|
Name |
Accession |
Description |
Interval |
E-value |
| MT super family |
cl37598 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
724-1067 |
0e+00 |
|
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.
The actual alignment was detected with superfamily member pfam12777:
Pssm-ID: 463699 [Multi-domain] Cd Length: 344 Bit Score: 700.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 724 ERLENGLLKLHSTSAQVDDLKAKLATQEVELRQKNEDTDKLIQVVGVETSKVSREKAIADEEEQKVALIMLEVQQKQKDC 803
Cdd:pfam12777 1 ERLENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 804 EEDLAKAEPALTAAQAALNTLNKTNLTELKSFGSPPLAVSNVSAAVMVLMAPGGKVPKDRSWKAAKITMTKVDSFLDSLI 883
Cdd:pfam12777 81 EEDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMAPGGKIPKDKSWKAAKIMMAKVDGFLDSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 884 HFDKENIHENCLKAIRPYLQDPAFNPEFVATKSYAAAGLCSWVINIVRFYEVFCDVEPKRQALNKATSDLTAAQEKLAAI 963
Cdd:pfam12777 161 KFDKEHIHEACLKAFKPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQEKLAAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 964 KAKITHLNENLAKLTTKFEKATAEKLKCQQEAEVTAGTISLANRLVGGLASENVRWAEAVQNFRQQERTLCGDILLTTAF 1043
Cdd:pfam12777 241 KAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDILLISAF 320
|
330 340
....*....|....*....|....
gi 1958662330 1044 ISYLGFFTKKYRKSLMDGTWKPYL 1067
Cdd:pfam12777 321 ISYLGFFTKKYRNELLDKFWIPYI 344
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
1846-2141 |
1.09e-125 |
|
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: 397.76 E-value: 1.09e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1846 TQTSEKLFRTVLEMQPRDSQAGDGAGSTREEKVKAFLEEILDRVTDEFNIPELMAK--VEERTPYIVVALQECERMNILT 1923
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGGSSREEIVLELAKDILEKLPEPFDIEEAEEKypVGYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1924 REIQRSLRELHLGLQGELTMTSEMENLQNALYLDVVPEPWARRAYPSTAGLAAWFLDLLNRIKELETWTGDFVMPSTVWL 2003
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLGSWIRDLLERLKQLQDWLDDEGPPKVFWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 2004 TGFFNPQSFLTAIMQSMARKNEWPLDQMALQCDVTKKNR-EEFRSPPREGAYIYGLFMEGACWDTQAGIIAEAKLKDLTP 2082
Cdd:pfam18199 161 SGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTKKVSpEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958662330 2083 PMPVMFLKAIPAEKQDCR-SIYACPVYKTCQRG-PTYVWTFNLKTKENPSKWVLAGVALLL 2141
Cdd:pfam18199 241 PLPVIHLKPVESDKKKLDeNTYECPVYKTSERHsTNFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
1093-1311 |
4.49e-107 |
|
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: 340.96 E-value: 4.49e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1093 ATWQNEGLPADRMSMENATILINCERWPLMVDPQLQGIKWIKNKYGEE-LRVTQIGQKGCLQTIERALEAGDVVLIENLE 1171
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNgLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1172 ESIDPVLGPLLGREVIKKGR--FIKIGDKECEFNPKFRLILHTKLANPHYQPELQAQATLINFTVTRDGLEDQLLAAVVS 1249
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGrkVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958662330 1250 MEIPDLEHLKSDLTKQQNGFKITLKTLEDNLLSRLSSASGNFLGETALVENLEVTKQTAAEV 1311
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| AAA_8 |
pfam12780 |
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
452-711 |
1.42e-103 |
|
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: 332.65 E-value: 1.42e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 452 MDLVLFEDAIHHICHINRILESPRGNALLVGVGGSGKQSLTRLAAFISSMDVFQITLRKGYQIPDFKVDLASLCLKAGVK 531
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 532 NLSTVFLMTDAHVADERFLVLINDLLASGEIPDLYSEEEEENIINNVRNEVKSQGLIDSRENCWKFFIERVRRQLKVTLC 611
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 612 FSPVGNKLRIRSRKFPAIVNCTAINWFHEWPQEALESVSLRFLQNTkNIEPAVKQSISKFMAFVHISVNKISQSYLINEQ 691
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFLEDI-EIPEELKSNVVKVFVYVHSSVEDMSKKFYEELK 239
|
250 260
....*....|....*....|
gi 1958662330 692 RYNYTTPKSFLEFIRLYQSL 711
Cdd:pfam12780 240 RKNYVTPKSYLELLRLYKNL 259
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
98-275 |
9.96e-92 |
|
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: 295.07 E-value: 9.96e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 98 FDPEMPLQACLVHTSETIRVCYFMERLMERRRPVMLVGSAGSGKSVLVGAKLSSLNPEEYMVKNVPFNYYTTSAMLQAVL 177
Cdd:pfam12775 1 IPPDVPFSEILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPLFINFSAQTTSNQTQDII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 178 EKPLEKKAGRNYGPPGNRKLIYFIDDMNMPEVDAYGTVQPHTVIRQHLDYGHWYDRNKLSLKEIMNVQYISCMNPTAGS- 256
Cdd:pfam12775 81 ESKLEKRRKGVYGPPGGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKLTFKEIVDVQFVAAMGPPGGGr 160
|
170
....*....|....*....
