|
Name |
Accession |
Description |
Interval |
E-value |
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
121-439 |
3.72e-123 |
|
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276812 [Multi-domain] Cd Length: 326 Bit Score: 379.29 E-value: 3.72e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 121 SDADFADLVELQPEiKRLKLRKN---NWNSESYKFDEVFTDTASQKRVYEGVAKPVVEGVLSGYNGTIMAYGQTGTGKTY 197
Cdd:cd00106 15 EARSAKSVISVDGG-KSVVLDPPknrVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNGTIFAYGQTGSGKTY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 198 TVgkIGKDDAaERGIMVRALEDILLNAS-----SASISVEISYLQLYMETIQDLLAP-EKNNISINEDAKTGeVSVPGAT 271
Cdd:cd00106 94 TM--LGPDPE-QRGIIPRALEDIFERIDkrketKSSFSVSASYLEIYNEKIYDLLSPvPKKPLSLREDPKRG-VYVKGLT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 272 VVNIQDLDHFLQVLQVGETNRHAANTKMNTESSRSHAILTVYVRRAMNEKTEkakpeslgdkaiPRVRKSKLLIVDLAGS 351
Cdd:cd00106 170 EVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSG------------ESVTSSKLNLVDLAGS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 352 ERINKSGTDGHMIEEAKFINLSLTSLGKCINALAEGSS-HIPTRDSKLTRLLRDSFGGSARTSLIITIGPSARYHAETTS 430
Cdd:cd00106 238 ERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNkHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLS 317
|
....*....
gi 1063716835 431 TIMFGQRAM 439
Cdd:cd00106 318 TLRFASRAK 326
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
115-441 |
5.07e-113 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 352.65 E-value: 5.07e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 115 NGEELISDADFADLVELQ-PEIKRLKLRKNNWNSESYKFDEVFTDTASQKRVYEGVAKPVVEGVLSGYNGTIMAYGQTGT 193
Cdd:pfam00225 6 NEREKERGSSVIVSVESVdSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAYGQTGS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 194 GKTYTVGkiGKDDaaERGIMVRALEDILLNASSA----SISVEISYLQLYMETIQDLLAPEKNN---ISINEDAKTGeVS 266
Cdd:pfam00225 86 GKTYTME--GSDE--QPGIIPRALEDLFDRIQKTkersEFSVKVSYLEIYNEKIRDLLSPSNKNkrkLRIREDPKKG-VY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 267 VPGATVVNIQDLDHFLQVLQVGETNRHAANTKMNTESSRSHAILTVYVRRamnektekakpESLGDKAIPRVRKSKLLIV 346
Cdd:pfam00225 161 VKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQ-----------RNRSTGGEESVKTGKLNLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 347 DLAGSERINKSG-TDGHMIEEAKFINLSLTSLGKCINALAEG-SSHIPTRDSKLTRLLRDSFGGSARTSLIITIGPSARY 424
Cdd:pfam00225 230 DLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKkSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSN 309
|
330
....*....|....*..
gi 1063716835 425 HAETTSTIMFGQRAMKI 441
Cdd:pfam00225 310 YEETLSTLRFASRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
121-443 |
4.45e-102 |
|
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.
Pssm-ID: 214526 [Multi-domain] Cd Length: 335 Bit Score: 324.14 E-value: 4.45e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 121 SDADFADLVELQPEIKRlKLRKNNWNSE----SYKFDEVFTDTASQKRVYEGVAKPVVEGVLSGYNGTIMAYGQTGTGKT 196
Cdd:smart00129 16 KSRKSPSVVPFPDKVGK-TLTVRSPKNRqgekKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYNATIFAYGQTGSGKT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 197 YTVGkiGKDDaaERGIMVRALEDIL--LNASSA--SISVEISYLQLYMETIQDLLAPEKNNISINEDAKtGEVSVPGATV 272
Cdd:smart00129 95 YTMI--GTPD--SPGIIPRALKDLFekIDKREEgwQFSVKVSYLEIYNEKIRDLLNPSSKKLEIREDEK-GGVYVKGLTE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 273 VNIQDLDHFLQVLQVGETNRHAANTKMNTESSRSHAILTVYVRRAM-NEKTEkakpeslgdkaipRVRKSKLLIVDLAGS 351
Cdd:smart00129 170 ISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIkNSSSG-------------SGKASKLNLVDLAGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 352 ERINKSGTDGHMIEEAKFINLSLTSLGKCINALAE--GSSHIPTRDSKLTRLLRDSFGGSARTSLIITIGPSARYHAETT 429
Cdd:smart00129 237 ERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQhsKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETL 316
|
330
....*....|....
gi 1063716835 430 STIMFGQRAMKIVN 443
Cdd:smart00129 317 STLRFASRAKEIKN 330
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
149-441 |
1.62e-90 |
|
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276820 [Multi-domain] Cd Length: 325 Bit Score: 292.70 E-value: 1.62e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 149 SYKFDEVFTDTASQKRVYEGVAKPVVEGVLSGYNGTIMAYGQTGTGKTYTV-GKIGkdDAAERGIMVRALED----ILLN 223
Cdd:cd01369 44 TFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMeGKLG--DPESMGIIPRIVQDifetIYSM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 224 ASSASISVEISYLQLYMETIQDLLAPEKNNISINEDaKTGEVSVPGATVVNIQDLDHFLQVLQVGETNRHAANTKMNTES 303
Cdd:cd01369 122 DENLEFHVKVSYFEIYMEKIRDLLDVSKTNLSVHED-KNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEES 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 304 SRSHAILTVYVRRAmNEKTEKAKpeslgdkaiprvrKSKLLIVDLAGSERINKSGTDGHMIEEAKFINLSLTSLGKCINA 383
Cdd:cd01369 201 SRSHSIFLINVKQE-NVETEKKK-------------SGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINA 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063716835 384 LAEG-SSHIPTRDSKLTRLLRDSFGGSARTSLIITIGPSARYHAETTSTIMFGQRAMKI 441
Cdd:cd01369 267 LTDGkKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
149-441 |
8.21e-79 |
|
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276825 [Multi-domain] Cd Length: 321 Bit Score: 260.73 E-value: 8.21e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 149 SYKFDEVFTDTASQKRVYEGVAKPVVEGVLSGYNGTIMAYGQTGTGKTYTVgkigKDDAAERGIMVRALEDIL---LNAS 225
Cdd:cd01374 40 SFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFAYGQTSSGKTFTM----SGDEDEPGIIPLAIRDIFskiQDTP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 226 SASISVEISYLQLYMETIQDLLAPEKNNISINEDAKTGeVSVPGATVVNIQDLDHFLQVLQVGETNRHAANTKMNTESSR 305
Cdd:cd01374 116 DREFLLRVSYLEIYNEKINDLLSPTSQNLKIRDDVEKG-VYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 306 SHAILTVYVRRamnekteKAKPESLGDKaiprVRKSKLLIVDLAGSERINKSGTDGHMIEEAKFINLSLTSLGKCINALA 385
Cdd:cd01374 195 SHTIFRITIES-------SERGELEEGT----VRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLS 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063716835 386 EG--SSHIPTRDSKLTRLLRDSFGGSARTSLIITIGPSARYHAETTSTIMFGQRAMKI 441
Cdd:cd01374 264 EGkvGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
136-447 |
5.10e-77 |
|
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276817 [Multi-domain] Cd Length: 329 Bit Score: 255.98 E-value: 5.10e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 136 KRLKLRKNNWNSESYKFDEVFTDTASQKRVYEGVaKPVVEGVLSGYNGTIMAYGQTGTGKTYTVgkIGKDDaaERGIMVR 215
Cdd:cd01366 33 QTIELTSIGAKQKEFSFDKVFDPEASQEDVFEEV-SPLVQSALDGYNVCIFAYGQTGSGKTYTM--EGPPE--SPGIIPR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 216 ALEDI-----LLNASSASISVEISYLQLYMETIQDLLAPEKN---NISINEDAKTGEVSVPGATVVNIQDLDHFLQVLQV 287
Cdd:cd01366 108 ALQELfntikELKEKGWSYTIKASMLEIYNETIRDLLAPGNApqkKLEIRHDSEKGDTTVTNLTEVKVSSPEEVRQLLKK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 288 GETNRHAANTKMNTESSRSHAILTVYVRRAmNEKTEKAkpeslgdkaiprvRKSKLLIVDLAGSERINKSGTDGHMIEEA 367
Cdd:cd01366 188 ASKNRSTASTAMNEHSSRSHSVFILHISGR-NLQTGEI-------------SVGKLNLVDLAGSERLNKSGATGDRLKET 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 368 KFINLSLTSLGKCINALAEGSSHIPTRDSKLTRLLRDSFGGSARTSLIITIGPSARYHAETTSTIMFGQRamkiVNMVKL 447
Cdd:cd01366 254 QAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASK----VNSCEL 329
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
115-441 |
1.03e-76 |
|
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276821 [Multi-domain] Cd Length: 345 Bit Score: 255.73 E-value: 1.03e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 115 NGEELISDADFADLVELQPEIKRLKLRKNNWNSESYKFDEVFTDTASQKRVYEGVAKPVVEGVLSGYNGTIMAYGQTGTG 194
Cdd:cd01370 28 DNHMLVFDPKDEEDGFFHGGSNNRDRRKRRNKELKYVFDRVFDETSTQEEVYEETTKPLVDGVLNGYNATVFAYGATGAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 195 KTYTVgkIGKDDaaERGIMVRALEDILLNASSASIS----VEISYLQLYMETIQDLLAPEKNNISINEDAKTGeVSVPGA 270
Cdd:cd01370 108 KTHTM--LGTPQ--EPGLMVLTMKELFKRIESLKDEkefeVSMSYLEIYNETIRDLLNPSSGPLELREDAQNG-IVVAGL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 271 TVVNIQDLDHFLQVLQVGETNRHAANTKMNTESSRSHAILTVYVRRamnektekakpESLGDKAIPRVRKSKLLIVDLAG 350
Cdd:cd01370 183 TEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQ-----------QDKTASINQQVRQGKLSLIDLAG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 351 SERINKSGTDGHMIEEAKFINLSLTSLGKCINALAEGSS---HIPTRDSKLTRLLRDSFGGSARTSLIITIGPSARYHAE 427
Cdd:cd01370 252 SERASATNNRGQRLKEGANINRSLLALGNCINALADPGKknkHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEE 331
|
330
....*....|....
gi 1063716835 428 TTSTIMFGQRAMKI 441
Cdd:cd01370 332 THNTLKYANRAKNI 345
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
146-441 |
1.33e-75 |
|
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276823 [Multi-domain] Cd Length: 341 Bit Score: 252.64 E-value: 1.33e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 146 NSESYKFDEVFTDTASQKRVYEGVAKPVVEGVLSGYNGTIMAYGQTGTGKTYTVGKIGKD--DAAERGIMVRALEDI--L 221
Cdd:cd01372 38 TDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAYTAeeDEEQVGIIPRAIQHIfkK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 222 LNASSASI--SVEISYLQLYMETIQDLLAPE---KNNISINEDAKtGEVSVPGATVVNIQDLDHFLQVLQVGETNRHAAN 296
Cdd:cd01372 118 IEKKKDTFefQLKVSFLEIYNEEIRDLLDPEtdkKPTISIREDSK-GGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTAS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 297 TKMNTESSRSHAILTVYVRRamnEKTEKAKPESLGDKAIPRVRkSKLLIVDLAGSERINKSGTDGHMIEEAKFINLSLTS 376
Cdd:cd01372 197 TAMNSQSSRSHAIFTITLEQ---TKKNGPIAPMSADDKNSTFT-SKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLA 272
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063716835 377 LGKCINALAEGS---SHIPTRDSKLTRLLRDSFGGSARTSLIITIGPSARYHAETTSTIMFGQRAMKI 441
Cdd:cd01372 273 LGNVISALGDESkkgAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNI 340
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
149-441 |
1.96e-74 |
|
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276822 [Multi-domain] Cd Length: 334 Bit Score: 249.30 E-value: 1.96e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 149 SYKFDEVFTDTASQKRVYEGVAKPVVEGVLSGYNGTIMAYGQTGTGKTYTVGKIgKDDAAERGIMVRALEDILLNASSAS 228
Cdd:cd01371 49 TFTFDAVFDPNSKQLDVYDETARPLVDSVLEGYNGTIFAYGQTGTGKTYTMEGK-REDPELRGIIPNSFAHIFGHIARSQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 229 IS----VEISYLQLYMETIQDLLAPE-KNNISINEDAKTGeVSVPGATVVNIQDLDHFLQVLQVGETNRHAANTKMNTES 303
Cdd:cd01371 128 NNqqflVRVSYLEIYNEEIRDLLGKDqTKRLELKERPDTG-VYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 304 SRSHAILTVYVRRAmnEKTEKAKPEslgdkaiprVRKSKLLIVDLAGSERINKSGTDGHMIEEAKFINLSLTSLGKCINA 383
Cdd:cd01371 207 SRSHAIFTITIECS--EKGEDGENH---------IRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISA 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063716835 384 LAEG-SSHIPTRDSKLTRLLRDSFGGSARTSLIITIGPSARYHAETTSTIMFGQRAMKI 441
Cdd:cd01371 276 LVDGkSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
146-444 |
2.52e-74 |
|
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276815 [Multi-domain] Cd Length: 353 Bit Score: 249.55 E-value: 2.52e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 146 NSESYKFDEVFTDTASQKRVYEGVAKPVVEGVLSGYNGTIMAYGQTGTGKTYT-VGKIGKDD------AAERGIMVRALE 218
Cdd:cd01364 47 STKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYNCTIFAYGQTGTGKTYTmEGDRSPNEeytwelDPLAGIIPRTLH 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 219 DIL--LNASSASISVEISYLQLYMETIQDLLAPEKNN---ISINED-AKTGEVSVPGATVVNIQDLDHFLQVLQVGETNR 292
Cdd:cd01364 127 QLFekLEDNGTEYSVKVSYLEIYNEELFDLLSPSSDVserLRMFDDpRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKR 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 293 HAANTKMNTESSRSHAILTVYVrramNEKTEKAKPESLgdkaiprVRKSKLLIVDLAGSERINKSGTDGHMIEEAKFINL 372
Cdd:cd01364 207 KTAATLMNAQSSRSHSVFSITI----HIKETTIDGEEL-------VKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQ 275
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063716835 373 SLTSLGKCINALAEGSSHIPTRDSKLTRLLRDSFGGSARTSLIITIGPSARYHAETTSTIMFGQRAMKIVNM 444
Cdd:cd01364 276 SLLTLGRVITALVERAPHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNK 347
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
150-449 |
8.41e-69 |
|
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276824 [Multi-domain] Cd Length: 347 Bit Score: 233.94 E-value: 8.41e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 150 YKFDEVFTDTASQKRVYEGVAKPVVEGVLSGYNGTIMAYGQTGTGKTYTV-GKIGKDDAA---ERGIMVRALEDI--LLN 223
Cdd:cd01373 43 FTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAYGQTGSGKTYTMwGPSESDNESphgLRGVIPRIFEYLfsLIQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 224 ------ASSASISVEISYLQLYMETIQDLLAPEKNNISINEDAKTGeVSVPGATVVNIQDLDHFLQVLQVGETNRHAANT 297
Cdd:cd01373 123 rekekaGEGKSFLCKCSFLEIYNEQIYDLLDPASRNLKLREDIKKG-VYVENLVEEYVTSAEDVYQVLSKGWSNRKVAAT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 298 KMNTESSRSHAILTVYVrramnektekakpESLGDKA-IPRVRKSKLLIVDLAGSERINKSGTDGHMIEEAKFINLSLTS 376
Cdd:cd01373 202 SMNRESSRSHAVFTCTI-------------ESWEKKAcFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSC 268
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063716835 377 LGKCINALAE----GSSHIPTRDSKLTRLLRDSFGGSARTSLIITIGPSARYHAETTSTIMFGQRAMKIVNMVKLKE 449
Cdd:cd01373 269 LGHVINALVDvahgKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNE 345
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
128-446 |
2.02e-68 |
|
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.
