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Conserved domains on  [gi|1958663405|ref|XP_038943539|]
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dynein axonemal heavy chain 2 isoform X3 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

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 super family cl34955
Dynein, heavy chain [Cytoskeleton];
92-2492 1.77e-127

Dynein, heavy chain [Cytoskeleton];


The actual alignment was detected with superfamily member COG5245:

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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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