gi 1958662330 257 FTINPRLQRHFSVFALCFP 275
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 ... |
1704-1840 |
1.17e-72 |
|
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: 238.89 E-value: 1.17e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1704 FKTILFALCYFHAVVAERRKFGPQGWNRSYPFNTGDLTISVNVLYNFL-EANTKVPYDDLRYLFGEIMYGGHITDDWDRR 1782
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLdEYDEKIPWDALRYLIGEINYGGRVTDDWDRR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1783 LCRTYLEEFIRPEMLEGELSLAPG-FPLPGNMDYSGYHQYIDaELP-PESPYLYGLHPNA 1840
Cdd:pfam18198 81 LLNTYLEEFFNPEVLEEDFKFSPSlYYIPPDGDLEDYLEYIE-SLPlVDSPEVFGLHPNA 139
|
|
| AAA_lid_1 super family |
cl39339 |
AAA+ lid domain; This domain represents the AAA lid domain from dynein heavy chain D3. |
308-407 |
1.57e-50 |
|
AAA+ lid domain; This domain represents the AAA lid domain from dynein heavy chain D3.
The actual alignment was detected with superfamily member pfam17857:
Pssm-ID: 465535 [Multi-domain] Cd Length: 100 Bit Score: 173.97 E-value: 1.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 308 LINLAVTFHQKIATTFLPTAIKFHYIFNLRDFANIFQGILFSSTECVKSTQDLVKLYLHESDRVYRDKMVEEKDFNLFDK 387
Cdd:pfam17857 1 LIAAALAFHQKIAATFLPTAIKFHYIFNLRDFANIFQGILFSSAECLKSPLDLIRLWLHESERVYGDKMVDEKDFDLFDK 80
|
90 100
....*....|....*....|
gi 1958662330 388 LQTEFLKKNFDDSKGMLEQT 407
Cdd:pfam17857 81 IQMASLKKFFDDIEDELEFA 100
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
1552-1672 |
1.89e-46 |
|
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: 163.00 E-value: 1.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1552 PATPMFFILSPGVDPLKDVENQGKKLGYtfnNRNFHNVSLGQGQEVVAEAALDLAAKKGHWVILQNIHLVAKWLST-LEK 1630
Cdd:pfam03028 2 PTTPLIFILSPGSDPTADLEKLAKKLGF---GGKLHSISLGQGQGPIAEKLIEEAAKEGGWVLLQNCHLALSWMPElEKI 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1958662330 1631 KLEELSEESHPDFRVFISAEPAPSpeghiIPQGILENSIKIT 1672
Cdd:pfam03028 79 LEELPEETLHPDFRLWLTSEPSPK-----FPISILQNSIKIT 115
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
1-89 |
2.82e-21 |
|
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: 91.19 E-value: 2.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1 MIQMLCYLLECLLTK-------EAVPADCPKEIYELYFVFAAIWAFGSSMVQDQlvdyRAEFSKWWLTEFKTVKFP--SQ 71
Cdd:pfam17852 31 LVQSLCRLLESLLDEvleyngvHPLSPDKLKEYLEKLFLFALVWSIGGTLDEDS----RKKFDEFLRELFSGLDLPppEK 106
|
90
....*....|....*...
gi 1958662330 72 GTVFDYYIDQETKKFEPW 89
Cdd:pfam17852 107 GTVYDYFVDLEKGEWVPW 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
724-1067 |
0e+00 |
|
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: 700.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 724 ERLENGLLKLHSTSAQVDDLKAKLATQEVELRQKNEDTDKLIQVVGVETSKVSREKAIADEEEQKVALIMLEVQQKQKDC 803
Cdd:pfam12777 1 ERLENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 804 EEDLAKAEPALTAAQAALNTLNKTNLTELKSFGSPPLAVSNVSAAVMVLMAPGGKVPKDRSWKAAKITMTKVDSFLDSLI 883
Cdd:pfam12777 81 EEDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMAPGGKIPKDKSWKAAKIMMAKVDGFLDSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 884 HFDKENIHENCLKAIRPYLQDPAFNPEFVATKSYAAAGLCSWVINIVRFYEVFCDVEPKRQALNKATSDLTAAQEKLAAI 963
Cdd:pfam12777 161 KFDKEHIHEACLKAFKPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQEKLAAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 964 KAKITHLNENLAKLTTKFEKATAEKLKCQQEAEVTAGTISLANRLVGGLASENVRWAEAVQNFRQQERTLCGDILLTTAF 1043
Cdd:pfam12777 241 KAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDILLISAF 320
|
330 340
....*....|....*....|....