Pssm-ID: 276816 [Multi-domain] Cd Length: 361 Bit Score: 233.40 E-value: 2.02e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 128 LVELQPE---IKRLKLRKNNWNSE-----SYKFDEVF-------TDTASQKRVYEGVAKPVVEGVLSGYNGTIMAYGQTG 192
Cdd:cd01365 24 IVQMSGKettLKNPKQADKNNKATrevpkSFSFDYSYwshdsedPNYASQEQVYEDLGEELLQHAFEGYNVCLFAYGQTG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 193 TGKTYTVgkIGKDdaAERGIMVRALEDIL--LNASSA---SISVEISYLQLYMETIQDLLAP----EKNNISINEDAKTG 263
Cdd:cd01365 104 SGKSYTM--MGTQ--EQPGIIPRLCEDLFsrIADTTNqnmSYSVEVSYMEIYNEKVRDLLNPkpkkNKGNLKVREHPVLG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 264 eVSVPGATVVNIQDLDHFLQVLQVGETNRHAANTKMNTESSRSHAILTVYVRRAMNEKTEKAKPEslgdkaiprvRKSKL 343
Cdd:cd01365 180 -PYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAETNLTTE----------KVSKI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 344 LIVDLAGSERINKSGTDGHMIEEAKFINLSLTSLGKCINALAEGS--------SHIPTRDSKLTRLLRDSFGGSARTSLI 415
Cdd:cd01365 249 SLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSsgkskkksSFIPYRDSVLTWLLKENLGGNSKTAMI 328
|
330 340 350
....*....|....*....|....*....|.
gi 1063716835 416 ITIGPSARYHAETTSTIMFGQRAMKIVNMVK 446
Cdd:cd01365 329 AAISPADINYEETLSTLRYADRAKKIVNRAV 359
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
143-437 |
5.47e-68 |
|
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276826 [Multi-domain] Cd Length: 334 Bit Score: 231.32 E-value: 5.47e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 143 NNWNSESYKFDEVFtDTASQKRVYEGVAKPVVEGVLSGYNGTIMAYGQTGTGKTYTVGKiGKDDAAERGIMVRALEDI-- 220
Cdd:cd01375 43 NQQEDWSFKFDGVL-HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTG-GTENYKHRGIIPRALQQVfr 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 221 -LLNASSASISVEISYLQLYMETIQDLLA------PEKNNISINEDAKTGeVSVPGATVVNIQDLDHFLQVLQVGETNRH 293
Cdd:cd01375 121 mIEERPTKAYTVHVSYLEIYNEQLYDLLStlpyvgPSVTPMTILEDSPQN-IFIKGLSLHLTSQEEEALSLLFLGETNRI 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 294 AANTKMNTESSRSHAILTVYVrramnekteKAKPESLGDKaipRVRKSKLLIVDLAGSERINKSGTDGHMIEEAKFINLS 373
Cdd:cd01375 200 IASHTMNKNSSRSHCIFTIHL---------EAHSRTLSSE---KYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKS 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063716835 374 LTSLGKCINALAE-GSSHIPTRDSKLTRLLRDSFGGSARTSLIITIGPSARYHAETTSTIMFGQR 437
Cdd:cd01375 268 LSFLEQAIIALSDkDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASR 332
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
148-438 |
8.37e-66 |
|
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276827 [Multi-domain] Cd Length: 319 Bit Score: 224.69 E-value: 8.37e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 148 ESYKFDEVFTDTASQKRVYEGVAKPVVEGVLSGYNGTIMAYGQTGTGKTYTVgkIGKDDaaERGIMVRALEDIL-LNASS 226
Cdd:cd01376 44 LKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNATVFAYGSTGAGKTFTM--LGSPE--QPGLMPLTVMDLLqMTRKE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 227 A-SISVEISYLQLYMETIQDLLAPEKNNISINEDaKTGEVSVPGATVVNIQDLDHFLQVLQVGETNRHAANTKMNTESSR 305
Cdd:cd01376 120 AwALSFTMSYLEIYQEKILDLLEPASKELVIRED-KDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 306 SHAILTVYVrramnektekAKPESLgdkAIPRVRKSKLLIVDLAGSERINKSGTDGHMIEEAKFINLSLTSLGKCINALA 385
Cdd:cd01376 199 SHAVLLIKV----------DQRERL---APFRQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALN 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1063716835 386 EGSSHIPTRDSKLTRLLRDSFGGSARTSLIITIGPSARYHAETTSTIMFGQRA 438
Cdd:cd01376 266 KNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARS 318
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
129-602 |
2.58e-65 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 231.17 E-value: 2.58e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 129 VELQPEIKRLKLRKNNWNSES-----YKFDEVFTDTASQKRVYEGVAKPVVEGVLSGYNGTIMAYGQTGTGKTYTVGkig 203
Cdd:COG5059 32 PGELGERLINTSKKSHVSLEKskegtYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMS--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 204 kDDAAERGIMVRALEDIL----LNASSASISVEISYLQLYMETIQDLLAPEKNNISINEDAKTGeVSVPGATVVNIQDLD 279
Cdd:COG5059 109 -GTEEEPGIIPLSLKELFskleDLSMTKDFAVSISYLEIYNEKIYDLLSPNEESLNIREDSLLG-VKVAGLTEKHVSSKE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 280 HFLQVLQVGETNRHAANTKMNTESSRSHAILTVYVrramnEKTEKAKPESlgdkaiprvRKSKLLIVDLAGSERINKSGT 359
Cdd:COG5059 187 EILDLLRKGEKNRTTASTEINDESSRSHSIFQIEL-----ASKNKVSGTS---------ETSKLSLVDLAGSERAARTGN 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 360 DGHMIEEAKFINLSLTSLGKCINAL--AEGSSHIPTRDSKLTRLLRDSFGGSARTSLIITIGPSARYHAETTSTIMFGQR 437
Cdd:COG5059 253 RGTRLKEGASINKSLLTLGNVINALgdKKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 438 AMKIVNMVKLKEEFDY----ESLCRKLETQVDHLTAEVERQNKLRNSEKHELEKRLREC--ENSFAEAEKNAVTRSKFLE 511
Cdd:COG5059 333 AKSIKNKIQVNSSSDSsreiEEIKFDLSEDRSEIEILVFREQSQLSQSSLSGIFAYMQSlkKETETLKSRIDLIMKSIIS 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 512 KENTRLELSMKELLK---DLQLQKDQCDLMHDKAIQlEMKLKNTKQQQLENSAYeaklaDTSQVYEKKIAELVQRVEDEQ 588
Cdd:COG5059 413 GTFERKKLLKEEGWKyksTLQFLRIEIDRLLLLREE-ELSKKKTKIHKLNKLRH-----DLSSLLSSIPEETSDRVESEK 486
|
490
....*....|....*.
gi 1063716835 589 A--RSTNAEHQLTEMK 602
Cdd:COG5059 487 AskLRSSASTKLNLRS 502
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
129-434 |
7.84e-61 |
|
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276819 [Multi-domain] Cd Length: 345 Bit Score: 211.48 E-value: 7.84e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 129 VELQPEiKRLKLRKNNWNSES----YKFDEVFTDTASQKRVYEGVAKPVVEGVLSGYNGTIMAYGQTGTGKTYTV-GKIG 203
Cdd:cd01368 33 VVLHPP-KGSAANKSERNGGQketkFSFSKVFGPNTTQKEFFQGTALPLVQDLLHGKNGLLFTYGVTNSGKTYTMqGSPG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 204 kddaaERGIMVRALeDILLNaSSASISVEISYLQLYMETIQDLLAP-------EKNNISINEDaKTGEVSVPGATVVNIQ 276
Cdd:cd01368 112 -----DGGILPRSL-DVIFN-SIGGYSVFVSYIEIYNEYIYDLLEPspssptkKRQSLRLRED-HNGNMYVAGLTEIEVK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 277 DLDHFLQVLQVGETNRHAANTKMNTESSRSHAILTVYVRRAMNEktekAKPESLGDKAIPRVrkSKLLIVDLAGSERINK 356
Cdd:cd01368 184 STEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGD----SDGDVDQDKDQITV--SQLSLVDLAGSERTSR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 357 SGTDGHMIEEAKFINLSLTSLGKCINALAEG-----SSHIPTRDSKLTRLLRDSFGGSARTSLIITIGPSARYHAETTST 431
Cdd:cd01368 258 TQNTGERLKEAGNINTSLMTLGTCIEVLRENqlqgtNKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHV 337
|
...
gi 1063716835 432 IMF 434
Cdd:cd01368 338 MKF 340
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
148-439 |
2.65e-56 |
|
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276818 [Multi-domain] Cd Length: 328 Bit Score: 198.29 E-value: 2.65e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 148 ESYKFDEVFTDTASQKRVYEGVAKPVVEGVLSGYNGTIMAYGQTGTGKTYTVGKIGKDDAAERGIMVRALEDI--LLNAS 225
Cdd:cd01367 50 HTFRFDYVFDESSSNETVYRSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALAARDVfrLLNKL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 226 SA--SISVEISYLQLYMETIQDLLApEKNNISINEDAKtGEVSVPGATVVNIQDLDHFLQVLQVGETNRHAANTKMNTES 303
Cdd:cd01367 130 PYkdNLGVTVSFFEIYGGKVFDLLN-RKKRVRLREDGK-GEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQS 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 304 SRSHAILTVYVRRAmnektekAKPESLGdkaiprvrksKLLIVDLAGSERIN-KSGTDGHMIEEAKFINLSLTSLGKCIN 382
Cdd:cd01367 208 SRSHAILQIILRDR-------GTNKLHG----------KLSFVDLAGSERGAdTSSADRQTRMEGAEINKSLLALKECIR 270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063716835 383 ALAEGSSHIPTRDSKLTRLLRDSF-GGSARTSLIITIGPSARYHAETTSTIMFGQRAM 439
Cdd:cd01367 271 ALGQNKAHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADRVK 328
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
146-474 |
1.58e-45 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 178.98 E-value: 1.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 146 NSESYKFDEVFTDTASQKRVYEGVAKPVVEGVLSGYNGTIMAYGQTGTGKTYTVGKIGKDDAAE------RGIMVRALED 219
Cdd:PLN03188 130 NGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPANGLLEEhlsgdqQGLTPRVFER 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 220 ILLNASSASI---------SVEISYLQLYMETIQDLLAPEKNNISINEDAKTGeVSVPGATVVNIQDLDHFLQVLQVGET 290
Cdd:PLN03188 210 LFARINEEQIkhadrqlkyQCRCSFLEIYNEQITDLLDPSQKNLQIREDVKSG-VYVENLTEEYVKTMKDVTQLLIKGLS 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 291 NRHAANTKMNTESSRSHAILTVYVrramnekteKAKPESLGDkAIPRVRKSKLLIVDLAGSERINKSGTDGHMIEEAKFI 370
Cdd:PLN03188 289 NRRTGATSINAESSRSHSVFTCVV---------ESRCKSVAD-GLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNI 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 371 NLSLTSLGKCINALAEGSS-----HIPTRDSKLTRLLRDSFGGSARTSLIITIGPSARYHAETTSTIMFGQRAMKIVNMV 445
Cdd:PLN03188 359 NRSLSQLGNLINILAEISQtgkqrHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKA 438
|
330 340
....*....|....*....|....*....
gi 1063716835 446 KLKEEfdyeslcrkLETQVDHLTaEVERQ 474
Cdd:PLN03188 439 VVNEV---------MQDDVNFLR-EVIRQ 457
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
147-383 |
4.71e-13 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 68.14 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 147 SESYKFDEVFTDTASQKRVYEgVAKPVVEGVLSGYNG-TIMAYGQTGTGKTYTVgkigkddaaeRGIMVRALEDILlnas 225
Cdd:cd01363 17 SKIIVFYRGFRRSESQPHVFA-IADPAYQSMLDGYNNqSIFAYGESGAGKTETM----------KGVIPYLASVAF---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 226 sasisveisylqlymetiqdllapeknnisiNEDAKTGEVSVPGATVVNIQDLDHFLQVLQVGETNRHAAnTKMNTESSR 305
Cdd:cd01363 82 -------------------------------NGINKGETEGWVYLTEITVTLEDQILQANPILEAFGNAK-TTRNENSSR 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063716835 306 SHAILtvyvrramnektekakpeslgdkaiprvrkskLLIVDLAGSERINKsgtdghmieeakfinlSLTSLGKCINA 383
Cdd:cd01363 130 FGKFI--------------------------------EILLDIAGFEIINE----------------SLNTLMNVLRA 159
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
476-757 |
1.73e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 476 KLRNSEKHELEKRLRECENSFAEAEKNAVTrskfLEKENTRLELSMKELLKDLQLQKDQCDLMHDKAIQLEMKLKNTKQQ 555
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 556 QLENSAYEAKLADTSQVYEKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIHEQEKGNYQYQRELAEtthTYES 635
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE---LAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 636 KIAELQKKLEGENARSNAAEDQLRQMKRLISDRQVISQENEEANELKIKLEELSQmyestvdELQTVKLDYDDLLQQKEK 715
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE-------ALEEAAEEEAELEEEEEA 460
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1063716835 716 LGEEVRDMKERLLLEEKQRKQMESELSKLKKNLRESENVVEE 757
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
458-769 |
2.43e-11 |
|
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: 68.16 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 458 RKLETQVDHLTAEVER-------QNKLRNSEK-------HELEKRLRECENSFAEAE---KNAVTRSKFLEKENTRLELS 520
Cdd:TIGR02168 196 NELERQLKSLERQAEKaerykelKAELRELELallvlrlEELREELEELQEELKEAEeelEELTAELQELEEKLEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 521 MKELLKDLQ--------LQKDQCDLMHDKAIQLEmKLKNTKQQQLENSAYEAKLADTSQVYEKKIAELVQRVEDEQARST 592
Cdd:TIGR02168 276 VSELEEEIEelqkelyaLANEISRLEQQKQILRE-RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 593 NAEHQLTEMKNILSKQQKSIHEQEKgnyqyQRElaetthTYESKIAELQKKLEGENARSNAAEDQLRQMKRLIsDRQVIS 672
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEE-----QLE------TLRSKVAQLELQIASLNNEIERLEARLERLEDRR-ERLQQE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 673 QENEEANELKIKLEELSQMYESTVDELQTVKLDYDDLLQQKEKLGEEVRDMKERLLLEEKQRKQMESELSKLKKNLRESE 752
Cdd:TIGR02168 423 IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
330
....*....|....*..
