Cdd:pfam07728 65 -REGEIAVLDEINRAnpdVLNSLLSLLDERRLLLPDGGELVkAAPDGFRLIATMNPLdrglNELSPALRSRF 135
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1311-1655 |
1.45e-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: 57.42 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1311 LEVAEKYLVGVDLGTQENIHRKVAQIFVTMhwSVAQYSQKMLLELRRHNYVTPTNYLELVSGYKKLLGEKR---QELLDQ 1387
Cdd:pfam05483 434 LKGKEQELIFLLQAREKEIHDLEIQLTAIK--TSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKeltQEASDM 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1388 ANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKRE-----------ADEQQKAVTANSEKIAI 1456
Cdd:pfam05483 512 TLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEvkckldkseenARSIEYEVLKKEKQMKI 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1457 EEVKCqalaDNAQKDLEEALPALEEAMRALESLNKKDIGEIKsygrppaQVEIVMQAVMILrgnEPTWAEAKRQLGE--Q 1534
Cdd:pfam05483 592 LENKC----NNLKKQIENKNKNIEELHQENKALKKKGSAENK-------QLNAYEIKVNKL---ELELASAKQKFEEiiD 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1535 NFIKSLIyfDKDNISDKVLKKIGAYCAQPD----FQPDIIGRVSlaaKSLCMWVRAMELYGRLY-RVVEPKRIRMNAAIA 1609
Cdd:pfam05483 658 NYQKEIE--DKKISEEKLLEEVEKAKAIADeavkLQKEIDKRCQ---HKIAEMVALMEKHKHQYdKIIEERDSELGLYKN 732
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958663405 1610 QLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEE 1655
Cdd:pfam05483 733 KEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1397-1687 |
2.76e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1397 KIDETREKVEVMSLELEDAKKKVAEFQKQCEEylviivqqKREADEQQKavTANSEKIAIEEVKCQAL----ADNAQKDL 1472
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE--------KKKADEAKK--KAEEDKKKADELKKAAAakkkADEAKKKA 1427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1473 EEALPAlEEAMRALESLNKKDigEIKSYGRPPAQVEIVMQAVMILRGNEptwaEAKRQLGEQnfiksliyfdkdNISDKV 1552
Cdd:PTZ00121 1428 EEKKKA-DEAKKKAEEAKKAD--EAKKKAEEAKKAEEAKKKAEEAKKAD----EAKKKAEEA------------KKADEA 1488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1553 LKKigayCAQPDFQPDIIGRVSLAAKslcmwvRAMELygrlyRVVEPKRIRMNAAIAQLQEKQAALAEAQEKLR-EVAEK 1631
Cdd:PTZ00121 1489 KKK----AEEAKKKADEAKKAAEAKK------KADEA-----KKAEEAKKADEAKKAEEAKKADEAKKAEEKKKaDELKK 1553
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958663405 1632 LEMLKKQydEKLAQKEELRKKSEEMELKLERAGMLVSglaGEKARWEETVQGLEED 1687
Cdd:PTZ00121 1554 AEELKKA--EEKKKAEEAKKAEEDKNMALRKAEEAKK---AEEARIEEVMKLYEEE 1604
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
186-307 |
1.52e-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: 49.98 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 186 KGPAGTGKTETVKDLGKALGTY-VIVVNCSE---------GLDYKSMG--RMYSGL---AQTGAWGCFDEFNRINIEVLS 250
Cdd:pfam07728 5 VGPPGTGKTELAERLAAALSNRpVFYVQLTRdtteedlfgRRNIDPGGasWVDGPLvraAREGEIAVLDEINRANPDVLN 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958663405 251 VVaqqiLSILSA----LTANLTRFYFEGFEINLVwscgifITMNPGYAGRTELPENLKSMF 307
Cdd:pfam07728 85 SL----LSLLDErrllLPDGGELVKAAPDGFRLI------ATMNPLDRGLNELSPALRSRF 135
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1397-1688 |
1.73e-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: 53.92 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1397 KIDETREKVEVMSLELEDAKKkVAEFQKQCEEY-LVIIVQQKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEEA 1475
Cdd:TIGR02169 192 IIDEKRQQLERLRREREKAER-YQALLKEKREYeGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1476 LPALEEAMRALESLN-------KKDIGEIKsygrppAQVEivmQAVMILRGNEptwAEAKRQLGEQNFIKSLIYFDKDNI 1548
Cdd:TIGR02169 271 EQLLEELNKKIKDLGeeeqlrvKEKIGELE------AEIA---SLERSIAEKE---RELEDAEERLAKLEAEIDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1549 sDKVLKKIGAYCAQpdfqpdiigRVSLAAKslcmwvramelygrlyrvVEPKRIRMNAAIAQLQEKQAALAEAQEKLREV 1628