gi 1958662330 1044 ISYLGFFTKKYRKSLMDGTWKPYL 1067
Cdd:pfam12777 321 ISYLGFFTKKYRNELLDKFWIPYI 344
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
1846-2141 |
1.09e-125 |
|
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: 397.76 E-value: 1.09e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1846 TQTSEKLFRTVLEMQPRDSQAGDGAGSTREEKVKAFLEEILDRVTDEFNIPELMAK--VEERTPYIVVALQECERMNILT 1923
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGGSSREEIVLELAKDILEKLPEPFDIEEAEEKypVGYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1924 REIQRSLRELHLGLQGELTMTSEMENLQNALYLDVVPEPWARRAYPSTAGLAAWFLDLLNRIKELETWTGDFVMPSTVWL 2003
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLGSWIRDLLERLKQLQDWLDDEGPPKVFWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 2004 TGFFNPQSFLTAIMQSMARKNEWPLDQMALQCDVTKKNR-EEFRSPPREGAYIYGLFMEGACWDTQAGIIAEAKLKDLTP 2082
Cdd:pfam18199 161 SGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTKKVSpEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958662330 2083 PMPVMFLKAIPAEKQDCR-SIYACPVYKTCQRG-PTYVWTFNLKTKENPSKWVLAGVALLL 2141
Cdd:pfam18199 241 PLPVIHLKPVESDKKKLDeNTYECPVYKTSERHsTNFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
1093-1311 |
4.49e-107 |
|
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: 340.96 E-value: 4.49e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1093 ATWQNEGLPADRMSMENATILINCERWPLMVDPQLQGIKWIKNKYGEE-LRVTQIGQKGCLQTIERALEAGDVVLIENLE 1171
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNgLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1172 ESIDPVLGPLLGREVIKKGR--FIKIGDKECEFNPKFRLILHTKLANPHYQPELQAQATLINFTVTRDGLEDQLLAAVVS 1249
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGrkVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958662330 1250 MEIPDLEHLKSDLTKQQNGFKITLKTLEDNLLSRLSSASGNFLGETALVENLEVTKQTAAEV 1311
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| AAA_8 |
pfam12780 |
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
452-711 |
1.42e-103 |
|
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: 332.65 E-value: 1.42e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 452 MDLVLFEDAIHHICHINRILESPRGNALLVGVGGSGKQSLTRLAAFISSMDVFQITLRKGYQIPDFKVDLASLCLKAGVK 531
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 532 NLSTVFLMTDAHVADERFLVLINDLLASGEIPDLYSEEEEENIINNVRNEVKSQGLIDSRENCWKFFIERVRRQLKVTLC 611
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 612 FSPVGNKLRIRSRKFPAIVNCTAINWFHEWPQEALESVSLRFLQNTkNIEPAVKQSISKFMAFVHISVNKISQSYLINEQ 691
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFLEDI-EIPEELKSNVVKVFVYVHSSVEDMSKKFYEELK 239
|
250 260
....*....|....*....|
gi 1958662330 692 RYNYTTPKSFLEFIRLYQSL 711
Cdd:pfam12780 240 RKNYVTPKSYLELLRLYKNL 259
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
98-275 |
9.96e-92 |
|
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: 295.07 E-value: 9.96e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 98 FDPEMPLQACLVHTSETIRVCYFMERLMERRRPVMLVGSAGSGKSVLVGAKLSSLNPEEYMVKNVPFNYYTTSAMLQAVL 177
Cdd:pfam12775 1 IPPDVPFSEILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPLFINFSAQTTSNQTQDII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 178 EKPLEKKAGRNYGPPGNRKLIYFIDDMNMPEVDAYGTVQPHTVIRQHLDYGHWYDRNKLSLKEIMNVQYISCMNPTAGS- 256
Cdd:pfam12775 81 ESKLEKRRKGVYGPPGGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKLTFKEIVDVQFVAAMGPPGGGr 160
|
170
....*....|....*....
gi 1958662330 257 FTINPRLQRHFSVFALCFP 275
Cdd:pfam12775 161 NDITPRLLRHFNVFNITFP 179
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
93-1807 |
5.58e-84 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 308.84 E-value: 5.58e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 93 IPQFEFDPE--MPLQACLVHTSETIRVCYFMERLMERRRPVMLVGSAGSGKSVLVGAKLssLNPEEYMVKNVPFNYYTTS 170
Cdd:COG5245 1457 IAGFELRGErvMLRKEVVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSL--RSELITEVKYFNFSTCTMT 1534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 171 AMLQAVLEKPLEK----KAGRNYGPPGNRKLIYFIDDMNMPEVDAYGtvqPHTVI---RQHLDYGHWYDRNKLSLKEIMN 243
Cdd:COG5245 1535 PSKLSVLERETEYypntGVVRLYPKPVVKDLVLFCDEINLPYGFEYY---PPTVIvflRPLVERQGFWSSIAVSWVTICG 1611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 244 VQYISCMNP--TAGSFTINPRLQRHFSVFALCFPGADALSSIYSTILTHHLKLGNFPTTLQKSIPSLinlAVTFHQKIAT 321
Cdd:COG5245 1612 IILYGACNPgtDEGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSA---SVELYLSSKD 1688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 322 TFlPTAIKFHYIFNLRDFANIFQGIlFSSTECVKSTQD--LVKLYLHESDRVYRDKMVEEKDFNLFDKLQTEFLKK---N 396