gi 1063716835 753 NVVEEKRYMKEDLSKGS 769
Cdd:TIGR02168 503 GFSEGVKALLKNQSGLS 519
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
460-736 |
5.55e-10 |
|
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: 63.93 E-value: 5.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 460 LETQVDHLTAEVERQNKlrnsEKHELEKRLRECENSFAEAE-KNAVTRSKFLEKENTRLELSMKELLKDLQLqkdqcdlM 538
Cdd:TIGR02169 756 VKSELKELEARIEELEE----DLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNR-------L 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 539 HDKAIQLEMKLKNTKQQQLENSAYEAKLADTSQVYEKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIHEQEKG 618
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 619 nyqyQRELAETTHTYESKIAELQKKLEGENARSNAAEDQLRQMKRLISDRQVISQENEEANELKIKLEELSQMYESTVDE 698
Cdd:TIGR02169 905 ----IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQE 980
|
250 260 270
....*....|....*....|....*....|....*...
gi 1063716835 699 LQTVKLDYDDLLQQKEKLGEEVRDMKERLLLEEKQRKQ 736
Cdd:TIGR02169 981 YEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
550-838 |
8.50e-10 |
|
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: 63.15 E-value: 8.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 550 KNTKQQQLENSAYEAKLADtsqvYEKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIHEQEKGNYQYQRELAEt 629
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAE----LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE- 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 630 thtYESKIAELQKKLEGENARSNAAEDQL--------RQMKRLISDRQVISQENEEANELKIKLEELSQMYESTVDELQT 701
Cdd:TIGR02168 759 ---LEAEIEELEERLEEAEEELAEAEAEIeeleaqieQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 702 VKLDYDDLLQQKEKLGEEVRDMKERLLLEEKQRKQMESELSKLKKNLRESENVVEEKRYMKEDLSKG--SAESGAQTGSQ 779
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEElrELESKRSELRR 915
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063716835 780 RSQGLKKSLSGQRATMARLceEVGIQKILQLIkSEDLEVQIQAVKVVANLAAEEANQVK 838
Cdd:TIGR02168 916 ELEELREKLAQLELRLEGL--EVRIDNLQERL-SEEYSLTLEEAEALENKIEDDEEEAR 971
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
458-717 |
2.52e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 458 RKLETQVDHLTAEVERQNKLRNSEKHELE---KRLRECENSFAEAEKN---AVTRSKFLEKENTRLELSMKELLKDLQLQ 531
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEeaqAEEYELLAELARLEQDiarLEERRRELEERLEELEEELAELEEELEEL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 532 KDQCDLMHDKAIQLEMKLKNTKQQQLENsayEAKLADTSQVYEKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKS 611
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEA---EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 612 IHEQEKGNYQYQRELAETTHTYESKIAELQKKLEGENARSNAAEDQLRQMKRLISDRQVISQENEEANELKIKLEELSQM 691
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
250 260
....*....|....*....|....*.
gi 1063716835 692 YESTVDELQTVKLDYDDLLQQKEKLG 717
Cdd:COG1196 493 LLLLLEAEADYEGFLEGVKAALLLAG 518
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
421-771 |
6.35e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 60.14 E-value: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 421 SARYHAETTSTIMFGQRAMKIVNMVKLKEEFDYESLCRKLETQ-----VDHLTAEVERQNKLRNSEKHElEKRLRECENS 495
Cdd:pfam17380 257 TVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQErlrqeKEEKAREVERRRKLEEAEKAR-QAEMDRQAAI 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 496 FAEAEKNAVTRSKFLEKenTRLELSMKEL--LKDLQLQKDQCDLMHDKAIQLEMKLKNTKQQQLENSAYEAKLADTSQvy 573
Cdd:pfam17380 336 YAEQERMAMERERELER--IRQEERKRELerIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEER-- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 574 EKKIAElvQRVEDEQARSTNAEHQLTEMKNIlskqqksihEQEKgnyqyQRELAETthtyesKIAELQKKLEGENARSNA 653
Cdd:pfam17380 412 QRKIQQ--QKVEMEQIRAEQEEARQREVRRL---------EEER-----AREMERV------RLEEQERQQQVERLRQQE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 654 AEdqlRQMKRLISDRQVISQENEEANELKIKLEELSQMYESTVDElqtvkldyddllQQKEKLGEEVRDMKERLLLEEKQ 733
Cdd:pfam17380 470 EE---RKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEE------------ERKRKLLEKEMEERQKAIYEEER 534
|
330 340 350
....*....|....*....|....*....|....*...
gi 1063716835 734 RKQMESElsklkknlRESENVVEEKRYMKEDLSKGSAE 771
Cdd:pfam17380 535 RREAEEE--------RRKQQEMEERRRIQEQMRKATEE 564
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
483-849 |
1.15e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 483 HELEKRLRECEnsfAEAEKnAvtrSKFLEKENTRLELSMKELLKDLQLQKDQCDLMHDKAIQLEMKLKntkQQQLENSAY 562
Cdd:COG1196 196 GELERQLEPLE---RQAEK-A---ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELE---ELEAELAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 563 EAKLadtsQVYEKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIHEQEKGNYQYQRELAETthtyESKIAELQK 642
Cdd:COG1196 266 EAEL----EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL----EEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 643 KLEGENARSNAAEDQLRQMkrlisdRQVISQENEEANELKIKLEELSQMYESTVDELQTVKLDYDDLLQQKEKLGEEVRD 722
Cdd:COG1196 338 ELEELEEELEEAEEELEEA------EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 723 MKERLLLEEKQRKQMESELSKLKKNLRESENVVEEKRYMKEDLskgsAESGAQTGSQRSQGLKKSLSGQRATMARLCEEV 802
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL----EEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1063716835 803 GIQKILQLIKS--EDLEVQIQAVKVVANLAAEEANQVKIVEEGGVEALL 849
Cdd:COG1196 488 EAAARLLLLLEaeADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY 536
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
573-782 |
1.21e-08 |
|
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: 59.30 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 573 YEKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIHEQEKGNYQYQRELAETTHT---YESKIAELQKKLE---- 645
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqiLRERLANLERQLEelea 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 646 ----GENARSNAAEDQLRQMKRLISDRQVISQENEEANELKIKLEELSQMYESTVDELQTVKLDYDDLLQQKEKLGEEVR 721
Cdd:TIGR02168 324 qleeLESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063716835 722 DMKERLLLEEKQRKQMESELSKLKKNL-----RESENVVEEKRYMKEDLSKGSAESGAQTGSQRSQ 782
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKLeeaelKELQAELEELEEELEELQEELERLEEALEELREE 469
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
574-838 |
3.28e-08 |
|
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: 57.77 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 574 EKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIHEQEKGNYQYQRELAETTHTY-ESKIAELQK---KLEGENA 649
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAelsKLEEEVS 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 650 RSNAAEDQLRQ-MKRLISDRQVISQENEEANELKIKLEELSQMYESTVDELQTVKldyDDLLQQKEKLGEEVRDMKERLL 728
Cdd:TIGR02169 809 RIEARLREIEQkLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK---EELEEELEELEAALRDLESRLG 885
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 729 LEEKQRKQMESELSKLKKNLRESENVVEEKRYMKEDLskgsaesgaqtgSQRSQGLKKSLSGQRATMARLCEEVGIQKIL 808
Cdd:TIGR02169 886 DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL------------KAKLEALEEELSEIEDPKGEDEEIPEEELSL 953
|
250 260 270
....*....|....*....|....*....|..
gi 1063716835 809 QLIKS--EDLEVQIQAVKVVANLAAEEANQVK 838
Cdd:TIGR02169 954 EDVQAelQRVEEEIRALEPVNMLAIQEYEEVL 985
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
454-757 |
4.26e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 57.49 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 454 ESLCRKLETQVDHLtaevERQNKLRNSEKHELEKRLRECENSFAEAEKnavtRSKFLEKENTRLELSMKELLKDLQLQKD 533
Cdd:pfam01576 130 EAKIKKLEEDILLL----EDQNSKLSKERKLLEERISEFTSNLAEEEE----KAKSLSKLKNKHEAMISDLEERLKKEEK 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 534 QCDLMHDKAIQLEMKLKNTKQQQLENSAYEAKLADTSQVYEKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIh 613
Cdd:pfam01576 202 GRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDL- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 614 EQEKGNY----QYQRELAE--------------TTHTY-------ESKIAELQKKLEGENARSNAAEDQLRQmkRLISDR 668
Cdd:pfam01576 281 ESERAARnkaeKQRRDLGEelealkteledtldTTAAQqelrskrEQEVTELKKALEEETRSHEAQLQEMRQ--KHTQAL 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 669 QVISQENEEANELKIKLEELSQMYESTVDELQ----TVKLDYDDLLQQKEKLGEEVRDMKERLLLEEKQRKQMESELSKL 744
Cdd:pfam01576 359 EELTEQLEQAKRNKANLEKAKQALESENAELQaelrTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKL 438
|
330
....*....|...
gi 1063716835 745 KKNLRESENVVEE 757
Cdd:pfam01576 439 QSELESVSSLLNE 451
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
510-754 |
4.79e-08 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 57.06 E-value: 4.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 510 LEKENTRLELSMK----ELLKDLQLQKDQCDLMHDKAIQLEMKLKNTKQQQLENSAYEAKLADTSQVYEKKIAELVQRVE 585
Cdd:pfam05557 14 LQNEKKQMELEHKrariELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 586 DEQARSTNAEHQLTEMKNILSKQQKSIHEQE----KGNYQYQReLAETTHTYESKIAELQKKLEGENARSNAAEDQLRQM 661
Cdd:pfam05557 94 EKESQLADAREVISCLKNELSELRRQIQRAElelqSTNSELEE-LQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 662 KRLISDRQVISQENEEANELKIKLEELSQMyESTVDELQTVKLDYDDLLQQKEKLGEEVRDMKERLLLEEKQRKQ---ME 738
Cdd:pfam05557 173 KELEFEIQSQEQDSEIVKNSKSELARIPEL-EKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEaatLE 251
|
250
....*....|....*.
gi 1063716835 739 SELSKLKKNLRESENV 754
Cdd:pfam05557 252 LEKEKLEQELQSWVKL 267
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
555-757 |
7.72e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 7.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 555 QQLENSAYEAKLADTsqvyEKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIHEQEKGNYQYQRELAETthtyE 634
Cdd:COG4942 18 QADAAAEAEAELEQL----QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL----E 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 635 SKIAELQKKLEGE-------------NARSN------AAEDQLRQMKRLISDRQVISQENEEANELKIKLEELSQMYEST 695
Cdd:COG4942 90 KEIAELRAELEAQkeelaellralyrLGRQPplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063716835 696 VDELQTVKLDYDDLLQQKEKLGEEVRDMKERLLLEEKQRKQMESELSKLKKNLRESENVVEE 757
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
448-798 |
8.24e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 8.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 448 KEEFDYESLCRKLETQVDHLTAEVERQNKLRNSEKhELEKRLRECENSFAEAE--KNAVTRSKFLEKENTRLELS-MKEL 524
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLK-ELEKRLEELEERHELYEeaKAKKEELERLKKRLTGLTPEkLEKE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 525 LKDLQLQKdqcdlmhdKAIQLEMKLKNTKQQQLENSAYEAKLADTSQVYEKKIAELVQRVEDEQARSTNAEHQLTEMKNI 604
Cdd:PRK03918 393 LEELEKAK--------EEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRI 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 605 lSKQQKSIHEQEKGNYQYQRELaETTHTYESK----------IAELQKKLEGENARS-NAAEDQLRQMKR----LISDRQ 669
Cdd:PRK03918 465 -EKELKEIEEKERKLRKELREL-EKVLKKESEliklkelaeqLKELEEKLKKYNLEElEKKAEEYEKLKEklikLKGEIK 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 670 VISQENEEANELKIKLEELSQMYESTVDELQTV-----KLDYDDLLQQKEKLGE---------EVRDMKERLLLEEKQRK 735
Cdd:PRK03918 543 SLKKELEKLEELKKKLAELEKKLDELEEELAELlkeleELGFESVEELEERLKElepfyneylELKDAEKELEREEKELK 622
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063716835 736 QMESELSKLKKNLRESENVVEEKRYMKEDLSKGSAESGAQTGSQRSQGLKKSLSGQRATMARL 798
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEEL 685
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
470-842 |
1.32e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 470 EVERQNKLRNSE---------KHELEKRLRECENSFAEAEKNAVTRSKFLEKENTRLELSMKELLKDLQLQKDQCDLMHD 540
Cdd:PTZ00121 1186 EVRKAEELRKAEdarkaeaarKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHF 1265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 541 KAIQLEMKLKNTKQQQLENSAYEAKLADTS-QVYEKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIHEQEKGN 619
Cdd:PTZ00121 1266 ARRQAAIKAEEARKADELKKAEEKKKADEAkKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA 1345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 620 ----------------YQYQRELAETTHTYESKIAELQKKLEGENARSNAAEDQLRQMKRLISDRQVISQENEEANELKI 683
Cdd:PTZ00121 1346 eaakaeaeaaadeaeaAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKK 1425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 684 KLEELSQMYESTVDELQTVKLDyddllqQKEKLGEEVRDMKERLLLEEKQRKQMEselskLKKNLRESENVVEEKRYMKE 763
Cdd:PTZ00121 1426 KAEEKKKADEAKKKAEEAKKAD------EAKKKAEEAKKAEEAKKKAEEAKKADE-----AKKKAEEAKKADEAKKKAEE 1494
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063716835 764 DLSKGSAESGAQTGSQRSQGLKKSLSGQRATMARLCEEVgiQKILQLIKSEDLEvqiQAVKVVANLAAEEANQVKIVEE 842
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA--KKADEAKKAEEKK---KADELKKAEELKKAEEKKKAEE 1568
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
460-771 |
1.50e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 55.75 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 460 LETQVDHLTAEVERQNKLRNSEKHELEKRLRECENSFAEAEKNAvtrskflEKENTRLELSMKELLKDLQLQKDQCDLMH 539
Cdd:TIGR00618 561 LKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS-------EAEDMLACEQHALLRKLQPEQDLQDVRLH 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 540 DKAIQLEMKLKNTKQQQLENSAYEAKLADTSQVYEKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIHEQEKGN 619
Cdd:TIGR00618 634 LQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHI 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 620 YQYQRELAETTHTYESKIAELQKKLEGENARSNAAEDQLR-QMKRLISDRQVISQENEEANELKIKLEELSQMYESTVDE 698
Cdd:TIGR00618 714 EEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARtVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRL 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 699 LQTvklDYDDLLQQKEKLGEEVR-DMKERLLLEEKQRKQMESELSKLKKN------LRESENVVEEKRYMKEDLSKGSAE 771
Cdd:TIGR00618 794 REE---DTHLLKTLEAEIGQEIPsDEDILNLQCETLVQEEEQFLSRLEEKsatlgeITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
146-247 |
2.30e-07 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 51.07 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 146 NSESYKFDEVFTDTASQKRVYEGVaKPVVEGVLSGYNGTIMAYGQTGTGKTytvgkigkddaaeRGIMVRALEDILLNAS 225
Cdd:pfam16796 53 KNKSFSFDRVFPPESEQEDVFQEI-SQLVQSCLDGYNVCIFAYGQTGSGSN-------------DGMIPRAREQIFRFIS 118
|
90 100
....*....|....*....|....*.