Cdd:TIGR02169 339 -EELEREIEEERKR---------RDKLTEE------------------YAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1629 AEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDL 1688
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1377-1691 |
2.95e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1377 LGEKRQELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL--VIIVQQKREADEQQKAVTANSEKI 1454
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkrLEELEERHELYEEAKAKKEELERL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1455 AiEEVKCQALaDNAQKDLEEALPALEEAMRALESLNKKdIGEIKSygrppaQVEIVMQAVMILRGNEPTWAEAKRQLGEQ 1534
Cdd:PRK03918 378 K-KRLTGLTP-EKLEKELEELEKAKEEIEEEISKITAR-IGELKK------EIKELKKAIEELKKAKGKCPVCGRELTEE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1535 nfiksliyfDKDNISDKVLKKIGaycaqpDFQPDIIgrvSLAAKSLCMWVRAMELYGRLYRvvEPKRIRMNAAIAQLQEK 1614
Cdd:PRK03918 449 ---------HRKELLEEYTAELK------RIEKELK---EIEEKERKLRKELRELEKVLKK--ESELIKLKELAEQLKEL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1615 QAALAEAQ-EKLREVAEKLEMLKKQYD----------EKLAQKEELRKKSEEMELKLERAGMLVSGLAGE-KARWEETVQ 1682
Cdd:PRK03918 509 EEKLKKYNlEELEKKAEEYEKLKEKLIklkgeikslkKELEKLEELKKKLAELEKKLDELEEELAELLKElEELGFESVE 588
|
....*....
gi 1958663405 1683 GLEEDLGYL 1691
Cdd:PRK03918 589 ELEERLKEL 597
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1354-1498 |
6.56e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1354 ELRRHNYVTPTNYLELVSGYKKLLGE---KRQELLDQANKLRtglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL 1430
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEeakKAEEAKIKAEELK----KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958663405 1431 VIIVQQKREADEQQKAVtansekiaiEEVKcqaLADNAQKDLEEALPALEEAMRALESLNKKDIGEIK 1498
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKA---------EEAK---KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1398-1662 |
9.46e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 9.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1398 IDETREKVEVMSLELEDAKKKVAEFQKQCE--EYLVII------VQQKREADEQ---QKAVTANSEKIAIEEVKCQA--L 1464
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLEraEDLVEAedrierLEERREDLEEliaERRETIEEKRERAEELRERAaeL 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1465 ADNAQKDLEEALPALEEAMRALE---SLNKKdIGEIKSYGRPPAQVEIVMQAVMILRGNEPTWAEAKRQLGEQNfiksli 1541
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREevaELNSK-LAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELN------ 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1542 yfdkDNISDKvlkkigaycaqpdfqpdiigrvsLAAKSlcmwVRAMELYGRlyrvVEPKRIrmNAAIAQLQEKQAALAEA 1621
Cdd:PRK02224 623 ----DERRER-----------------------LAEKR----ERKRELEAE----FDEARI--EEAREDKERAEEYLEQV 665
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1958663405 1622 QEKLREVAEKLEMLKKQ---YDEKLAQKEELRKKSEEMELKLER 1662
Cdd:PRK02224 666 EEKLDELREERDDLQAEigaVENELEELEELRERREALENRVEA 709
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1377-1988 |
1.02e-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: 51.60 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1377 LGEKRQELLDQANKLRTGLF----KIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVII---VQQKREADEQQKAVTA 1449
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEeltaELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsrlEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1450 NSEKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKKdigeiksygrppaqveiVMQAVMILRGNEPTWAEAKR 1529