Cdd:COG5245 1689 KT-KFFLQMNYGYKPRELTRSLRAI-FGYAETRIDTPDvsLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRairE 1766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 397 FDDSKGMLEQTQNLNMYchfANGIGEpkympvqswdLLSQTLVEALE--------SHNEVnavmDLVLFEDAIHHICHIN 468
Cdd:COG5245 1767 MIAGHIGEAEITFSMIL---FFGMAC----------LLKKDLAVFVEevrkifgsSHLDV----EAVAYKDALLHILRSR 1829
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 469 RILESPRGNALLVGVGGSGKQSLTRLAAFISSMDVFQITLRKGYQIPDFKVDLASLCLKAGVKNLSTVFLMTDAHVADER 548
Cdd:COG5245 1830 RGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESS 1909
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 549 FLVLINDLLASGEIPDLYSEEEEENIINNVRNEVKSQGL-IDSRENCWKFFIERVRRQLKV--TLCfSPVGNKLRIRSRk 625
Cdd:COG5245 1910 FLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFESTSLeKDTEATLTRVFLVYMEENLPVvfSAC-CSQDTSVLAGIR- 1987
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 626 FPAIVNCTAINWFHEWPQEALESVSLRFLQNTK--------NIEPAVKQSISKFMAFVHISVNKISQSYLINEQR-YNYT 696
Cdd:COG5245 1988 SPALKNRCFIDFKKLWDTEEMSQYANSVETLSRdggrvffiNGELGVGKGALISEVFGDDAVVIEGRGFEISMIEgSLGE 2067
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 697 TPKSFLEFIRLYQSLLERNGKELQSKVERLENGLLKLHSTSAQVDDLKAKLATQEVELRQKNEDTDKLIQVVGVETSKVS 776
Cdd:COG5245 2068 SKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLERE 2147
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 777 REKAIADEEEQKVALIMLEVQQKQKDCEEDLAKAEPALTAAQAALNTLNKTNLTELKSFGSPPLAVSNVSAAVMVLMAPG 856
Cdd:COG5245 2148 VKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLLGFE 2227
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 857 GKVPKDRSwkaakiTMTKVDSFLDSLIHFDKE-NIHENCLKAIRP-YLQDPAFNPEFVATKSYAAAGLCSWVINIVRFYE 934
Cdd:COG5245 2228 AKIWFGEQ------QSLRRDDFIRIIGKYPDEiEFDLEARRFREArECSDPSFTGSILNRASKACGPLKRWLVRECNRSK 2301
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 935 VFCDVEPKRQALNKATSDLTAAQEKLAAIKAKITHLNENLAKLTTKFE---------KATAEKLKCQQEAEVTAGTIsla 1005
Cdd:COG5245 2302 VLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSldilrvhgkIADMDTVHKDVLRSIFVSEI--- 2378
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1006 nrlvggLASENVRWAEAVQNFRQQERTLCGDILLTTAFISYLGfFTKKYRKSLMDGTWKPYLSQlKVPIPTTPTLDPL-K 1084
Cdd:COG5245 2379 ------LINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIG-TLGFLCRAIEFGMSFIRISK-EFRDKEIRRRQFItE 2450
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1085 MLTDDADVATWQNeglpADRMSMENATILINCER-WPLMVDPQLQGIKWIKNKYGEELRV-TQIGQKGCLQTIERALEAG 1162
Cdd:COG5245 2451 GVQKIEDFKEEAC----STDYGLENSRIRKDLQDlTAVLNDPSSKIVTSQRQMYDEKKAIlGSFREMEFAFGLSQARREG 2526
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1163 DVVLIENlEESIDPVLGPLLGREVIKKGRFIK--IGDKECEFNPKFRLILHTKLANPHYQPELQAQATLINFTVTRDGLE 1240
Cdd:COG5245 2527 SDKIIGD-AEALDEEIGRLIKEEFKSNLSEVKvmINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCE 2605
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1241 DQLLAAVVSMEIPDLEHLKSDLTKQQNGFKITLKTLEDNLLSRLSSASGNFLGETALVENLEVTKQTAAEVQEKVQEAKL 1320
Cdd:COG5245 2606 TEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESME 2685
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1321 TEVKINEAREHYRPAAARASLLYFIMNDLSKIHPMYQFSLKAFSIVFQKAVEKAAPSEDVkerVTNLIDSITFSVYQYTT 1400
Cdd:COG5245 2686 IEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFEKWRRMKSKYLCA---IRYMLMSSEWILDHEDR 2762
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1401 RG-LFECDKLTYL--AQLTFQILLVN---QEVNAAELDF--LLRAPVQAGTPSPMEFLSHQawgsikalSSMEEFCnldr 1472
Cdd:COG5245 2763 SGfIHRLDVSFLLrtKRFVSTLLEDKnyrQVLSSCSLYGndVISHSCDRFDRDVYRALKHQ--------MDNRTHS---- 2830
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1473 dIEGSAKSWKKfvesecPEKEKFPQD-WKNKtglqrlcmmramrpdrmtyamrdFVEEKLGSKYvmgrplDFV-SSFEES 1550
Cdd:COG5245 2831 -TILTSNSKTN------PYKEYTYNDsWAEA-----------------------FEVEDSGDLY------KFEeGLLELI 2874
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1551 GPATPMFFILSPGVDPLKDVENQGKKlgytfnnrnfhnvslgqGQEVVAEAALDLAAKKGHWVILQNIHLVAKWLST--L 1628
Cdd:COG5245 2875 VGHAPLIYAHKKSLENERNVDRLGSK-----------------ENEVYAVLNSLFSRKEKSWFEVYNISLSFGWFKRyvE 2937
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1629 EKKLEELSEESHPDFRVFISAepapSPEGHIIPQGILENSIKITNEPPTGMHANLHK--ALDNFTQDTLEMCSREtefkt 1706
Cdd:COG5245 2938 DVVYPIKASRVCGKVKNMWTS----MVDADMLPIQLLIAIDSFVSSTYPETGCGYADlvEIDRYPFDYTLVIACD----- 3008
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1707 ILFALCYFHAVVAERRKFGPQGWNRSYPFNTGDLTISVNVLYNFLEANT--KVPYDDLRYLFGEIMYGGHITDDWD---- 1780
Cdd:COG5245 3009 DAFYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNILFLNHlnARKWGNNRDLIFTIVYGKKHSLMEDskvv 3088
|
1770 1780
....*....|....*....|....*..