gi 1063716835 226 S----ASISVEISYLQLYMETIQDLL 247
Cdd:pfam16796 119 SlkkgWKYTIELQFVEIYNESSQDLL 144
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
466-864 |
4.86e-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: 53.96 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 466 HLTAEVERQNKLRNSEKHELEKRLRECENSFAEAEKNAVTRSKFLEKENTRLELSMKELLKDLQLQKDQCDLMHDKAIQL 545
Cdd:pfam05483 328 QLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVEL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 546 E--MKLKNTKQQQLENSAYEAKLADTSQVYEKKIAELVQRVEDE--------QARSTNAEH---QLTEMKNILSKQQKSI 612
Cdd:pfam05483 408 EelKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEihdleiqlTAIKTSEEHylkEVEDLKTELEKEKLKN 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 613 HEQEKGNYQYQRELAETTHTYESKIAELQKKLEGENARSNAAEDQLRQMKRLisdrqvisqeNEEANELKIKLEELSQMY 692
Cdd:pfam05483 488 IELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENL----------EEKEMNLRDELESVREEF 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 693 ESTVDELQtVKLDyddllqqkeKLGEEVRDMKERLLLEEKQRKQMESELSKLKKNLRESENVVEEKRYMKEDLSKGSA-- 770
Cdd:pfam05483 558 IQKGDEVK-CKLD---------KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSae 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 771 ------------------ESGAQTGSQRSQGLKKSLSGQRATMARLCEEVGIQKI-----LQLIKSEDLEVQIQAVKVVA 827
Cdd:pfam05483 628 nkqlnayeikvnklelelASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAiadeaVKLQKEIDKRCQHKIAEMVA 707
|
410 420 430
....*....|....*....|....*....|....*..
gi 1063716835 828 NLAAEEANQVKIVEEGGVEaLLMLVQSSQNSTILRVA 864
Cdd:pfam05483 708 LMEKHKHQYDKIIEERDSE-LGLYKNKEQEQSSAKAA 743
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
470-771 |
7.64e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.95 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 470 EVERQNKLRNSEK----HELEKRLRECENSFAEAEKNAVTRSK---------------FLEKENTRLELSMKELLKDLQL 530
Cdd:pfam02029 6 EAARERRRRAREErrrqKEEEEPSGQVTESVEPNEHNSYEEDSelkpsgqggldeeeaFLDRTAKREERRQKRLQEALER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 531 QKDQCDLMHDKAIQLEMKLKNTKQQQLENSAYEAKLADTSQVYEKKIAELVQRVEDEQARST--NAEHQLTEMKNILSKQ 608
Cdd:pfam02029 86 QKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTevRQAEEEGEEEEDKSEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 609 QKSIHEQEKGNYQYQRELA--ETTHTYESKIAELQKKLEGENARSNAAED------QLRQMKRLISDRQVISQENEEANE 680
Cdd:pfam02029 166 AEEVPTENFAKEEVKDEKIkkEKKVKYESKVFLDQKRGHPEVKSQNGEEEvtklkvTTKRRQGGLSQSQEREEEAEVFLE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 681 LKIKLEEL--------SQMYESTVDELQTVKLDYDDLLQQKEKlgeevrdmKERLLLEEKQRKQMESELSKLKKNlrese 752
Cdd:pfam02029 246 AEQKLEELrrrrqekeSEEFEKLRQKQQEAELELEELKKKREE--------RRKLLEEEEQRRKQEEAERKLREE----- 312
|
330
....*....|....*....
gi 1063716835 753 nvvEEKRYMKEDLSKGSAE 771
Cdd:pfam02029 313 ---EEKRRMKEEIERRRAE 328
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
433-760 |
2.03e-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: 51.99 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 433 MFGQRAMKIVNMVKLKEEFDyeslcRKLETQVDHLtAEVERQNKLRNSEKHELEKRLRECENSFAEAEKNAVTRSKFLEK 512
Cdd:TIGR02169 150 MSPVERRKIIDEIAGVAEFD-----RKKEKALEEL-EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREY 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 513 ENTRLELSMKELLKDLQlqkdqcdlmhdkAIQLEMklkNTKQQQLENSAYEA-KLADTSQVYEKKIAELVQRVEDEqarS 591
Cdd:TIGR02169 224 EGYELLKEKEALERQKE------------AIERQL---ASLEEELEKLTEEIsELEKRLEEIEQLLEELNKKIKDL---G 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 592 TNAEHQLTEMKNILSKQQKSIHEQEKGNYQYQRELAETTHTYESKIAELQKKLEgenarsNAAEDQLRQMKRLISDRQVI 671
Cdd:TIGR02169 286 EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE------ELEREIEEERKRRDKLTEEY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 672 SQENEEANELKIKLEELSQMYESTVDELQTVKLDYDDLLQQKEKLGEEVRDMKERLLLEEKQRKQMESELSKLKKNLRES 751
Cdd:TIGR02169 360 AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL 439
|
....*....
gi 1063716835 752 ENVVEEKRY 760
Cdd:TIGR02169 440 EEEKEDKAL 448
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
459-752 |
2.10e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.94 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 459 KLETQVDHLTAEVERQNKLRNSEKHELEKRLRECENSFAEAEKnavtrskfLEKENTRLELSMKELLKDLQLQKDQCDLM 538
Cdd:TIGR04523 121 KLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND--------LKKQKEELENELNLLEKEKLNIQKNIDKI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 539 HDKAIQLEMKLKNTKQQQLENSAYEAKLAD---TSQVYEKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIHEQ 615
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKIQKNKSLESQISElkkQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 616 EKGNYQYQRELAETT---HTYESKIAELQKklEGENARSNAAEDQLRQMKRLISD--------RQVISQENEEANELKIK 684
Cdd:TIGR04523 273 QKELEQNNKKIKELEkqlNQLKSEISDLNN--QKEQDWNKELKSELKNQEKKLEEiqnqisqnNKIISQLNEQISQLKKE 350
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063716835 685 L-------EELSQMYESTVDELQTVKLDYDDLLQQKEKLGEEVRDMKERLLLEEKQRKQMESELSKLKKNLRESE 752
Cdd:TIGR04523 351 LtnsesenSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
436-856 |
4.02e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.27 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 436 QRAMKIVNMVKLKEEFDYESLCRKLETQVDHLTAEVERQNKLRNSEKHELEKRLRECENSFAEAEKNAVTRSKFLEKENT 515
Cdd:pfam15921 91 QRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 516 RLE------LSMKELLKDLQ--------------LQKDQCDLMHDKAI---------QLEMKLKNTK------QQQLE-- 558
Cdd:pfam15921 171 QIEqlrkmmLSHEGVLQEIRsilvdfeeasgkkiYEHDSMSTMHFRSLgsaiskilrELDTEISYLKgrifpvEDQLEal 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 559 NSAYEAKLADTSQVYEKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIHEQEKG-NYQYQR------------- 624
Cdd:pfam15921 251 KSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNqNSMYMRqlsdlestvsqlr 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 625 -ELAETTHTYESKIAELQKKLEGENARSNAA---EDQLRQMKRLISD--RQVISQENEEANELKIKLEELSQMYES---- 694
Cdd:pfam15921 331 sELREAKRMYEDKIEELEKQLVLANSELTEArteRDQFSQESGNLDDqlQKLLADLHKREKELSLEKEQNKRLWDRdtgn 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 695 --TVDELQTVKLDYDDLLQQKEKL----GEEVRDMKERLLLEEKQRKQMESELSKLKKNLresENVVEEKRYMKEDLS-- 766
Cdd:pfam15921 411 siTIDHLRRELDDRNMEVQRLEALlkamKSECQGQMERQMAAIQGKNESLEKVSSLTAQL---ESTKEMLRKVVEELTak 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 767 KGSAESGAQTGSQRSQGLKKSLSGQRATMARLCE-----EVGIQKILQLIKSEDLEVQIQAV------------KVVANL 829
Cdd:pfam15921 488 KMTLESSERTVSDLTASLQEKERAIEATNAEITKlrsrvDLKLQELQHLKNEGDHLRNVQTEcealklqmaekdKVIEIL 567
|
490 500
....*....|....*....|....*..
gi 1063716835 830 AAEEANQVKIVEEGGVEALLMLVQSSQ 856
Cdd:pfam15921 568 RQQIENMTQLVGQHGRTAGAMQVEKAQ 594
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
446-726 |
4.08e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 446 KLKEEFDYESLCRKLETQVDHLTAEVERQNKLRNSEKHELEkRLRECENSFAEAEKNAVTRSKFLEKENTRLELSMKELL 525
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT-ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 526 KDLQLQKDQCDLMHDKAIQLEMKLKN--TKQQQLENSAYEAK-----LADTSQVYEKKIAELVQRVEDEQARSTNAEHQL 598
Cdd:TIGR02168 796 EELKALREALDELRAELTLLNEEAANlrERLESLERRIAATErrledLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 599 TEMKNILSKQQKSIHEQEKGNYQYQ---RELAETTHTYESKIAELQKKLEGENARSNAAEDQLRQMKRLISDRQVISQEN 675
Cdd:TIGR02168 876 EALLNERASLEEALALLRSELEELSeelRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063716835 676 EEANELKIKLEELS-----------------------QMYESTVDELQTVKLDYDDLLQQKEKLGEEVRDMKER 726
Cdd:TIGR02168 956 AEALENKIEDDEEEarrrlkrlenkikelgpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
575-766 |
4.26e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 575 KKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIHEQEKGNYQYQRELAETTHTYE------SKIAELQKKLEGEN 648
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKeleelkEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 649 ARSNAAEDQLRQMKRLISDRQVISQENEE----ANELKIKLEE---LSQMYESTVDELQTVKL---DYDDLLQQKEKLGE 718
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEkvkeLKELKEKAEEyikLSEFYEEYLDELREIEKrlsRLEEEINGIEERIK 331
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063716835 719 EVRDMKERLLLEEKQRKQMESELSKLKKNLRESENV---VEEKRYMKEDLS 766
Cdd:PRK03918 332 ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAkakKEELERLKKRLT 382
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
446-856 |
5.38e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 446 KLKEEFDYESLCRKLET--QVDHLTAEVERQNKLRNSEKHELEKRLRECENSFAEAEKNAVTRSKFLEKENTRLElsmkE 523
Cdd:PTZ00121 1426 KAEEKKKADEAKKKAEEakKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAD----E 1501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 524 LLKDLQLQKdqcdlmhdKAIQLEMKLKNTKQQQLENSAYEAKLADTSQVYEKKIAELVQRVED----EQARSTNAEHQLT 599
Cdd:PTZ00121 1502 AKKAAEAKK--------KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkkaEEKKKAEEAKKAE 1573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 600 EMKNILSKQQKSIHEQEKGNYQYQRELAETTHTYEskiAELQKKLEGENARSNAAEDQLRQMKRLISDRQVISQENEEAN 679
Cdd:PTZ00121 1574 EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK---AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 680 ELK-------IKLEELSQMYESTVDELQTVKldyddllqqkeKLGEEVRDMKERLLLEEKQRKQMESELSKLKKNLRESE 752
Cdd:PTZ00121 1651 ELKkaeeenkIKAAEEAKKAEEDKKKAEEAK-----------KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE 1719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 753 NV--VEEKRYMKEDLSKGSAESGAQTGSQ--RSQGLKKSLSGQRATMARLCEEVGIQK---ILQLIKSEDLEVQIQAVKV 825
Cdd:PTZ00121 1720 ELkkAEEENKIKAEEAKKEAEEDKKKAEEakKDEEEKKKIAHLKKEEEKKAEEIRKEKeavIEEELDEEDEKRRMEVDKK 1799
|
410 420 430
....*....|....*....|....*....|.
gi 1063716835 826 VANLAAEEANqvkiVEEGGVEALLMLVQSSQ 856
Cdd:PTZ00121 1800 IKDIFDNFAN----IIEGGKEGNLVINDSKE 1826
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
443-765 |
6.38e-06 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 50.29 E-value: 6.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 443 NMVKLKEEFDYESLCRKLETQVDHLTAEVERQNKLRNSEKHELEKRL-RECENSFA------------EAEKNAVTRSKF 509
Cdd:pfam15964 348 NFEKTKALIQCEQLKSELERQKERLEKELASQQEKRAQEKEALRKEMkKEREELGAtmlalsqnvaqlEAQVEKVTREKN 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 510 -----LEKENTRL---ELSMKELLKDLQLQKDQCDLMHDKAIQLEMKLKNTKQQQLENSAYEAkladtsQVYEKKIAELV 581
Cdd:pfam15964 428 slvsqLEEAQKQLasqEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQEI------EKLGLELSESK 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 582 QRVEDEQARSTNAEHQLTEMKNILSKQQKSIH--EQEKGNYQ--YQRELAETTHTYESKIAELQKKLEGENARSNAAEDQ 657
Cdd:pfam15964 502 QRLEQAQQDAARAREECLKLTELLGESEHQLHltRLEKESIQqsFSNEAKAQALQAQQREQELTQKMQQMEAQHDKTVNE 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 658 LRQMkrLISDRQVISQENEEANELKIKLEELSQMYESTVDELQTVKLDYDDLLQQKEKLGEEVRD-----------MKER 726
Cdd:pfam15964 582 QYSL--LTSQNTFIAKLKEECCTLAKKLEEITQKSRSEVEQLSQEKEYLQDRLEKLQKRNEELEEqcvqhgrmherMKQR 659
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1063716835 727 LLLEEKQ----RKQMESELSKLKKNLRESENVVEEKRYMKEDL 765
Cdd:pfam15964 660 LRQLDKHcqatAQQLVQLLSKQNQLFKERQNLTEEVQSLRSQV 702
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
605-767 |
7.18e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 605 LSKQQKSIHEQEKGNYQYQrELAETTHTYESKIAELQKKLEgenaRSNAAEDQLRQMKRLISDRQVISQENEEANELKIK 684
Cdd:COG4717 73 LKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELE----ELREELEKLEKLLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 685 LEELSQMYEstvdELQTVKLDYDDLLQQKEKLGEEVRDMKERLLLEEKQR-KQMESELSKLKKNLRESENVVEEKRYMKE 763
Cdd:COG4717 148 LEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE 223
|
....