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-----------------LEELEAELEELESRLEELEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1530 QLGEQNfiksliyfdkDNISDKVLKkigaycaqpdfQPDIIGRVSLAAKSLCMWVRAMElygRLYRVVE-----PKRIRM 1604
Cdd:TIGR02168 380 QLETLR----------SKVAQLELQ-----------IASLNNEIERLEARLERLEDRRE---RLQQEIEellkkLEEAEL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1605 NAAIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKlaqKEELRKKSEEMELKLERAGMLvsglagekarweETVQGL 1684
Cdd:TIGR02168 436 KELQAELEELEEELEELQEELERLEEALEELREELEEA---EQALDAAERELAQLQARLDSL------------ERLQEN 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1685 EEDLGYLVgdcliAAAFLsymgpfltnyrdeivNQIWIKkiwelqvpcsprfaidnfltnptkvrdwNIQGLPSDSFSTE 1764
Cdd:TIGR02168 501 LEGFSEGV-----KALLK---------------NQSGLS----------------------------GILGVLSELISVD 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1765 NGI-----IVTRGNRWALMIDPQAQALKWI----KNMEGNQGLKIIDLQMHDYLRVLEHAIQFGFP--VLLQNVQEYLDP 1833
Cdd:TIGR02168 533 EGYeaaieAALGGRLQAVVVENLNAAKKAIaflkQNELGRVTFLPLDSIKGTEIQGNDREILKNIEgfLGVAKDLVKFDP 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1834 SLNPVLNKSVARIggrmlmRIAD-------KEVEYNPNFRFY-LTTKLSNPHYspetsakttIVNFAVKEQglEAQLLGi 1905
Cdd:TIGR02168 613 KLRKALSYLLGGV------LVVDdldnaleLAKKLRPGYRIVtLDGDLVRPGG---------VITGGSAKT--NSSILE- 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1906 vVRKERPELEEQKDSLVINIAAGKRKLKELEDEILRLLNEATG---SLLDDVQLVNTLQTSKITATEVTEQLEtSETTEI 1982
Cdd:TIGR02168 675 -RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQlrkELEELSRQISALRKDLARLEAEVEQLE-ERIAQL 752
|
....*.
gi 1958663405 1983 NIDLAR 1988
Cdd:TIGR02168 753 SKELTE 758
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1382-1492 |
1.26e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.91 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1382 QELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQQKAVTANSEKIaieeVKC 1461
Cdd:COG1340 146 EKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEI----VEA 221
|
90 100 110
....*....|....*....|....*....|.
gi 1958663405 1462 QALADNAQKDLEEALPALEEAMRALESLNKK 1492
Cdd:COG1340 222 QEKADELHEEIIELQKELRELRKELKKLRKK 252
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1307-1697 |
1.76e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1307 REAllEVAEKYLvgvDLGTQENIHRKvaqifvtmhwsvaqysQKMLLELRRHNyvtptNYLELVSGYKKLLGEKRQELLD 1386
Cdd:COG1196 207 RQA--EKAERYR---ELKEELKELEA----------------ELLLLKLRELE-----AELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1387 QANKLRTglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL-VIIVQQKREADEQQKAVTANSEKIAIEEV--KCQA 1463
Cdd:COG1196 261 ELAELEA---ELEELRLELEELELELEEAQAEEYELLAELARLEqDIARLEERRRELEERLEELEEELAELEEEleELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1464 LADNAQKDLEEALPALEEAMRALESLNKkdigeiksygrppAQVEIVMQAVMILRGNEPTWAEAKRQLGEQNFIKSLIYF 1543
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEE-------------ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1544 DKDNISDKVLKKIgaycaqpdfqpdiigrvslaakslcmwvRAMELYGRLYRVVEPKRIRMNAAIAQLQEKQAALAEAQE 1623
Cdd:COG1196 405 LEEAEEALLERLE----------------------------RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958663405 1624 KLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDLGYLVGDCLI 1697
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI 530
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1379-1485 |
3.66e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.03 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1379 EKRQELLDQANKLRtglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQ-KREADEQQKAVTANSEKIAiE 1457
Cdd:PRK09510 91 ELQQKQAAEQERLK----QLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAaKAKAEAEAKRAAAAAKKAA-A 165
|
90 100
....*....|....*....|....*...