gi 1958662330 1781 RRLCRTYLEEFIRPEMLEGELSLAPGF 1807
Cdd:COG5245 3089 DKYCRGYGAHETSSQILASVPGGDPEL 3115
|
|
| AAA_lid_11 |
pfam18198 |
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the ... |
1704-1840 |
1.17e-72 |
|
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: 238.89 E-value: 1.17e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1704 FKTILFALCYFHAVVAERRKFGPQGWNRSYPFNTGDLTISVNVLYNFL-EANTKVPYDDLRYLFGEIMYGGHITDDWDRR 1782
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLdEYDEKIPWDALRYLIGEINYGGRVTDDWDRR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1783 LCRTYLEEFIRPEMLEGELSLAPG-FPLPGNMDYSGYHQYIDaELP-PESPYLYGLHPNA 1840
Cdd:pfam18198 81 LLNTYLEEFFNPEVLEEDFKFSPSlYYIPPDGDLEDYLEYIE-SLPlVDSPEVFGLHPNA 139
|
|
| AAA_lid_1 |
pfam17857 |
AAA+ lid domain; This domain represents the AAA lid domain from dynein heavy chain D3. |
308-407 |
1.57e-50 |
|
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: 173.97 E-value: 1.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 308 LINLAVTFHQKIATTFLPTAIKFHYIFNLRDFANIFQGILFSSTECVKSTQDLVKLYLHESDRVYRDKMVEEKDFNLFDK 387
Cdd:pfam17857 1 LIAAALAFHQKIAATFLPTAIKFHYIFNLRDFANIFQGILFSSAECLKSPLDLIRLWLHESERVYGDKMVDEKDFDLFDK 80
|
90 100
....*....|....*....|
gi 1958662330 388 LQTEFLKKNFDDSKGMLEQT 407
Cdd:pfam17857 81 IQMASLKKFFDDIEDELEFA 100
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
1552-1672 |
1.89e-46 |
|
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: 163.00 E-value: 1.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1552 PATPMFFILSPGVDPLKDVENQGKKLGYtfnNRNFHNVSLGQGQEVVAEAALDLAAKKGHWVILQNIHLVAKWLST-LEK 1630
Cdd:pfam03028 2 PTTPLIFILSPGSDPTADLEKLAKKLGF---GGKLHSISLGQGQGPIAEKLIEEAAKEGGWVLLQNCHLALSWMPElEKI 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1958662330 1631 KLEELSEESHPDFRVFISAEPAPSpeghiIPQGILENSIKIT 1672
Cdd:pfam03028 79 LEELPEETLHPDFRLWLTSEPSPK-----FPISILQNSIKIT 115
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
1-89 |
2.82e-21 |
|
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: 91.19 E-value: 2.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1 MIQMLCYLLECLLTK-------EAVPADCPKEIYELYFVFAAIWAFGSSMVQDQlvdyRAEFSKWWLTEFKTVKFP--SQ 71
Cdd:pfam17852 31 LVQSLCRLLESLLDEvleyngvHPLSPDKLKEYLEKLFLFALVWSIGGTLDEDS----RKKFDEFLRELFSGLDLPppEK 106
|
90
....*....|....*...
gi 1958662330 72 GTVFDYYIDQETKKFEPW 89
Cdd:pfam17852 107 GTVYDYFVDLEKGEWVPW 124
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
938-1006 |
7.53e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 40.87 E-value: 7.53e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958662330 938 DVEPKRQALNKATSDLTAAQEKLAAIKAKITHLNENLAKLTTKFEK------ATAEKLKCQQEAEVTAGTISLAN 1006
Cdd:TIGR04320 269 DLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQtaqnnlATAQAALANAEARLAKAKEALAN 343
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
724-1067 |
0e+00 |
|
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: 700.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 724 ERLENGLLKLHSTSAQVDDLKAKLATQEVELRQKNEDTDKLIQVVGVETSKVSREKAIADEEEQKVALIMLEVQQKQKDC 803
Cdd:pfam12777 1 ERLENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 804 EEDLAKAEPALTAAQAALNTLNKTNLTELKSFGSPPLAVSNVSAAVMVLMAPGGKVPKDRSWKAAKITMTKVDSFLDSLI 883
Cdd:pfam12777 81 EEDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMAPGGKIPKDKSWKAAKIMMAKVDGFLDSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 884 HFDKENIHENCLKAIRPYLQDPAFNPEFVATKSYAAAGLCSWVINIVRFYEVFCDVEPKRQALNKATSDLTAAQEKLAAI 963
Cdd:pfam12777 161 KFDKEHIHEACLKAFKPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQEKLAAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 964 KAKITHLNENLAKLTTKFEKATAEKLKCQQEAEVTAGTISLANRLVGGLASENVRWAEAVQNFRQQERTLCGDILLTTAF 1043
Cdd:pfam12777 241 KAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDILLISAF 320
|
330 340
....*....|....*....|....