gi 1063716835 764 DLSK 767
Cdd:COG4717 224 ELEE 227
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
502-757 |
1.08e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 502 NAVTRSKFLEKENTRLELSMKELLKDLQLQKDQCDLMHDKAIQLEmKLKNTKQQQLENSAYEAKLADTSQVYEK------ 575
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEIDVASAEREIAELEAELERldassd 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 576 KIAELVQRVEDEQARSTNAEHQLTEMknilsKQQKSIHEQEKGNYQYQRELAETTHTYESKIAELQKKLEGENARSNAAE 655
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDEL-----KGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 656 DQL-RQMKRLISDRqvISQENEEANELKIKLEEL----SQMYESTVDELQTVKLDYDDLLQQKEKLGEE-----VRDMKE 725
Cdd:COG4913 761 DAVeRELRENLEER--IDALRARLNRAEEELERAmrafNREWPAETADLDADLESLPEYLALLDRLEEDglpeyEERFKE 838
|
250 260 270
....*....|....*....|....*....|..
gi 1063716835 726 RLlleekqRKQMESELSKLKKNLRESENVVEE 757
Cdd:COG4913 839 LL------NENSIEFVADLLSKLRRAIREIKE 864
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
421-806 |
1.41e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.35 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 421 SARYHAETTstimfgQRAMKIVNMVKLKEEFDYESLCRKLETQVDHLTAEVERQNKLRNSEKHELEKRLRECENSFAEAE 500
Cdd:pfam15921 289 SARSQANSI------QSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEAR 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 501 knaVTRSKFlEKENTRLELSMKELL-------KDLQLQKDQCDLMHDK---------AIQLEMKLKNTKQQQLE------ 558
Cdd:pfam15921 363 ---TERDQF-SQESGNLDDQLQKLLadlhkreKELSLEKEQNKRLWDRdtgnsitidHLRRELDDRNMEVQRLEallkam 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 559 ----NSAYEAKLADTSQVYE--KKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQK-------SIHEQEKGNYQYQRE 625
Cdd:pfam15921 439 ksecQGQMERQMAAIQGKNEslEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERtvsdltaSLQEKERAIEATNAE 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 626 LAETTHTYESKIAELQK-KLEGENARSNAAE-------------------DQLRQMKRLISDR-------QV-ISQENEE 677
Cdd:pfam15921 519 ITKLRSRVDLKLQELQHlKNEGDHLRNVQTEcealklqmaekdkvieilrQQIENMTQLVGQHgrtagamQVeKAQLEKE 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 678 ANELKIKLEELSQMYESTVDELQTVKLDYDDLLQQKEKLgeeVRDMKERLLLEEKQRKQMESELSKLKKNLRESENVVEE 757
Cdd:pfam15921 599 INDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL---VNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSED 675
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063716835 758 KRYMKEDLSKGSAE------------SGAQTGSQRSQGLKKSLSGQRATMARLCeeVGIQK 806
Cdd:pfam15921 676 YEVLKRNFRNKSEEmetttnklkmqlKSAQSELEQTRNTLKSMEGSDGHAMKVA--MGMQK 734
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
443-767 |
2.03e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 443 NMVKLKEEFDyeslcRKLETQVDHLTAEVERQNKLRNSEK---------HELEKRLRECENSFAEAEKnavtRSKFLEKE 513
Cdd:PRK03918 166 NLGEVIKEIK-----RRIERLEKFIKRTENIEELIKEKEKeleevlreiNEISSELPELREELEKLEK----EVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 514 NTRLELSMKELLKDLQlqkdqcdlmhdKAIQLEMKLKNTkqqqlensayeakladtsqvyEKKIAELVQRVEDeqarstn 593
Cdd:PRK03918 237 KEEIEELEKELESLEG-----------SKRKLEEKIREL---------------------EERIEELKKEIEE------- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 594 aehqltemkniLSKQQKSIHEQEKGNYQYqRELAETTHTYESKIAELQKKLEgenarsnAAEDQLRQMKRLISDrqvISQ 673
Cdd:PRK03918 278 -----------LEEKVKELKELKEKAEEY-IKLSEFYEEYLDELREIEKRLS-------RLEEEINGIEERIKE---LEE 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 674 ENEEANELKIKLEELSQMY---ESTVDELQTVKLDYDDLLQQKEKL-GEEVRDMKERLLLEEKQRKQMESELSKLKKNLR 749
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLeelEERHELYEEAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
330
....*....|....*...
gi 1063716835 750 ESENVVEEKRYMKEDLSK 767
Cdd:PRK03918 416 ELKKEIKELKKAIEELKK 433
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
458-756 |
2.28e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 458 RKLETQVDHLTAEVE-RQNKLRNSEKHELEK--RLRECENSFAEAEKNAVTRSKFLEKENTRLElsmkELLKDLQLQKDQ 534
Cdd:TIGR04523 36 KQLEKKLKTIKNELKnKEKELKNLDKNLNKDeeKINNSNNKIKILEQQIKDLNDKLKKNKDKIN----KLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 535 CDLMHDKAIQLEMKLKNTKQQQLENSAYEAKLADTSQVYEKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIhe 614
Cdd:TIGR04523 112 IKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI-- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 615 qEKGNYQYQRE--LAETTHTYESKIAELQKKLEGENARSNAAEDQLRQMKRLISDR------------QVISQENEEANE 680
Cdd:TIGR04523 190 -DKIKNKLLKLelLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKtteisntqtqlnQLKDEQNKIKKQ 268
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063716835 681 LKIKLEELSQ---MYESTVDELQTVKLDYDDLLQQKEKlgEEVRDMKERLLLEEKQRKQMESELSKLKKNLRESENVVE 756
Cdd:TIGR04523 269 LSEKQKELEQnnkKIKELEKQLNQLKSEISDLNNQKEQ--DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS 345
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
470-751 |
2.36e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.63 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 470 EVERQNKLRNSEKHELEKRLRECENSFAEAEKnavTRSKfLEKENTRLELSMKELLKDLQLQKDQCDLMHDKAIQLEMKL 549
Cdd:pfam01576 30 ELEKKHQQLCEEKNALQEQLQAETELCAEAEE---MRAR-LAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 550 KNTKQQQLENSAYEAKLADTSQVYEKKIAELVQRV---EDEQARSTNAEHQLTEMKNILSKQQKSIHEQEKgnyqyqrEL 626
Cdd:pfam01576 106 QDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDIlllEDQNSKLSKERKLLEERISEFTSNLAEEEEKAK-------SL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 627 AETTHTYESKIAELQKKLEGENARSNAAEDQLRQMKRLISDRQvisqenEEANELKIKLEELSQMYESTVDELQTVKLDY 706
Cdd:pfam01576 179 SKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQ------EQIAELQAQIAELRAQLAKKEEELQAALARL 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063716835 707 DDLLQQKEKLGEEVR-------DMKERLLLE-------EKQRKQMESELSKLKKNLRES 751
Cdd:pfam01576 253 EEETAQKNNALKKIReleaqisELQEDLESEraarnkaEKQRRDLGEELEALKTELEDT 311
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
563-777 |
2.71e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 563 EAKLADTSQVYEKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKqqksiHEQEKgnyqyqrelaETTHTYESKIAELQK 642
Cdd:PRK02224 201 EKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEE-----HEERR----------EELETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 643 KLEG-ENARSNAAE---DQLRQMKRLISDRQVISQENE----EANELKIKLEELSQMYESTVDELQTVKLDYDDLLQQKE 714
Cdd:PRK02224 266 TIAEtEREREELAEevrDLRERLEELEEERDDLLAEAGlddaDAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAE 345
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063716835 715 KLGEEVRDMKERLLLEEKQRKQMESELSKLKKNLRESENVVEEKRYMKEDLSKGSAESGAQTG 777
Cdd:PRK02224 346 SLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLG 408
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
634-797 |
4.37e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 634 ESKIAELQKKLEGENARSNAAEDQLRQMKRL---ISDRQVISQENEEANELKIKLEELSQMYESTVDELQTVKLDYDDLL 710
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAEldaLQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 711 ---QQKEKLGEEVRDMKERLLLEEKQRKQMESELSKLKKNLRESENVVE--EKRYMKEDLSKGSAESGAQTGSQRSQGLK 785
Cdd:COG4913 689 aleEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEaaEDLARLELRALLEERFAAALGDAVERELR 768
|
170
....*....|..
gi 1063716835 786 KSLSGQRATMAR 797
Cdd:COG4913 769 ENLEERIDALRA 780
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
574-747 |
6.34e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 574 EKKIAELvQRVEDEQARSTNAEHQLTEMKNILSKQQKSIhEQEKGNYQYQRELAETTHTYEskiaELQKKLEGENARSNA 653
Cdd:COG4717 77 EEELKEA-EEKEEEYAELQEELEELEEELEELEAELEEL-REELEKLEKLLQLLPLYQELE----ALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 654 AEDQLRQMKRLISDRQVISQENEEA-NELKIKLEELSqmyESTVDELQTVKLDYDDLLQQKEKLGEEVRDMKERLLLEEK 732
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELqEELEELLEQLS---LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170
....*....|....*
gi 1063716835 733 QRKQMESELSKLKKN 747
Cdd:COG4717 228 ELEQLENELEAAALE 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
481-757 |
6.35e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 481 EKHELEKRLRECENSFAEAEKNAVTRSKFLEKENTRLelSMKELLKDLqlqkdqcdlmhdkaIQLEMKLKNTKQQQLENS 560
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI--KLKELAEQL--------------KELEEKLKKYNLEELEKK 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 561 AYEA-KLADTSQVYEKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIHEQEKGNYQYQRELaetthtyESKIAE 639
Cdd:PRK03918 524 AEEYeKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL-------EERLKE 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 640 LQKKLEGENARSNAAEDQLRQMKRLISDRQVISQENEEANELKIKLEELsqmyESTVDELQTV--KLDYDDLLQQKEKLG 717
Cdd:PRK03918 597 LEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL----RKELEELEKKysEEEYEELREEYLELS 672
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1063716835 718 EEVRDMKERLLLEEKQRKQMESELSKLKKNLRESENVVEE 757
Cdd:PRK03918 673 RELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
503-767 |
9.39e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.50 E-value: 9.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 503 AVTRSKFLEKENTRLELSMKELLKDLQLQKDQCDLMHDKaiqLEMKLKNTKQQQLENSAYEAKLADTSQVYEKKIAELVQ 582
Cdd:pfam02463 161 EAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQE---LKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 583 RVEDEQARSTNAEHQLTEMKNILSKQQKSIHEQEKGNYQYQRELAETThtyeskiaELQKKLEGENARSNAAEDQLRQMK 662
Cdd:pfam02463 238 RIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE--------EELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 663 RLISDRQVISQENEEANELKIKLEELSqmyestVDELQTVKLDYDDllqQKEKLGEEVRDMKERLLLEEKQRKQMESELS 742
Cdd:pfam02463 310 VDDEEKLKESEKEKKKAEKELKKEKEE------IEELEKELKELEI---KREAEEEEEEELEKLQEKLEQLEEELLAKKK 380
|
250 260
....*....|....*....|....*
gi 1063716835 743 KLKKNLRESENVVEEKRYMKEDLSK 767
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEK 405
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
469-817 |
9.46e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 469 AEVERQNKLRNSEKHELEKRLRECENSFAEAEKnavtRSKFLEKENTRLElsmkellkdlQLQKDQcdlmhDKAIQLEMK 548
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKK----EIEELEEKVKELK----------ELKEKA-----EEYIKLSEF 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 549 LKNTKQQQLENSAYEAKLADTSQVYEKKIAELvqrvEDEQARSTNAEHQLTEMKNILSKQQKSIHEqekgnYQYQRELAE 628
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKEL----EEKEERLEELKKKLKELEKRLEELEERHEL-----YEEAKAKKE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 629 TTHTYESKIA-----ELQKKLEGENARSNAAEDQLRQMKRLISD-RQVISQENEEANELK-------IKLEELSQmyEST 695
Cdd:PRK03918 373 ELERLKKRLTgltpeKLEKELEELEKAKEEIEEEISKITARIGElKKEIKELKKAIEELKkakgkcpVCGRELTE--EHR 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 696 VDELQTVKLDYDDLLQQKEKLGEEVRDMKERLLLEEKQRKQmESELSKLKKNLRESENVVEE-KRYMKEDLSKGSAEsgA 774
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKlKKYNLEELEKKAEE--Y 527
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1063716835 775 QTGSQRSQGLKKSLSGQRATMARLcEEVGIQKILQLIKSEDLE 817
Cdd:PRK03918 528 EKLKEKLIKLKGEIKSLKKELEKL-EELKKKLAELEKKLDELE 569
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
540-783 |
1.11e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 540 DKAIQLEMKLKNTKQQQLENSAYEAKLADTSQVYEKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIHEQEKGN 619
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 620 YQYQRELAETTHTYESK-IAELqkkLEGENARSNAAEDQLRQMKRLISDRQVISQENEEANELKIKLEELSQMYESTVDE 698
Cdd:COG3883 96 YRSGGSVSYLDVLLGSEsFSDF---LDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 699 LQTVKLDYDDLLQQkekLGEEVRDMKERLLLEEKQRKQMESELSKLKKNLRESENVVEEKRYMKEDLSKGSAESGAQTGS 778
Cdd:COG3883 173 LEAQQAEQEALLAQ---LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGA 249
|
....*
gi 1063716835 779 QRSQG 783
Cdd:COG3883 250 GAAGA 254
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
458-746 |