gi 1958663405 1458 EVKCQALADNAQKDLEEALPALEEAMRA 1485
Cdd:PRK09510 166 EAKKKAEAEAAKKAAAEAKKKAEAEAAA 193
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1368-1679 |
4.18e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.37 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1368 ELVSGYKKLLgEKRQELLDQANKLRTglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQQKAV 1447
Cdd:COG1340 54 ELREEAQELR-EKRDELNEKVKELKE---ERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1448 -TANSEKIAIEEVKcqaladnaqkDLEEALPALEEAMRALESLnKKDIGEIKsygrppaqvEIVMQAvmilrgneptwAE 1526
Cdd:COG1340 130 lSPEEEKELVEKIK----------ELEKELEKAKKALEKNEKL-KELRAELK---------ELRKEA-----------EE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1527 AKRQLGEqnfiksliYFDKdniSDKVLKKIGAycaqpdfqpdiigrvslaakslcmwvramelygrLYRVVEPKRIRMNA 1606
Cdd:COG1340 179 IHKKIKE--------LAEE---AQELHEEMIE----------------------------------LYKEADELRKEADE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1607 AIAQLQEKQAALAE-------AQEKLREVAEKLEMLKKQYD--EKLAQKEELRKKSEEMELKLERagmlvsglaGEKARW 1677
Cdd:COG1340 214 LHKEIVEAQEKADElheeiieLQKELRELRKELKKLRKKQRalKREKEKEELEEKAEEIFEKLKK---------GEKLTT 284
|
..
gi 1958663405 1678 EE 1679
Cdd:COG1340 285 EE 286
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1397-1682 |
4.39e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1397 KIDETREKVEVMSLELEDAKKKVAEFQKQceeylviIVQQKREADEQQKAVTANSEKIaieevkcqalaDNAQKDLEEAL 1476
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAE-------LEELNEEYNELQAELEALQAEI-----------DKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1477 PALEEAMRALeslnKKDIGEIKSYGRPPAQVEIVMQAvmilrgneptwaeakrqlgeqnfiksliyfdkDNISDkVLKKI 1556
Cdd:COG3883 79 AEIEERREEL----GERARALYRSGGSVSYLDVLLGS--------------------------------ESFSD-FLDRL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1557 GAYCAQPDFQPDIIGRVslaakslcmwvramelygrlyrvvepkrirmNAAIAQLQEKQAALAEAQEKLREVAEKLEMLK 1636
Cdd:COG3883 122 SALSKIADADADLLEEL-------------------------------KADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1958663405 1637 KQYDEKLAQKEELRK--KSEEMELKLERAGMLVSGLAGEKARWEETVQ 1682
Cdd:COG3883 171 AELEAQQAEQEALLAqlSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1436-1688 |
5.85e-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: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1436 QKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKkdigEIKSygrppAQVEIvmqavm 1515
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA----EIAE-----AEAEI------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1516 ilrgneptwAEAKRQLGEQnfIKSLiYfdkdnISDKVLKKIGAYCAQPDFQpDIIGRVSLaakslcmwvramelygrLYR 1595
Cdd:COG3883 82 ---------EERREELGER--ARAL-Y-----RSGGSVSYLDVLLGSESFS-DFLDRLSA-----------------LSK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1596 VVEpkriRMNAAIAQLQEKQAALAEAQEKLREVAEKLEmlkkqydeklAQKEELRKKSEEMELKLERAGMLVSGLAGEKA 1675
Cdd:COG3883 127 IAD----ADADLLEELKADKAELEAKKAELEAKLAELE----------ALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
250
....*....|...
gi 1958663405 1676 RWEETVQGLEEDL 1688
Cdd:COG3883 193 AAEAQLAELEAEL 205
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1606-1688 |
7.77e-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: 44.55 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1606 AAIAQLQE---KQAALA-EAQEKL-REV------AEKLEMLKKQYdeklaqkEELRKKSEEMELKLERAgmlVSGLAGEK 1674
Cdd:pfam07926 22 AQLQKLQEdleKQAEIArEAQQNYeRELvlhaedIKALQALREEL-------NELKAEIAELKAEAESA---KAELEESE 91
|
90
....*....|....