gi 1958662330 1044 ISYLGFFTKKYRKSLMDGTWKPYL 1067
Cdd:pfam12777 321 ISYLGFFTKKYRNELLDKFWIPYI 344
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
1846-2141 |
1.09e-125 |
|
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: 397.76 E-value: 1.09e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1846 TQTSEKLFRTVLEMQPRDSQAGDGAGSTREEKVKAFLEEILDRVTDEFNIPELMAK--VEERTPYIVVALQECERMNILT 1923
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGGSSREEIVLELAKDILEKLPEPFDIEEAEEKypVGYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1924 REIQRSLRELHLGLQGELTMTSEMENLQNALYLDVVPEPWARRAYPSTAGLAAWFLDLLNRIKELETWTGDFVMPSTVWL 2003
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLGSWIRDLLERLKQLQDWLDDEGPPKVFWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 2004 TGFFNPQSFLTAIMQSMARKNEWPLDQMALQCDVTKKNR-EEFRSPPREGAYIYGLFMEGACWDTQAGIIAEAKLKDLTP 2082
Cdd:pfam18199 161 SGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTKKVSpEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958662330 2083 PMPVMFLKAIPAEKQDCR-SIYACPVYKTCQRG-PTYVWTFNLKTKENPSKWVLAGVALLL 2141
Cdd:pfam18199 241 PLPVIHLKPVESDKKKLDeNTYECPVYKTSERHsTNFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
1093-1311 |
4.49e-107 |
|
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: 340.96 E-value: 4.49e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1093 ATWQNEGLPADRMSMENATILINCERWPLMVDPQLQGIKWIKNKYGEE-LRVTQIGQKGCLQTIERALEAGDVVLIENLE 1171
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNgLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1172 ESIDPVLGPLLGREVIKKGR--FIKIGDKECEFNPKFRLILHTKLANPHYQPELQAQATLINFTVTRDGLEDQLLAAVVS 1249
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGrkVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958662330 1250 MEIPDLEHLKSDLTKQQNGFKITLKTLEDNLLSRLSSASGNFLGETALVENLEVTKQTAAEV 1311
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| AAA_8 |
pfam12780 |
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
452-711 |
1.42e-103 |
|
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: 332.65 E-value: 1.42e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 452 MDLVLFEDAIHHICHINRILESPRGNALLVGVGGSGKQSLTRLAAFISSMDVFQITLRKGYQIPDFKVDLASLCLKAGVK 531
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 532 NLSTVFLMTDAHVADERFLVLINDLLASGEIPDLYSEEEEENIINNVRNEVKSQGLIDSRENCWKFFIERVRRQLKVTLC 611
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 612 FSPVGNKLRIRSRKFPAIVNCTAINWFHEWPQEALESVSLRFLQNTkNIEPAVKQSISKFMAFVHISVNKISQSYLINEQ 691
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFLEDI-EIPEELKSNVVKVFVYVHSSVEDMSKKFYEELK 239
|
250 260
....*....|....*....|
gi 1958662330 692 RYNYTTPKSFLEFIRLYQSL 711
Cdd:pfam12780 240 RKNYVTPKSYLELLRLYKNL 259
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
98-275 |
9.96e-92 |
|
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: 295.07 E-value: 9.96e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 98 FDPEMPLQACLVHTSETIRVCYFMERLMERRRPVMLVGSAGSGKSVLVGAKLSSLNPEEYMVKNVPFNYYTTSAMLQAVL 177
Cdd:pfam12775 1 IPPDVPFSEILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPLFINFSAQTTSNQTQDII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 178 EKPLEKKAGRNYGPPGNRKLIYFIDDMNMPEVDAYGTVQPHTVIRQHLDYGHWYDRNKLSLKEIMNVQYISCMNPTAGS- 256
Cdd:pfam12775 81 ESKLEKRRKGVYGPPGGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKLTFKEIVDVQFVAAMGPPGGGr 160
|
170
....*....|....*....
gi 1958662330 257 FTINPRLQRHFSVFALCFP 275
Cdd:pfam12775 161 NDITPRLLRHFNVFNITFP 179
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
93-1807 |
5.58e-84 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 308.84 E-value: 5.58e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 93 IPQFEFDPE--MPLQACLVHTSETIRVCYFMERLMERRRPVMLVGSAGSGKSVLVGAKLssLNPEEYMVKNVPFNYYTTS 170
Cdd:COG5245 1457 IAGFELRGErvMLRKEVVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSL--RSELITEVKYFNFSTCTMT 1534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 171 AMLQAVLEKPLEK----KAGRNYGPPGNRKLIYFIDDMNMPEVDAYGtvqPHTVI---RQHLDYGHWYDRNKLSLKEIMN 243
Cdd:COG5245 1535 PSKLSVLERETEYypntGVVRLYPKPVVKDLVLFCDEINLPYGFEYY---PPTVIvflRPLVERQGFWSSIAVSWVTICG 1611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 244 VQYISCMNP--TAGSFTINPRLQRHFSVFALCFPGADALSSIYSTILTHHLKLGNFPTTLQKSIPSLinlAVTFHQKIAT 321
Cdd:COG5245 1612 IILYGACNPgtDEGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSA---SVELYLSSKD 1688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 322 TFlPTAIKFHYIFNLRDFANIFQGIlFSSTECVKSTQD--LVKLYLHESDRVYRDKMVEEKDFNLFDKLQTEFLKK---N 396