1.47e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.22 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 458 RKLETQVDHLTAEVERQNKLRNSEKhelEKRLRECENSFAEAEKNAVTRSKF--LEKEN------TRLELSMKELlKDLQ 529
Cdd:COG5022 813 RSYLACIIKLQKTIKREKKLRETEE---VEFSLKAEVLIQKFGRSLKAKKRFslLKKETiylqsaQRVELAERQL-QELK 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 530 LQKDQCDLMHDKAIQLEMK-LKNTKQQQ----------LENSAYEAKLADTSQVYEKKIAELVQRVEDEQARSTNAE-HQ 597
Cdd:COG5022 889 IDVKSISSLKLVNLELESEiIELKKSLSsdlienlefkTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKlKE 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 598 LTEMKNILSKQqksiHEQEKGNYQYQRELaetTHTYESKIAELQKKLEGENARSNAAEDQLRQMKRLISDRQVISQENEE 677
Cdd:COG5022 969 TSEEYEDLLKK----STILVREGNKANSE---LKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTE 1041
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063716835 678 ANELKikleelsqmyestvdELQTVKLDYDDLLQQKEKLGEEVRDMKERLLLEEKQRKQMESELSKLKK 746
Cdd:COG5022 1042 LSILK---------------PLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKT 1095
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
469-780 |
1.96e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 469 AEVERQNKLRNSE--KHELEKRLRECENSFAEAEKNAVTRSKFLEKENTRLElsmkELLKDLQLQKDQCDLMHDKAIQLE 546
Cdd:PTZ00121 1572 AEEDKNMALRKAEeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE----ELKKAEEEKKKVEQLKKKEAEEKK 1647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 547 mKLKNTKQQQLENSAYEAKLADTSQVYEKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIHEQEKGNYQYQREL 626
Cdd:PTZ00121 1648 -KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 627 AETTHTYESKIAELQKKLEGENARSNAAEDQLRQMKRLISDRQVISQENEEANELKIKLEELSQMYESTVDE-LQTVKLD 705
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKkIKDIFDN 1806
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063716835 706 YDDLLQQKEKLGEEVRDMKERLLLEEKqrkqmesELSKLKKNLRESENVVEEKRYMKEDLSKGSAESGAQTGSQR 780
Cdd:PTZ00121 1807 FANIIEGGKEGNLVINDSKEMEDSAIK-------EVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEK 1874
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
563-847 |
2.00e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 563 EAKLADTSQVYEKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIHEQEKGNYQYQRELAETTHTYESKIAELQK 642
Cdd:PTZ00121 1211 ERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKK 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 643 KlegenarsnAAEDQLRQMKRLISDRQVISQENEEANELKIKLEELSQMYESTVDELQTVKLDYDDLLQQKEKLGEEVRD 722
Cdd:PTZ00121 1291 K---------ADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 723 MKERLLLEEKQRKQMESELSKLKKNLRESENVVEEKRYMKEDLSKGSAESGAQTGSQRSQGLKKslsgqRATMARLCEEV 802
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKK-----KAEEKKKADEA 1436
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1063716835 803 GiQKILQLIKSEDLEVQIQAVKVVANLA--AEEANQVKIVEEGGVEA 847
Cdd:PTZ00121 1437 K-KKAEEAKKADEAKKKAEEAKKAEEAKkkAEEAKKADEAKKKAEEA 1482
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
461-871 |
2.05e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.81 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 461 ETQVDHLTAEVERQ-NKLRNSEKHELEKRLRECENSFAEAEKNAVTRSKFLEKE-------------NTRLELSMKelLK 526
Cdd:TIGR01612 695 KAKLDDLKSKIDKEyDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGEinkdlnkiledfkNKEKELSNK--IN 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 527 DLQLQKDQCDLMHDKAIqlEMKLKNTKQQQLENSAYEaklaDTSQVYE--KKIAELVQRVEDEQARSTNaehqltEMKN- 603
Cdd:TIGR01612 773 DYAKEKDELNKYKSKIS--EIKNHYNDQINIDNIKDE----DAKQNYDksKEYIKTISIKEDEIFKIIN------EMKFm 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 604 ---ILSKQQKSIHeqekgnyqYQRELAETTHTYESKIAELQKKLEGE--NARSNAAEDQLRQMKRLISD-RQVISQENEE 677
Cdd:TIGR01612 841 kddFLNKVDKFIN--------FENNCKEKIDSEHEQFAELTNKIKAEisDDKLNDYEKKFNDSKSLINEiNKSIEEEYQN 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 678 ANELKiKLEELSQMYESTVDELQTVKLDYDDLlqqKEKLGEEVRDMKERLLLEEKQRKQMESELSKLKKNLresenvveE 757
Cdd:TIGR01612 913 INTLK-KVDEYIKICENTKESIEKFHNKQNIL---KEILNKNIDTIKESNLIEKSYKDKFDNTLIDKINEL--------D 980
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 758 KRYmkEDLSKGSAESGAQTGSQRSQGLKKSLSGQRATMARLC---EEVGIQKILQliKSEDLEVQIQAVKVVANLAAeea 834
Cdd:TIGR01612 981 KAF--KDASLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQfdeKEKATNDIEQ--KIEDANKNIPNIEIAIHTSI--- 1053
|
410 420 430
....*....|....*....|....*....|....*..
gi 1063716835 835 nqVKIVEEggVEALLMLVQSSQNSTILRVASGAIANL 871
Cdd:TIGR01612 1054 --YNIIDE--IEKEIGKNIELLNKEILEEAEINITNF 1086
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
471-758 |
2.56e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 471 VERQNKLRNSEKHELEKRLRECENSFAEAEKNAV---TRSKFLEKENTRLELSMKELLKDLQLQKDQCDLMHDKAIQLEM 547
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQqkdEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 548 KLKN----TKQQQLENSAYEAKLADTSQVYEKKIAELVQRVEDEQarstnaehQLTEMKNILSKQQKSIHEQEKGNYQYQ 623
Cdd:TIGR04523 455 IIKNldntRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK--------KLNEEKKELEEKVKDLTKKISSLKEKI 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 624 RELAETTHTYESKIAELQKKLEGENarSNAAEDQLRQMKRliSDRQVISQENEEANELKIK---LEELSQMYESTVDELQ 700
Cdd:TIGR04523 527 EKLESEKKEKESKISDLEDELNKDD--FELKKENLEKEID--EKNKEIEELKQTQKSLKKKqeeKQELIDQKEKEKKDLI 602
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063716835 701 TVKLDYDDLLQQKEKLGEEVRDMKERLLLEEKQRKQMESELSKLKKNLRESENVVEEK 758
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
470-753 |
2.74e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 470 EVERQNKLRNSEKHELEKRLRECENSFAEAEKNAVTRSKFLEKENTRLELSMKELLKdlqLQKDqcdlmhdkAIQLEMKL 549
Cdd:pfam01576 402 DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK---LSKD--------VSSLESQL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 550 KNTKQQQLENSAYEAKLADTSQVYEKKIAELVQRVEDEQARSTNAEH-------QLTEMKNILSKQQKSIHEQEKGNYQY 622
Cdd:pfam01576 471 QDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERqlstlqaQLSDMKKKLEEDAGTLEALEEGKKRL 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 623 QRELAETTHTYESKIAELQK------KLEGENARSNAAEDQLRQM-----------------KRLISDRQVISQENEEAN 679
Cdd:pfam01576 551 QRELEALTQQLEEKAAAYDKlektknRLQQELDDLLVDLDHQRQLvsnlekkqkkfdqmlaeEKAISARYAEERDRAEAE 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 680 ---------ELKIKLEELSQMYESTVDELQTVKLDYDDLLQQKEKLGEEVRDMkerllleEKQRKQMESELSKLKKNLRE 750
Cdd:pfam01576 631 areketralSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHEL-------ERSKRALEQQVEEMKTQLEE 703
|
...
gi 1063716835 751 SEN 753
Cdd:pfam01576 704 LED 706
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
544-757 |
2.81e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 544 QLEmKLKNTKQQQLENSAYEAKLADT------SQVYEKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIHEQEk 617
Cdd:PRK11281 44 QLD-ALNKQKLLEAEDKLVQQDLEQTlalldkIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTL- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 618 GNYQYQRELAETThtyeSKIAELQKKLEGENARSNAAEDQLRQMKRLISDRQVISQENEeaNELKIKLEELSQMYESTVD 697
Cdd:PRK11281 122 SLRQLESRLAQTL----DQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIR--NLLKGGKVGGKALRPSQRV 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063716835 698 ELQT--VKLDYDDLLQQKE--------KLGEEVRDmkerlLLEEKQRkQMESELSKLK-----KNLRESENVVEE 757
Cdd:PRK11281 196 LLQAeqALLNAQNDLQRKSlegntqlqDLLQKQRD-----YLTARIQ-RLEHQLQLLQeainsKRLTLSEKTVQE 264
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
463-587 |
3.26e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 463 QVDHLTAEVERQNKLRNSEKHELEKRLRECENSFAEaeknavtRSKFLEKENTRLELSMKEL---LKDLQLQKDQCDLMH 539
Cdd:PRK12704 65 EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR-------KLELLEKREEELEKKEKELeqkQQELEKKEEELEELI 137
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1063716835 540 DKAiqlemklkntkQQQLEN----SAYEAK---LADTSQVYEKKIAELVQRVEDE 587
Cdd:PRK12704 138 EEQ-----------LQELERisglTAEEAKeilLEKVEEEARHEAAVLIKEIEEE 181
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
631-758 |
3.86e-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: 43.37 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 631 HTYESKIAELQKKLEGENARSNAAEDQLRQMK-RLISDRQVISQENEEANELKIKLEELSQM---YESTVDELQTVKlDY 706
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEaRLEAAKTELEDLEKEIKRLELEIEEVEARikkYEEQLGNVRNNK-EY 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063716835 707 DDLLQQKEKLGEEVRDMKERLL-----LEEKQR--KQMESELSKLKKNLRESENVVEEK 758
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILelmerIEELEEelAELEAELAELEAELEEKKAELDEE 150
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
467-749 |
4.96e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 467 LTAEVERQNKLRNsEKHELEKRLRECENSFAEAEKnavTRSKfLEKENTRLELSMKELLKDLQLQKDQCDLMHDKAIQLE 546
Cdd:pfam01576 84 LEEEEERSQQLQN-EKKKMQQHIQDLEEQLDEEEA---ARQK-LQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 547 MKLKNTKQQQLENSAYEAKLADTSQVYEKKIAELVQRVEDE---------------------QARSTNAEHQLTEMKNIL 605
Cdd:pfam01576 159 ERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEekgrqelekakrklegestdlQEQIAELQAQIAELRAQL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 606 SKQQKSIH------EQEKG-NYQYQRELAETthtyESKIAELQKKLEGENARSNAAEDQ-------LRQMKRLISD---- 667
Cdd:pfam01576 239 AKKEEELQaalarlEEETAqKNNALKKIREL----EAQISELQEDLESERAARNKAEKQrrdlgeeLEALKTELEDtldt 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 668 ----RQVISQENEEANELKIKLEELSQMYESTVDELQTVKldyddlLQQKEKLGEEVRDMKERLLLEEKQRKQMESELSK 743
Cdd:pfam01576 315 taaqQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKH------TQALEELTEQLEQAKRNKANLEKAKQALESENAE 388
|
....*.
gi 1063716835 744 LKKNLR 749
Cdd:pfam01576 389 LQAELR 394
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
449-728 |
5.09e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.27 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 449 EEFDYESLcrKLETQVDHL---TAEVERQNKLRNSEKHELEKRLRECENSfAEAEKNAVTRSKFLEKENTRLElsmkell 525
Cdd:TIGR01612 568 EEENEDSI--HLEKEIKDLfdkYLEIDDEIIYINKLKLELKEKIKNISDK-NEYIKKAIDLKKIIENNNAYID------- 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 526 kdlqlqkdqcDLMHDKAIQLEMKLKNTkqqqleNSAYEAKLADTSQVYEKKI----AELVQRVEDEQARSTNAEHQLTEM 601
Cdd:TIGR01612 638 ----------ELAKISPYQVPEHLKNK------DKIYSTIKSELSKIYEDDIdalyNELSSIVKENAIDNTEDKAKLDDL 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 602 KNILSKQQKSIHEQEKGNYQYQRELAETT-HTYESKIAELQKKLEGE--NARSNAAEDQLRQMKRLISDRQVISQENEEA 678
Cdd:TIGR01612 702 KSKIDKEYDKIQNMETATVELHLSNIENKkNELLDIIVEIKKHIHGEinKDLNKILEDFKNKEKELSNKINDYAKEKDEL 781
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063716835 679 NELKIKLEELSQMY--ESTVDEL--QTVKLDYDdllQQKE-------------KLGEEVRDMKERLL 728
Cdd:TIGR01612 782 NKYKSKISEIKNHYndQINIDNIkdEDAKQNYD---KSKEyiktisikedeifKIINEMKFMKDDFL 845
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
454-763 |
5.38e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.27 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 454 ESLCRKLETQVDHLTAEVE-RQNKLRNSEKH--ELEKRLRECENSFAEAEKNAVTRSKFLEKENTRLELSmKELLKDLQL 530
Cdd:TIGR00606 715 ESELKKKEKRRDEMLGLAPgRQSIIDLKEKEipELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESA-KVCLTDVTI 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 531 QKDQCDLMHDKAIQLEMKLKNTKQQQLENSAYEakLADTSQVYEKKIAELVQRVEDEQARSTNAEHQLTEMK---NILSK 607
Cdd:TIGR00606 794 MERFQMELKDVERKIAQQAAKLQGSDLDRTVQQ--VNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKsktNELKS 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 608 QQKSIHEQEKGNYQYQRELAETTHTYESKIAELQKKLEGENARSNAAEDQLRQMKRLISDRQVISQENE-EANELKIKLE 686
Cdd:TIGR00606 872 EKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQdKVNDIKEKVK 951
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 687 ELSQMYESTVDELQTVKLDY---------------DDLLQQKEKLGEEVRDMKERLLLEEKQRKQMESELSKLKKNLRES 751
Cdd:TIGR00606 952 NIHGYMKDIENKIQDGKDDYlkqketelntvnaqlEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELK 1031
|
330
....*....|..