gi 1958663405 1675 ARWEETVQGLEEDL 1688
Cdd:pfam07926 92 ESWEEQKKELEKEL 105
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1603-1688 |
9.55e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1603 RMNAAIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQ 1682
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE 160
|
....*.
gi 1958663405 1683 GLEEDL 1688
Cdd:COG4372 161 SLQEEL 166
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
1603-1663 |
1.16e-04 |
|
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: 43.73 E-value: 1.16e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958663405 1603 RMNAAIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYD---EKLA-QKEELRKKSEEMELKLERA 1663
Cdd:pfam18595 51 KLEEAKKKLKELRDALEEKEIELRELERREERLQRQLEnaqEKLErLREQAEEKREAAQARLEEL 115
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
794-852 |
1.66e-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: 1.66e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958663405 794 NPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKG 852
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASG 61
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1603-1661 |
3.38e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 3.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958663405 1603 RMNAAIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLA----QKEELRKKSEEMELKLE 1661
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAeleaELEELEAEREELAAKIP 173
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1601-1679 |
3.82e-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: 45.29 E-value: 3.82e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958663405 1601 RIRMNAAIAQLQEKQaaLAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAgmlvsglAGEKARWEE 1679
Cdd:pfam13868 100 REQMDEIVERIQEED--QAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEY-------LKEKAEREE 169
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1377-1688 |
4.14e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1377 LGEKRQELLDQANKLRTGLFKIDETREKVEvmslELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQ-QKAVTANSEKIA 1455
Cdd:COG4717 134 LEALEAELAELPERLEELEERLEELRELEE----ELEELEAELAELQEELEELLEQLSLATEEELQDlAEELEELQQRLA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1456 IEEVKcQALADNAQKDLEEALPALEEAMRALESLNKkdIGEIKSYGRPPAQVEIVMQAVMILRGNEPTWAEAkRQLGEQN 1535
Cdd:COG4717 210 ELEEE-LEEAQEELEELEEELEQLENELEAAALEER--LKEARLLLLIAAALLALLGLGGSLLSLILTIAGV-LFLVLGL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1536 FIKSLIYFDKDNISdkVLKKIGAYCAQPDFQpdiigrvSLAAKSLCMWVRAMELYGRLyrvvEPKRIRMN-AAIAQLQEK 1614
Cdd:COG4717 286 LALLFLLLAREKAS--LGKEAEELQALPALE-------ELEEEELEELLAALGLPPDL----SPEELLELlDRIEELQEL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1615 QAALAEAQEKLR--EVAEKLEMLKKQYD-----------EKLAQKEELRKKSEEMELKLERA--GMLVSGLAGEKARWEE 1679
Cdd:COG4717 353 LREAEELEEELQleELEQEIAALLAEAGvedeeelraalEQAEEYQELKEELEELEEQLEELlgELEELLEALDEEELEE 432
|
....*....
gi 1958663405 1680 TVQGLEEDL 1688
Cdd:COG4717 433 ELEELEEEL 441
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1374-1492 |
5.46e-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: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1374 KKLLGEKRQELLDQANKLRtglfKIDETREKV--EVMSLELEDAKKKVAEFQKQCEEylviivQQKREADEQQKAVTANS 1451
Cdd:TIGR02794 71 KKLEQQAEEAEKQRAAEQA----RQKELEQRAaaEKAAKQAEQAAKQAEEKQKQAEE------AKAKQAAEAKAKAEAEA 140
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1958663405 1452 EKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKK 1492
Cdd:TIGR02794 141 ERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKA 181
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1382-1492 |
8.93e-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: 44.68 E-value: 8.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1382 QELLDQANKLRTGLfkidET-----REKVEVMSLELEDAKKKVAEFQKQCEEYlviiVQQKREADEQQKAVT-ANSE--- 1452
Cdd:pfam05622 310 QQLLEDANRRKNEL----ETqnrlaNQRILELQQQVEELQKALQEQGSKAEDS----SLLKQKLEEHLEKLHeAQSElqk 381
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958663405 1453 -KIAIEEVKCQALADNAQK--DLEEALPALEEAMRALESLNKK 1492
Cdd:pfam05622 382 kKEQIEELEPKQDSNLAQKidELQEALRKKDEDMKAMEERYKK 424
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1607-1692 |
1.06e-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: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1607 AIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEE 1686
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
....*.