Cdd:COG5245 1689 KT-KFFLQMNYGYKPRELTRSLRAI-FGYAETRIDTPDvsLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRairE 1766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 397 FDDSKGMLEQTQNLNMYchfANGIGEpkympvqswdLLSQTLVEALE--------SHNEVnavmDLVLFEDAIHHICHIN 468
Cdd:COG5245 1767 MIAGHIGEAEITFSMIL---FFGMAC----------LLKKDLAVFVEevrkifgsSHLDV----EAVAYKDALLHILRSR 1829
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 469 RILESPRGNALLVGVGGSGKQSLTRLAAFISSMDVFQITLRKGYQIPDFKVDLASLCLKAGVKNLSTVFLMTDAHVADER 548
Cdd:COG5245 1830 RGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESS 1909
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 549 FLVLINDLLASGEIPDLYSEEEEENIINNVRNEVKSQGL-IDSRENCWKFFIERVRRQLKV--TLCfSPVGNKLRIRSRk 625
Cdd:COG5245 1910 FLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFESTSLeKDTEATLTRVFLVYMEENLPVvfSAC-CSQDTSVLAGIR- 1987
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 626 FPAIVNCTAINWFHEWPQEALESVSLRFLQNTK--------NIEPAVKQSISKFMAFVHISVNKISQSYLINEQR-YNYT 696
Cdd:COG5245 1988 SPALKNRCFIDFKKLWDTEEMSQYANSVETLSRdggrvffiNGELGVGKGALISEVFGDDAVVIEGRGFEISMIEgSLGE 2067
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 697 TPKSFLEFIRLYQSLLERNGKELQSKVERLENGLLKLHSTSAQVDDLKAKLATQEVELRQKNEDTDKLIQVVGVETSKVS 776
Cdd:COG5245 2068 SKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLERE 2147
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 777 REKAIADEEEQKVALIMLEVQQKQKDCEEDLAKAEPALTAAQAALNTLNKTNLTELKSFGSPPLAVSNVSAAVMVLMAPG 856
Cdd:COG5245 2148 VKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLLGFE 2227
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 857 GKVPKDRSwkaakiTMTKVDSFLDSLIHFDKE-NIHENCLKAIRP-YLQDPAFNPEFVATKSYAAAGLCSWVINIVRFYE 934
Cdd:COG5245 2228 AKIWFGEQ------QSLRRDDFIRIIGKYPDEiEFDLEARRFREArECSDPSFTGSILNRASKACGPLKRWLVRECNRSK 2301
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 935 VFCDVEPKRQALNKATSDLTAAQEKLAAIKAKITHLNENLAKLTTKFE---------KATAEKLKCQQEAEVTAGTIsla 1005
Cdd:COG5245 2302 VLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSldilrvhgkIADMDTVHKDVLRSIFVSEI--- 2378
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1006 nrlvggLASENVRWAEAVQNFRQQERTLCGDILLTTAFISYLGfFTKKYRKSLMDGTWKPYLSQlKVPIPTTPTLDPL-K 1084
Cdd:COG5245 2379 ------LINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIG-TLGFLCRAIEFGMSFIRISK-EFRDKEIRRRQFItE 2450
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1085 MLTDDADVATWQNeglpADRMSMENATILINCER-WPLMVDPQLQGIKWIKNKYGEELRV-TQIGQKGCLQTIERALEAG 1162
Cdd:COG5245 2451 GVQKIEDFKEEAC----STDYGLENSRIRKDLQDlTAVLNDPSSKIVTSQRQMYDEKKAIlGSFREMEFAFGLSQARREG 2526
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1163 DVVLIENlEESIDPVLGPLLGREVIKKGRFIK--IGDKECEFNPKFRLILHTKLANPHYQPELQAQATLINFTVTRDGLE 1240
Cdd:COG5245 2527 SDKIIGD-AEALDEEIGRLIKEEFKSNLSEVKvmINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCE 2605
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1241 DQLLAAVVSMEIPDLEHLKSDLTKQQNGFKITLKTLEDNLLSRLSSASGNFLGETALVENLEVTKQTAAEVQEKVQEAKL 1320
Cdd:COG5245 2606 TEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESME 2685
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1321 TEVKINEAREHYRPAAARASLLYFIMNDLSKIHPMYQFSLKAFSIVFQKAVEKAAPSEDVkerVTNLIDSITFSVYQYTT 1400
Cdd:COG5245 2686 IEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFEKWRRMKSKYLCA---IRYMLMSSEWILDHEDR 2762
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1401 RG-LFECDKLTYL--AQLTFQILLVN---QEVNAAELDF--LLRAPVQAGTPSPMEFLSHQawgsikalSSMEEFCnldr 1472
Cdd:COG5245 2763 SGfIHRLDVSFLLrtKRFVSTLLEDKnyrQVLSSCSLYGndVISHSCDRFDRDVYRALKHQ--------MDNRTHS---- 2830
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1473 dIEGSAKSWKKfvesecPEKEKFPQD-WKNKtglqrlcmmramrpdrmtyamrdFVEEKLGSKYvmgrplDFV-SSFEES 1550
Cdd:COG5245 2831 -TILTSNSKTN------PYKEYTYNDsWAEA-----------------------FEVEDSGDLY------KFEeGLLELI 2874
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1551 GPATPMFFILSPGVDPLKDVENQGKKlgytfnnrnfhnvslgqGQEVVAEAALDLAAKKGHWVILQNIHLVAKWLST--L 1628
Cdd:COG5245 2875 VGHAPLIYAHKKSLENERNVDRLGSK-----------------ENEVYAVLNSLFSRKEKSWFEVYNISLSFGWFKRyvE 2937
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1629 EKKLEELSEESHPDFRVFISAepapSPEGHIIPQGILENSIKITNEPPTGMHANLHK--ALDNFTQDTLEMCSREtefkt 1706
Cdd:COG5245 2938 DVVYPIKASRVCGKVKNMWTS----MVDADMLPIQLLIAIDSFVSSTYPETGCGYADlvEIDRYPFDYTLVIACD----- 3008
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1707 ILFALCYFHAVVAERRKFGPQGWNRSYPFNTGDLTISVNVLYNFLEANT--KVPYDDLRYLFGEIMYGGHITDDWD---- 1780
Cdd:COG5245 3009 DAFYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNILFLNHlnARKWGNNRDLIFTIVYGKKHSLMEDskvv 3088
|
1770 1780
....*....|....*....|....*..