gi 1063716835 752 ENVVEEKRYMKE 763
Cdd:TIGR00606 1032 EVEEELKQHLKE 1043
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
458-759 |
9.52e-04 |
|
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: 43.17 E-value: 9.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 458 RKLETQVDHLTAEVERQNKLRNSEKHELEKRLRECENsfaeaeknavtrskfLEKENTRLELSMKELLKDLQLQKDQcdl 537
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEN---------------LEEKEMNLRDELESVREEFIQKGDE--- 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 538 mhdkaiqLEMKLKNTKQQQLENSAYEAKLADTSQVYEKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIHEQEK 617
Cdd:pfam05483 564 -------VKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEI 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 618 GNYQYQRELAETTHTYESKIAELQKKLEGENARSNAAEDQLRQMKRLISDRQVISQENEEANELKIK-----LEELSQMY 692
Cdd:pfam05483 637 KVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAemvalMEKHKHQY 716
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063716835 693 ESTVDELQTVKLDYDDLLQQ----KEKLGEEVRDMKERLLLEEKQRKQMESELSKLKKNLRESENVVEEKR 759
Cdd:pfam05483 717 DKIIEERDSELGLYKNKEQEqssaKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
511-744 |
1.15e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 511 EKENTRLELSMKELLKDLQLQKDQcdlmHDKAIQLEMKL---------KNTKQQQLENSAYEAKLADTSQVYEKKIAELV 581
Cdd:PRK04863 451 EQEATEELLSLEQKLSVAQAAHSQ----FEQAYQLVRKIagevsrseaWDVARELLRRLREQRHLAEQLQQLRMRLSELE 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 582 QRVEDEQarstNAEHQLTEMKNILSKQQKSIHEQEkgnyQYQRELaetthtyESKIAELQKKLEGENARSNAAEDQLRQM 661
Cdd:PRK04863 527 QRLRQQQ----RAERLLAEFCKRLGKNLDDEDELE----QLQEEL-------EARLESLSESVSEARERRMALRQQLEQL 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 662 KRLISDRQVISQENEEANElkiKLEELSQMYESTVDELQTVkldyDDLLQQkekLGEEVRDMK-ERLLLEEkQRKQMESE 740
Cdd:PRK04863 592 QARIQRLAARAPAWLAAQD---ALARLREQSGEEFEDSQDV----TEYMQQ---LLERERELTvERDELAA-RKQALDEE 660
|
....
gi 1063716835 741 LSKL 744
Cdd:PRK04863 661 IERL 664
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
454-786 |
1.17e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 454 ESLCRKLETQVDHLTAEVERQNKLRN--SEKHELEKRLRECENSFAEAEKNAVTRSKFLEKENTRLELSM---KELLKDL 528
Cdd:pfam10174 198 EVLLDQKEKENIHLREELHRRNQLQPdpAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTedrEEEIKQM 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 529 QLQKDQCDLMHDKAIQLEMKLkNTKQQQLEnsAYEAKL-------ADTSQ---VYEKKIAELVQRVEDEQARSTNAEHQL 598
Cdd:pfam10174 278 EVYKSHSKFMKNKIDQLKQEL-SKKESELL--ALQTKLetltnqnSDCKQhieVLKESLTAKEQRAAILQTEVDALRLRL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 599 TEMKNILSKQQKSIHE--QEKGNYQYQ-RELAETTHTYESKIAELQKKLEGenarsnaAEDQLRQmkrliSDRQVisqen 675
Cdd:pfam10174 355 EEKESFLNKKTKQLQDltEEKSTLAGEiRDLKDMLDVKERKINVLQKKIEN-------LQEQLRD-----KDKQL----- 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 676 eeaNELKIKLEELSQMYESTVDELQTVkldyDDLLQQKEKLGEEVRDMKERlllEEKQRKQmesELSKLKKNLRESENVV 755
Cdd:pfam10174 418 ---AGLKERVKSLQTDSSNTDTALTTL----EEALSEKERIIERLKEQRER---EDRERLE---ELESLKKENKDLKEKV 484
|
330 340 350
....*....|....*....|....*....|.
gi 1063716835 756 EEKRYMKEDLSKGSAESGAQTGSQRSQGLKK 786
Cdd:pfam10174 485 SALQPELTEKESSLIDLKEHASSLASSGLKK 515
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
575-820 |
1.23e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 575 KKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIHEQEKGNYQYQRELAETTHTYESKIAELQKKLEGENARSNAA 654
Cdd:pfam01576 15 QKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 655 EDQLRQMKRLISDRQViSQENEEANELKIKLEELSQmyESTVDELQTVKLDYDD----LLQQKEKLGEEVRDMKERLLLE 730
Cdd:pfam01576 95 QNEKKKMQQHIQDLEE-QLDEEEAARQKLQLEKVTT--EAKIKKLEEDILLLEDqnskLSKERKLLEERISEFTSNLAEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 731 E-------KQRKQMESELSKLKKNLRESENVVEEKRYMKEDLSKGSAESGAQTGSQRSQ--GLKKSLSGQ----RATMAR 797
Cdd:pfam01576 172 EekakslsKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQiaELRAQLAKKeeelQAALAR 251
|
250 260
....*....|....*....|...
gi 1063716835 798 LcEEVGIQKILQLIKSEDLEVQI 820
Cdd:pfam01576 252 L-EEETAQKNNALKKIRELEAQI 273
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
573-824 |
1.56e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 573 YEKKIAELVQRVEDEQARSTNAEHQLTEmkniLSKQQKSIHEQEkgnyqyqRELAETTHTYESKIAELQKKLEGENARSN 652
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAE----LRKELEELEEEL-------EQLRKELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 653 AAEDQLRQmkrlisdrqvisqENEEANELKIKLEELSQMyestVDELQTVKldyDDLLQQKEKLGEEVRDMKERLLLEEK 732
Cdd:TIGR02168 744 QLEERIAQ-------------LSKELTELEAEIEELEER----LEEAEEEL---AEAEAEIEELEAQIEQLKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 733 QRKQMESELSKLKKNLRESENVVEEKRYMKEDLSKGSAESGAQTGSQRSQGLkkSLSGQRATMARLCEEVGIQKILQLIK 812
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE--SLAAEIEELEELIEELESELEALLNE 881
|
250
....*....|..
gi 1063716835 813 SEDLEVQIQAVK 824
Cdd:TIGR02168 882 RASLEEALALLR 893
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
448-746 |
1.74e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 448 KEEFDYESLCRKLETQVD---HLTAEVE----RQNKLRNSEKH------------ELEKRLRECEnsfaEAEKNAVTRSK 508
Cdd:PRK04863 304 AEQYRLVEMARELAELNEaesDLEQDYQaasdHLNLVQTALRQqekieryqadleELEERLEEQN----EVVEEADEQQE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 509 FLEKENTRLELSMKELLKDLQLQKDQCDLMHDKAIQLemklkNTKQQQLENSAYEAKLADTSqvyekkIAELVQRVEDEQ 588
Cdd:PRK04863 380 ENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQY-----QQAVQALERAKQLCGLPDLT------ADNAEDWLEEFQ 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 589 ARSTNAEHQLTEMKNILSkqqksiheqekgnyqyqreLAETTHTYESKIAELQKKLEGENARSNAAE------------- 655
Cdd:PRK04863 449 AKEQEATEELLSLEQKLS-------------------VAQAAHSQFEQAYQLVRKIAGEVSRSEAWDvarellrrlreqr 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 656 ---DQLRQMKRLISDRQVISQENEEANELkikLEELSQMYESTVDELQTVKLDYDDLLQQKEKLGEEVRDMKERLLLEEK 732
Cdd:PRK04863 510 hlaEQLQQLRMRLSELEQRLRQQQRAERL---LAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQ 586
|
330
....*....|....
gi 1063716835 733 QRKQMESELSKLKK 746
Cdd:PRK04863 587 QLEQLQARIQRLAA 600
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
567-778 |
1.85e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 567 ADTS-QVYEKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIHEQEKGNYQYQRELAETthtyESKIAELQKKLe 645
Cdd:COG3883 14 ADPQiQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA----EAEIEERREEL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 646 GENARS------------------NAAE--DQLRQMKRLIS-DRQVIsqenEEANELKIKLEELSQMYESTVDELQTVKL 704
Cdd:COG3883 89 GERARAlyrsggsvsyldvllgseSFSDflDRLSALSKIADaDADLL----EELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063716835 705 DYDDLLQQKEKLGEEVRDMKERLLLEEKQRKQMESELSKLKKNLRESENVVEEKRYMKEDLSKGSAESGAQTGS 778
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
453-760 |
2.30e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 453 YESLCRKLETQVDHLtaevERQNKLRNSEKHELEKRLRECENSFAEAEKNAVTRSKFLEKENTRLELSMKELLKDLQLQK 532
Cdd:TIGR04523 209 KIQKNKSLESQISEL----KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIK 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 533 DQCDLMHDKAIQLEmKLKNTKQQQLEN------SAYEAKLADT-SQVY--EKKIAELVQRVEDEQARSTNAEHQLTEMKN 603
Cdd:TIGR04523 285 ELEKQLNQLKSEIS-DLNNQKEQDWNKelkselKNQEKKLEEIqNQISqnNKIISQLNEQISQLKKELTNSESENSEKQR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 604 ILSKQQKSIHEQEKGNYQYQRE---LAETTHTYESKI-------AELQKKLEGENARSNAAEDQLRQMKRLISD-RQVIS 672
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEiknLESQINDLESKIqnqeklnQQKDEQIKKLQQEKELLEKEIERLKETIIKnNSEIK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 673 QENEEANELKIKLEELSQMYESTVDELQTVKLDY---------------------DDLLQQKEKLGEEVRDMKERLLLEE 731
Cdd:TIGR04523 444 DLTNQDSVKELIIKNLDNTRESLETQLKVLSRSInkikqnleqkqkelkskekelKKLNEEKKELEEKVKDLTKKISSLK 523
|
330 340
....*....|....*....|....*....
gi 1063716835 732 KQRKQMESELSKLKKNLRESENVVEEKRY 760
Cdd:TIGR04523 524 EKIEKLESEKKEKESKISDLEDELNKDDF 552
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
426-750 |
2.55e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 426 AETTSTIMFGQRAMKIVNMVKLKEEFDYESLCRKLETQVDHLTAEVERQNKLRNSEKH--ELEKRLRECENSFAEAEKNA 503
Cdd:TIGR00606 415 ADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRilELDQELRKAERELSKAEKNS 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 504 VTRSKFLEKENTRLE-LSMKELLKDLQLQKDQCDLMHDKAIQLEM--KLKNTKQQQLENSAYEAKLADTSQVYEKKIAEL 580
Cdd:TIGR00606 495 LTETLKKEVKSLQNEkADLDRKLRKLDQEMEQLNHHTTTRTQMEMltKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQ 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 581 VQRVEDEQARSTNaehqltEMKNILSKQQKSIHEQEKGNYQYQRELaetthtyESKIAELQKkLEGENARSNAAEDQLRQ 660
Cdd:TIGR00606 575 LEDWLHSKSKEIN------QTRDRLAKLNKELASLEQNKNHINNEL-------ESKEEQLSS-YEDKLFDVCGSQDEESD 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 661 MKRLisdRQVISQENEEANELKIKLEELSQMYESTVDELQTVKLDYDDLLQQKEKLGEEVRDMKERLLLEEKQRKQMESE 740
Cdd:TIGR00606 641 LERL---KEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESE 717
|
330
....*....|
gi 1063716835 741 LSKLKKNLRE 750
Cdd:TIGR00606 718 LKKKEKRRDE 727
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
447-758 |
3.89e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 447 LKEEFDYESLCRKLETQVDHLTAEVERQNKLRnsekhelEKRLRECENSFAEAEKNAVTrskfLEKENTRLELSMKELLK 526
Cdd:COG5185 235 LKGFQDPESELEDLAQTSDKLEKLVEQNTDLR-------LEKLGENAESSKRLNENANN----LIKQFENTKEKIAEYTK 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 527 DLQLQKDQcdlmhdkaiqlemklkNTKQQQLENSAYEAKLADTSQVYEKKIAELVQRVEDEQARSTNAEHQL-TEMKNIL 605
Cdd:COG5185 304 SIDIKKAT----------------ESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIkEEIENIV 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 606 SKQQKSIHEQEKGNYQYQRElAETTHTYESKIAELQKKLEGENARSNAAEDQLRQMKRLISDRQVISQENEEANELKIKL 685
Cdd:COG5185 368 GEVELSKSSEELDSFKDTIE-STKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNEL 446
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063716835 686 EELSQMYESTVDELQTVKLDyddllQQKEKLGEEVRDMKERLlleEKQRKQMESELSKLKKNLRESENVVEEK 758
Cdd:COG5185 447 ISELNKVMREADEESQSRLE-----EAYDEINRSVRSKKEDL---NEELTQIESRVSTLKATLEKLRAKLERQ 511
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
664-764 |
4.60e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.39 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 664 LISDRQVISQENEEANELKIKLEELSQMYESTVDELQTVK-----LDYDDLLQQKEKLGEEVRDMKERL-LLEEK--QRK 735
Cdd:smart00787 156 LKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEdeledCDPTELDRAKEKLKKLLQEIMIKVkKLEELeeELQ 235
|
90 100 110
....*....|....*....|....*....|....*.
gi 1063716835 736 QMESELSKLKK-------NLRESENVVEEKRYMKED 764
Cdd:smart00787 236 ELESKIEDLTNkkselntEIAEAEKKLEQCRGFTFK 271
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
668-752 |
4.67e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 668 RQVISQENEEANELKIKLEELSQMYESTVDELQTVKLD----YDDLLQQKEKLGEEVRDMKERLLLEEKQR-KQMESELS 742
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEaeklKEELEEKKEKLQEEEDKLLEEAEKEAQQAiKEAKKEAD 587
|
90
....*....|
gi 1063716835 743 KLKKNLRESE 752
Cdd:PRK00409 588 EIIKELRQLQ 597
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
577-782 |
4.82e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 577 IAELVQ--RVEDEQARSTNA----EHQLTEMKNILSKQQKSIHEQEkgnyqyQRELAETTHTYESKIAELQKKLEGENAR 650
Cdd:PRK02224 155 IDDLLQlgKLEEYRERASDArlgvERVLSDQRGSLDQLKAQIEEKE------EKDLHERLNGLESELAELDEEIERYEEQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 651 SNAAEDQLRQMKRLISD----RQVI---------SQEN------------EEANELKIKLEELSQMYESTVDELQTVKLD 705
Cdd:PRK02224 229 REQARETRDEADEVLEEheerREELetleaeiedLRETiaeterereelaEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063716835 706 YDDLLQQKEKLGEEVRDMKERLLLEEKQRKQMESELSKLKKNLRESENVVEEKRYMKEDLSKGSAESGAQTGSQRSQ 782
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREE 385
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
446-663 |
5.16e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 446 KLKEEFDYESLCRKLETQVDHLT---AEVERQNKLRNSEKHELEKRLRECENSFAEAEKNAVTRSKFLEKENTRLELSMK 522
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEerrRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 523 ELLKDLQLQKDQCDLMHDKAIQLEMKLkntkQQQLENSAYEAKLADTSQVYEKKIAELVQRVEDEQARSTNAEHQLTEMK 602
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEAL----RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063716835 603 NILSKQQKSIHEQEKGNYQYQRELAETTHTYESKIAELQKKLEGENARSNAAEDQLRQMKR 663
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Arm |
pfam00514 |
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ... |
839-873 |
5.27e-03 |
|
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.