gi 1958663405 1687 DLGYLV 1692
Cdd:TIGR02168 310 RLANLE 315
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1582-1664 |
1.44e-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: 43.87 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1582 MWVRAMELY-GRLYRVVEPKRIRMNAAIAQLQEKQAALAEAQEKLREvaEKLE------MLKKQYDEK-LAQKEELRKK- 1652
Cdd:pfam15558 62 QWQAEKEQRkARLGREERRRADRREKQVIEKESRWREQAEDQENQRQ--EKLErarqeaEQRKQCQEQrLKEKEEELQAl 139
|
90
....*....|....*.
gi 1958663405 1653 --SEEMEL--KLERAG 1664
Cdd:pfam15558 140 reQNSLQLqeRLEEAC 155
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1379-1645 |
1.58e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1379 EKRQELLDQANK-LRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCE--------------EYLVIIVQQKREADEQ 1443
Cdd:COG4372 76 EQLEEELEELNEqLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQdleqqrkqleaqiaELQSEIAEREEELKEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1444 QKAVTANSEKIA-IEEVKCQALADNAQKDLEEalpALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMILRGNEp 1522
Cdd:COG4372 156 EEQLESLQEELAaLEQELQALSEAEAEQALDE---LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1523 twaeakRQLGEQNFIKSLIYFDKDNISDKVLKKIGAYCAQPDFQPDIIGRVSLAAKSLCMWVRAMELYGRLYRVVEPKRI 1602
Cdd:COG4372 232 ------GLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLA 305
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958663405 1603 RMNAAIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQ 1645
Cdd:COG4372 306 ALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1597-1688 |
1.65e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1597 VEPKRIRMNAAIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKAR 1676
Cdd:COG4372 54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133
|
90
....*....|..
gi 1958663405 1677 WEETVQGLEEDL 1688
Cdd:COG4372 134 LEAQIAELQSEI 145
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1603-1663 |
2.29e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.12 E-value: 2.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1603 RMNAAIAQLQEK-QAALAEAQEKL-REVAEK-------LEMLKKQYDEKLAQKEELRKKSEEMELKLERA 1663
Cdd:COG1842 62 ELEAEAEKWEEKaRLALEKGREDLaREALERkaeleaqAEALEAQLAQLEEQVEKLKEALRQLESKLEEL 131
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1606-1673 |
2.46e-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: 43.09 E-value: 2.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958663405 1606 AAIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGE 1673
Cdd:pfam05701 121 AAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIE 188
|
|
| FliJ |
COG2882 |
Flagellar biosynthesis chaperone FliJ [Cell motility]; |
1608-1648 |
2.60e-03 |
|
Flagellar biosynthesis chaperone FliJ [Cell motility];
Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 40.66 E-value: 2.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1958663405 1608 IAQLQEKQAA--LAEAQEKLREVAEKLEMLKKQYDEKLAQKEE 1648
Cdd:COG2882 13 LAEKEEDEAAreLGQAQQALEQAEEQLEQLEQYREEYEQRLQQ 55
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1350-1691 |
2.63e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1350 KMLLELRRHNYVTPTNYLELVSGYKK-LLGEKRQELLDQANKLRtglfKIDETREKVEVMSLELEDAKKKVAEFQKQcee 1428
Cdd:PRK03918 426 KAIEELKKAKGKCPVCGRELTEEHRKeLLEEYTAELKRIEKELK----EIEEKERKLRKELRELEKVLKKESELIKL--- 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1429 ylviivqqkREADEQQKAVTANSEKIAIEEVKcqALADNAQKdLEEALPALEEAMRALeslnKKDIGEIKSYGRPPAQVE 1508
Cdd:PRK03918 499 ---------KELAEQLKELEEKLKKYNLEELE--KKAEEYEK-LKEKLIKLKGEIKSL----KKELEKLEELKKKLAELE 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1509 IVMQAVmilrgnEPTWAEAKRQLGEQNFiKSliyFDKDNISDKVLKKIgaycaqpdfqpdiigrvslaakslcmWVRAME 1588
Cdd:PRK03918 563 KKLDEL------EEELAELLKELEELGF-ES---VEELEERLKELEPF--------------------------YNEYLE 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1589 LYGRLYRVVEPKRiRMNAAIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEklaqkEELRKKSEEMeLKLERAgmlVS 1668
Cdd:PRK03918 607 LKDAEKELEREEK-ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE-----EEYEELREEY-LELSRE---LA 676
|
330 340
....*....|....*....|...