gi 1958662330 1781 RRLCRTYLEEFIRPEMLEGELSLAPGF 1807
Cdd:COG5245 3089 DKYCRGYGAHETSSQILASVPGGDPEL 3115
|
|
| AAA_lid_11 |
pfam18198 |
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the ... |
1704-1840 |
1.17e-72 |
|
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: 238.89 E-value: 1.17e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1704 FKTILFALCYFHAVVAERRKFGPQGWNRSYPFNTGDLTISVNVLYNFL-EANTKVPYDDLRYLFGEIMYGGHITDDWDRR 1782
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLdEYDEKIPWDALRYLIGEINYGGRVTDDWDRR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1783 LCRTYLEEFIRPEMLEGELSLAPG-FPLPGNMDYSGYHQYIDaELP-PESPYLYGLHPNA 1840
Cdd:pfam18198 81 LLNTYLEEFFNPEVLEEDFKFSPSlYYIPPDGDLEDYLEYIE-SLPlVDSPEVFGLHPNA 139
|
|
| AAA_lid_1 |
pfam17857 |
AAA+ lid domain; This domain represents the AAA lid domain from dynein heavy chain D3. |
308-407 |
1.57e-50 |
|
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: 173.97 E-value: 1.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 308 LINLAVTFHQKIATTFLPTAIKFHYIFNLRDFANIFQGILFSSTECVKSTQDLVKLYLHESDRVYRDKMVEEKDFNLFDK 387
Cdd:pfam17857 1 LIAAALAFHQKIAATFLPTAIKFHYIFNLRDFANIFQGILFSSAECLKSPLDLIRLWLHESERVYGDKMVDEKDFDLFDK 80
|
90 100
....*....|....*....|
gi 1958662330 388 LQTEFLKKNFDDSKGMLEQT 407
Cdd:pfam17857 81 IQMASLKKFFDDIEDELEFA 100
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
1552-1672 |
1.89e-46 |
|
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: 163.00 E-value: 1.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1552 PATPMFFILSPGVDPLKDVENQGKKLGYtfnNRNFHNVSLGQGQEVVAEAALDLAAKKGHWVILQNIHLVAKWLST-LEK 1630
Cdd:pfam03028 2 PTTPLIFILSPGSDPTADLEKLAKKLGF---GGKLHSISLGQGQGPIAEKLIEEAAKEGGWVLLQNCHLALSWMPElEKI 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1958662330 1631 KLEELSEESHPDFRVFISAEPAPSpeghiIPQGILENSIKIT 1672
Cdd:pfam03028 79 LEELPEETLHPDFRLWLTSEPSPK-----FPISILQNSIKIT 115
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
1-89 |
2.82e-21 |
|
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: 91.19 E-value: 2.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 1 MIQMLCYLLECLLTK-------EAVPADCPKEIYELYFVFAAIWAFGSSMVQDQlvdyRAEFSKWWLTEFKTVKFP--SQ 71
Cdd:pfam17852 31 LVQSLCRLLESLLDEvleyngvHPLSPDKLKEYLEKLFLFALVWSIGGTLDEDS----RKKFDEFLRELFSGLDLPppEK 106
|
90
....*....|....*...
gi 1958662330 72 GTVFDYYIDQETKKFEPW 89
Cdd:pfam17852 107 GTVYDYFVDLEKGEWVPW 124
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
717-824 |
8.87e-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: 42.99 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 717 KELQSKVERLENGLLKLHstsAQVDDLKAKLATQEVELRQKNEDTDKLI-QVVGVETSK----VSREKAIADEEEQKVAL 791
Cdd:COG1579 34 AELEDELAALEARLEAAK---TELEDLEKEIKRLELEIEEVEARIKKYEeQLGNVRNNKeyeaLQKEIESLKRRISDLED 110
|
90 100 110
....*....|....*....|....*....|...
gi 1958662330 792 IMLEVQQKQKDCEEDLAKAEPALTAAQAALNTL 824
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
130-267 |
9.32e-04 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 41.51 E-value: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 130 PVMLVGSAGSGKSVLVGAKLSSLNPEEYMVknVPFNYYTTSA-MLQAVLEKPLEKKagRNYGP---PGNRKLIYFIDDMN 205
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFY--VQLTRDTTEEdLFGRRNIDPGGAS--WVDGPlvrAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958662330 206 MPEVDAYGTVqpHTVI---RQHLDYGHWYDRNKLSlkeimNVQYISCMNPT-AGSFTINPRLQRHF 267
Cdd:pfam07728 77 RANPDVLNSL--LSLLderRLLLPDGGELVKAAPD-----GFRLIATMNPLdRGLNELSPALRSRF 135
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
938-1006 |
7.53e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 40.87 E-value: 7.53e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958662330 938 DVEPKRQALNKATSDLTAAQEKLAAIKAKITHLNENLAKLTTKFEK------ATAEKLKCQQEAEVTAGTISLAN 1006
Cdd:TIGR04320 269 DLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQtaqnnlATAQAALANAEARLAKAKEALAN 343
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
709-831 |
9.54e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958662330 709 QSLLERNGKELQSKVERLENGLLKLHSTSAQVDDLKAKLATQEVELRQKNEDTDKLIQvvgvETSKVSREKAIADEEEQK 788
Cdd:COG4372 65 EEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK----ERQDLEQQRKQLEAQIAE 140
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958662330 789 VALIMLEVQQKQKDCEEDLAKAEPALTAAQAALNTLNKTNLTE 831
Cdd:COG4372 141 LQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
|
|
| |