Pssm-ID: 425727 [Multi-domain] Cd Length: 41 Bit Score: 35.51 E-value: 5.27e-03
10 20 30
....*....|....*....|....*....|....*
gi 1063716835 839 IVEEGGVEALLMLVQSsQNSTILRVASGAIANLAM 873
Cdd:pfam00514 8 VIEAGAVPPLVRLLSS-PDEEVQEEAAWALSNLAA 41
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
515-786 |
5.27e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 515 TRLELSMKELlkdlqlQKDQCDLMHDKAIqLEMKLKNTKQQQLENSAYEAKLADTSQVYEKKIAELVQRVEDEQARSTNA 594
Cdd:pfam01576 22 QKAESELKEL------EKKHQQLCEEKNA-LQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 595 EHQLTEMKNILSKQQKSIHEQEKGNYQYQRELAetthTYESKIaelqKKLEGENARSNAAEDQLRQMKRLISDR--QVIS 672
Cdd:pfam01576 95 QNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKV----TTEAKI----KKLEEDILLLEDQNSKLSKERKLLEERisEFTS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 673 QENEEANELKiKLEELSQMYESTVDELQtvkldydDLLQQKEKLGEEVrdmkerllleEKQRKQMESELSKLKKNLRESE 752
Cdd:pfam01576 167 NLAEEEEKAK-SLSKLKNKHEAMISDLE-------ERLKKEEKGRQEL----------EKAKRKLEGESTDLQEQIAELQ 228
|
250 260 270
....*....|....*....|....*....|....*..
gi 1063716835 753 NVVEEKRYM---KEDLSKGSAESGAQTGSQRSQGLKK 786
Cdd:pfam01576 229 AQIAELRAQlakKEEELQAALARLEEETAQKNNALKK 265
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
460-790 |
5.28e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 460 LETQVDHLtAEVerQNKLRNSEK--------HELEKRLRECENSFAEAEKNAVTRskflEKENTRLELSMKEL---LKDL 528
Cdd:COG3096 329 YQAASDHL-NLV--QTALRQQEKieryqedlEELTERLEEQEEVVEEAAEQLAEA----EARLEAAEEEVDSLksqLADY 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 529 QlqkDQCDLMHDKAIQLEMKLKNTKQQQ---------LENSA-YEAKLADTSQVYEKKIAELVQRVEDEQARSTNAEHQL 598
Cdd:COG3096 402 Q---QALDVQQTRAIQYQQAVQALEKARalcglpdltPENAEdYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAY 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 599 TEMKNILSKQQKS-IHEQEKG---NYQYQRELAETTHTYESKIAELQKKLEgenaRSNAAEDQLRQMKRLISdRQVISQE 674
Cdd:COG3096 479 ELVCKIAGEVERSqAWQTAREllrRYRSQQALAQRLQQLRAQLAELEQRLR----QQQNAERLLEEFCQRIG-QQLDAAE 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 675 N--EEANELKIKLEELSQMYESTVDELQTVKLDYDDLLQQKEKLGE------EVRDMKERL------LLEEKQR--KQME 738
Cdd:COG3096 554 EleELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAArapawlAAQDALERLreqsgeALADSQEvtAAMQ 633
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1063716835 739 SELSKLKKNLRESENVVEEKRYMKEDLSKGSAESGAQtgSQRSQGLKKSLSG 790
Cdd:COG3096 634 QLLEREREATVERDELAARKQALESQIERLSQPGGAE--DPRLLALAERLGG 683
|
|
| BAR_Rvs167p |
cd07599 |
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon ... |
493-660 |
5.69e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon starvation protein 167 and similar proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of fungal proteins with similarity to Saccharomyces cerevisiae Reduced viability upon starvation protein 167 (Rvs167p) and Schizosaccharomyces pombe Hob1 (homolog of Bin1). S. cerevisiae Rvs167p plays a role in regulation of the actin cytoskeleton, endocytosis, and sporulation. It forms a heterodimer with another BAR domain protein Rvs161p. Rvs161p and Rvs167p share common functions but are not interchangeable. Their BAR domains cannot be replaced with each other and the overexpression of one cannot suppress the mutant phenotypes of the other. Rvs167p also interacts with the GTPase activating protein (GAP) Gyp5p, which is involved in ER to Golgi vesicle trafficking. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153283 [Multi-domain] Cd Length: 216 Bit Score: 39.55 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 493 ENSFAEAEKNavtrSKFLEKENTRLELSMKELLkDLQLQKDQCdlmhdkAIQLEMKLKNTKQQQLENSAYEAKLADTSQv 572
Cdd:cd07599 8 EKDFKSLEKS----LKKLIEQSKAFRDSWRSIL-THQIAFAKE------FAELYDPIVGPKESVGSHPAPESTLARLSR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 573 YEKKIAELVQRVE-DEQARSTNAEHQLTEMKNILSKQQKSIHEQEKGNYQYQR----------ELAETTHTYESKIAELQ 641
Cdd:cd07599 76 YVKALEELKKELLeELEFFEERVILPAKELKKYIKKIRKTIKKRDHKKLDYDKlqnklnkllqKKKELSLKDEKQLAKLE 155
|
170
....*....|....*....
gi 1063716835 642 KKLEGENARSNAAEDQLRQ 660
Cdd:cd07599 156 RKLEEAKEEYEALNELLKS 174
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
644-789 |
5.71e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.13 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 644 LEGENArSNAAEDQLRQMKRLIsdRQVISQENEEANELKIKLEELSQMYESTVDELQtvkldyddllqqkeklgEEVRDM 723
Cdd:pfam09787 39 LDSSTA-LTLELEELRQERDLL--REEIQKLRGQIQQLRTELQELEAQQQEEAESSR-----------------EQLQEL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063716835 724 KERLLLEEKQRKQMESELSKLKknlresenvvEEKRYMKEDLSKGSA-------ESGAQTGSQRSQGLKKSLS 789
Cdd:pfam09787 99 EEQLATERSARREAEAELERLQ----------EELRYLEEELRRSKAtlqsrikDREAEIEKLRNQLTSKSQS 161
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
516-716 |
5.74e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 516 RLELSMKELLKDLQLQKDQCDLMHDKAIQLEMKLKNTKQQQLENSayeakLADTSQVYEKKIAELVQRVEDEQARSTNAE 595
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 596 HQLTEMKNILSKQQKSIHE--QEKGNYQYQRELAETthtyESKIAELQKKLEGENARSNAAEDQLRQMKRLISDR--QVI 671
Cdd:COG3206 240 ARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAEL----EAELAELSARYTPNHPDVIALRAQIAALRAQLQQEaqRIL 315
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063716835 672 SQENEEANELKIKLEELSQMYESTVDELQT-----VKLD------------YDDLLQQKEKL 716
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEARLAElpeleAELRrlerevevarelYESLLQRLEEA 377
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
518-758 |
5.90e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 518 ELSMKELLKDLQlqkDQCDLMHDKAIQLEMKLKNTKQQQLENSAYEAKLADTSQVYEKKIAELVQRVE----DEQARSTN 593
Cdd:TIGR00606 690 EAELQEFISDLQ---SKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQkvnrDIQRLKND 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 594 AEHQLTEMKNILSKQQKSihEQEKGNYQYQRELAETTHTYESKIAELQKKLEGENArsNAAEDQLRQMKRLISDR-QVIS 672
Cdd:TIGR00606 767 IEEQETLLGTIMPEEESA--KVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDL--DRTVQQVNQEKQEKQHElDTVV 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 673 QENEEANELKIKLEELSQMYESTVDELQTVKLDYDDLLQQKEKLGEEVRDMK---ERLLLEEKQRKQMESELSK-LKKNL 748
Cdd:TIGR00606 843 SKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELStevQSLIREIKDAKEQDSPLETfLEKDQ 922
|
250
....*....|
gi 1063716835 749 RESENVVEEK 758
Cdd:TIGR00606 923 QEKEELISSK 932
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
412-862 |
5.97e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 412 TSLIITIGPSARYHAETTSTIMFGQRAMKIVN--MVKLKEEFDYE-SLCRKLETQVDHL---TAEVERQnKLRNSEKHEL 485
Cdd:pfam15921 485 TAKKMTLESSERTVSDLTASLQEKERAIEATNaeITKLRSRVDLKlQELQHLKNEGDHLrnvQTECEAL-KLQMAEKDKV 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 486 EKRLRE-CENSFAEAEKNAVTRSKF------LEKE--NTRLELSMKELLKDLQLQKDQCDLMHDKAIQLE-MKLKNTKQQ 555
Cdd:pfam15921 564 IEILRQqIENMTQLVGQHGRTAGAMqvekaqLEKEinDRRLELQEFKILKDKKDAKIRELEARVSDLELEkVKLVNAGSE 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 556 QLEnSAYEAKLADTSQVYEKKIA--ELVQRVEDEQARSTNAEHQLTEMK---NILSKQQKSIheqekgnyqyQRELAETT 630
Cdd:pfam15921 644 RLR-AVKDIKQERDQLLNEVKTSrnELNSLSEDYEVLKRNFRNKSEEMEtttNKLKMQLKSA----------QSELEQTR 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 631 HTYES---------KIA-ELQKKLEGENARSNAAEDQLRQMKrlisdrQVISQENEEANELKIKLEELSQMYESTVDELQ 700
Cdd:pfam15921 713 NTLKSmegsdghamKVAmGMQKQITAKRGQIDALQSKIQFLE------EAMTNANKEKHFLKEEKNKLSQELSTVATEKN 786
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 701 TVKLDYDDLLQQKEKLGEEVRDM-----KERLLLEE----KQRKQMESELSKLKKNLRESE---NVVEEKRYMKEDLSKG 768
Cdd:pfam15921 787 KMAGELEVLRSQERRLKEKVANMevaldKASLQFAEcqdiIQRQEQESVRLKLQHTLDVKElqgPGYTSNSSMKPRLLQP 866
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 769 SAESGAQTGSQRSQGLKKSLSGQRATMARLCEEvgiqkilqliKSEDLEVQIQAVKVVANlaAEEANQVKIVEEGGVEAL 848
Cdd:pfam15921 867 ASFTRTHSNVPSSQSTASFLSHHSRKTNALKED----------PTRDLKQLLQELRSVIN--EEPTVQLSKAEDKGRAPS 934
|
490
....*....|....
gi 1063716835 849 LMLVQSSQNSTILR 862
Cdd:pfam15921 935 LGALDDRVRDCIIE 948
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
485-745 |
7.28e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.26 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 485 LEKRLRECENSFAE--AEKNAVTRSKFLEKENTR-----LELSMKELLKDLQLQKDQCDLMHDKAIQLEMKLKNTKQQQL 557
Cdd:pfam07888 32 LQNRLEECLQERAEllQAQEAANRQREKEKERYKrdreqWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 558 ENSAYEAKLADTSQVYEKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIHEQEKGNYQYQRELAET-------- 629
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTeeelrsls 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 630 ----------------THTYESKIAELQKKLEGENARSNAAEDQLRQMkRLISDRQVISQENEEAneLKIKLEELSQMYE 693
Cdd:pfam07888 192 kefqelrnslaqrdtqVLQLQDTITTLTQKLTTAHRKEAENEALLEEL-RSLQERLNASERKVEG--LGEELSSMAAQRD 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 694 STVDELQTVKLDYDDL------------------------LQQK--------EKLGEEVRDMKERLLLEEKQRKQMESEL 741
Cdd:pfam07888 269 RTQAELHQARLQAAQLtlqladaslalregrarwaqeretLQQSaeadkdriEKLSAELQRLEERLQEERMEREKLEVEL 348
|
....
gi 1063716835 742 SKLK 745
Cdd:pfam07888 349 GREK 352
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
634-768 |
8.07e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 634 ESKIAELQKKLEGENARSNAAEDQlrqmkrlisdrqVISQENEEANELKIKLEELsqmyESTVDELQTvklDYDDLLQQK 713
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEER------------ELTEEEEEIRRLEEQVERL----EAEVEELEA---ELEEKDERI 443
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063716835 714 EKLGEEVRDMKERL---LLEEKQRKQMESELSKLKKNLRESENVVEE--------KRYMKEDLSKG 768
Cdd:COG2433 444 ERLERELSEARSEErreIRKDREISRLDREIERLERELEEERERIEElkrklerlKELWKLEHSGE 509
|
|
| SRP1 |
COG5064 |
Karyopherin (importin) alpha [Intracellular trafficking and secretion]; |
718-914 |
9.82e-03 |
|
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
Pssm-ID: 227396 [Multi-domain] Cd Length: 526 Bit Score: 39.87 E-value: 9.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 718 EEVRDMKERLLLEEKQRKQMESeLSKlKKNLRESENVVEEKRY-MKEDLSKgsaESGAQTGSQRSQGLKKSLSGQRATMA 796
Cdd:COG5064 23 DELRRRREEQQVELRKQKREEL-LNK-RRNLADVSEEAESSFIpMEQQFYS---ELPQLTQQLFSDDIEQQLQAVYKFRK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 797 RLCEEVG--IQKILQ----------LIKSEDLEVQIQAVKVVANLAAEEANQVKIVEEGGVEALLMLVQSSQNSTILRVA 864
Cdd:COG5064 98 LLSKETSppIQPVIDagvvprfvefMDEIQRDMLQFEAAWALTNIASGTTQQTKVVVDAGAVPLFIQLLSSTEDDVREQA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063716835 865 SGAIANLAMN-EKSQDLIMNKGGAQ-LLAKMVTKTDDPQTLRMVAGALANLC 914
Cdd:COG5064 178 VWALGNIAGDsEGCRDYVLQCGALEpLLGLLLSSAIHISMLRNATWTLSNLC 229
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
444-741 |
9.92e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.95 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 444 MVKLKEEFDYESLCRKLETQVDHLTAEVERQNKLRNSE-KHELEKRLRECENSFAEAEKNAVTRSKFLEKENTRLELSMK 522
Cdd:TIGR00618 205 LLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHaYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 523 ELlkDLQLQKDQCDLMHDKAIQLEmklkntKQQQLENSAYEAKLADTSQVYEKKIAELVQRVEDEQARST----NAEHQL 598
Cdd:TIGR00618 285 RI--NRARKAAPLAAHIKAVTQIE------QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLlqtlHSQEIH 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 599 TEMKNILSKQQKSIHEQEKGNYQYQRELAETTHTYESKIAELQKKLEGENARSNAAEDQLR------------------Q 660
Cdd:TIGR00618 357 IRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSafrdlqgqlahakkqqelQ 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063716835 661 MKRLISDRQVISQENEEANELKIKLEELSQMYESTVDELQTVKldydDLLQQKEKLGEEVRDMKERLLLEEKQRKQMESE 740
Cdd:TIGR00618 437 QRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE----QIHLQETRKKAVVLARLLELQEEPCPLCGSCIH 512
|
.
gi 1063716835 741 L 741
Cdd:TIGR00618 513 P 513
|
|
| |