gi 1958663405 1669 GLAGEKARWEETVQGLEEDLGYL 1691
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEKL 699
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1374-1691 |
4.47e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1374 KKLLGEKRQELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEylviIVQQKREADEQQKAVTANSEK 1453
Cdd:COG4372 51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES----LQEEAEELQEELEELQKERQD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1454 IAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKKDigeiksygrppAQVEIVMQAVMilrgNEPTWAEAKRQLGE 1533
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL-----------AALEQELQALS----EAEAEQALDELLKE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1534 QNFIKSLIYFDKDNIsdkvlkkigaycAQPDFQPDIIGRVSLAAKslcmwvrAMELYGRLYRVVEPKRIRMNAAIAQLQE 1613
Cdd:COG4372 192 ANRNAEKEEELAEAE------------KLIESLPRELAEELLEAK-------DSLEAKLGLALSALLDALELEEDKEELL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1614 KQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEM--ELKLERAGMLVSGLAGEKARWEETVQGLEEDLGYL 1691
Cdd:COG4372 253 EEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELklLALLLNLAALSLIGALEDALLAALLELAKKLELAL 332
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1587-1688 |
4.89e-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: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1587 MELYGRLYRVVEPKRIRMNAaiaqLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELR-------KKSEEMELK 1659
Cdd:pfam20492 9 QELEERLKQYEEETKKAQEE----LEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEesaemeaEEKEQLEAE 84
|
90 100
....*....|....*....|....*....
gi 1958663405 1660 LERAGMLVSGLAGEKARWEETVQGLEEDL 1688
Cdd:pfam20492 85 LAEAQEEIARLEEEVERKEEEARRLQEEL 113
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
187-272 |
8.49e-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: 38.73 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 187 GPAGTGKTETVKDLGKALGTYVIVVNCSEgLDYKSMGRMYSGL------AQTGAWGC--FDEFNRI-------NIEVLSV 251
Cdd:pfam00004 5 GPPGTGKTTLAKAVAKELGAPFIEISGSE-LVSKYVGESEKRLrelfeaAKKLAPCVifIDEIDALagsrgsgGDSESRR 83
|
90 100
....*....|....*....|.
gi 1958663405 252 VAQQILSILSALTANLTRFYF 272
Cdd:pfam00004 84 VVNQLLTELDGFTSSNSKVIV 104
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1600-1685 |
8.90e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.19 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663405 1600 KRIRMNAAIAQLQEKQAALAEAQEKLRevaEKLEMLKKQYDEKLAQKEEL--RKKSEEMELKLERA--GMLVSGLAGEKA 1675
Cdd:COG1842 92 RKAELEAQAEALEAQLAQLEEQVEKLK---EALRQLESKLEELKAKKDTLkaRAKAAKAQEKVNEAlsGIDSDDATSALE 168
|
90
....*....|
gi 1958663405 1676 RWEETVQGLE 1685
Cdd:COG1842 169 RMEEKIEEME 178
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
1606-1649 |
9.07e-03 |
|
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. It has a coiled coil structure with an atypical 3(10)-helix in the alpha-hairpin region. It is involved in DNA_binding.
Pssm-ID: 465095 [Multi-domain] Cd Length: 69 Bit Score: 37.06 E-value: 9.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1958663405 1606 AAIAQLQEKQAALAEA---------QEKLREVAEKLEMLKKQYDEKLAQKEEL 1649
Cdd:pfam16326 15 AEIEKLEEEIAELEAQladpelysdYEKLQELSAELEELEAELEELYERWEEL 67
|
|
|