|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
58-475 |
1.73e-159 |
|
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: 490.37 E-value: 1.73e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 58 YLQVCLRIRPFTQSEKEHEAEGCVQVLDSQSVLLKDPQSILGHLSEKSSGQVAQKFSFSKVFGPETSQKEFFLGCIMQPV 137
Cdd:cd01368 2 PVKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHPPKGSAANKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTALPLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 138 KDLLEGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmsfkphrcreylklssdqekeesankn 217
Cdd:cd01368 82 QDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG-------------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 218 tllrqikevtihndsydvlcghltnsltipefeesvnscdqsslnvdnikYSVWVSFFEIYNESIYDLFVPV-SSKFQKR 296
Cdd:cd01368 130 --------------------------------------------------YSVFVSYIEIYNEYIYDLLEPSpSSPTKKR 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 297 KMLRLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEI------PRVT 370
Cdd:cd01368 160 QSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDgdvdqdKDQI 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 371 RVSELSLCDLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLKNSEKSK-VQHVPFRESKLTHYFQSFFTGKGKIC 449
Cdd:cd01368 240 TVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGtNKMVPFRDSKLTHLFQNYFDGEGKAS 319
|
410 420
....*....|....*....|....*.
gi 569007259 450 MIINISQSCSAYDETLNVLKFSTTAQ 475
Cdd:cd01368 320 MIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
64-477 |
7.53e-94 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 307.19 E-value: 7.53e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 64 RIRPFTQSEKEHEAEGCVQVLDsqsvllkdPQSILGHLSEKSSGQVAQKFSFSKVFGPETSQKEFFLGCIMQPVKDLLEG 143
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVES--------VDSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 144 HSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERLytkmsfkphrcreylklssdqekeesankntllrqi 223
Cdd:pfam00225 73 YNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK------------------------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 224 kevtihndsydvlcghltnsltipefeesvnscdqsslnvDNIKYSVWVSFFEIYNESIYDLFVPVSSKFQKrkmLRLSQ 303
Cdd:pfam00225 117 ----------------------------------------ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRK---LRIRE 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 304 DIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQ-IEDSEIPRVTRVSELSLCDLAG 382
Cdd:pfam00225 154 DPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQrNRSTGGEESVKTGKLNLVDLAG 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 383 SERSMKTQN-EGERLREAGNINTSLLTLGKCINVLknSEKSKvQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAY 461
Cdd:pfam00225 234 SERASKTGAaGGQRLKEAANINKSLSALGNVISAL--ADKKS-KHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNY 310
|
410
....*....|....*.
gi 569007259 462 DETLNVLKFSTTAQRV 477
Cdd:pfam00225 311 EETLSTLRFASRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
60-475 |
5.71e-92 |
|
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: 302.18 E-value: 5.71e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 60 QVCLRIRPFTQSEKEHEAEGCVQVLDSQSVllkdpQSILGHLSEKssgQVAQKFSFSKVFGPETSQKEFFLGCIMQPVKD 139
Cdd:smart00129 3 RVVVRVRPLNKREKSRKSPSVVPFPDKVGK-----TLTVRSPKNR---QGEKKFTFDKVFDATASQEDVFEETAAPLVDS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 140 LLEGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERlytkmsfkphrcreylklssdqekeesankntl 219
Cdd:smart00129 75 VLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKR--------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 220 lrqikevtihndsydvlcghltnsltipefeesvnscdqsslnVDNIKYSVWVSFFEIYNESIYDLFVPVSSKfqkrkmL 299
Cdd:smart00129 122 -------------------------------------------EEGWQFSVKVSYLEIYNEKIRDLLNPSSKK------L 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 300 RLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRVTRVSELSLCD 379
Cdd:smart00129 153 EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKASKLNLVD 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 380 LAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLknSEKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCS 459
Cdd:smart00129 233 LAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINAL--AQHSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSS 310
|
410
....*....|....*.
gi 569007259 460 AYDETLNVLKFSTTAQ 475
Cdd:smart00129 311 NLEETLSTLRFASRAK 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
60-475 |
1.10e-87 |
|
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: 289.54 E-value: 1.10e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 60 QVCLRIRPFTQSEKEhEAEGCVQVLDSQSVLLKDPqsilghlseKSSGQVAQKFSFSKVFGPETSQKEFFLGCIMQPVKD 139
Cdd:cd00106 3 RVAVRVRPLNGREAR-SAKSVISVDGGKSVVLDPP---------KNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 140 LLEGHSRLIFTYGLTNSGKTYTFQGT-EENIGILPRTLNVLFDSLQERLYTKMSfkphrcreylklssdqekeesanknt 218
Cdd:cd00106 73 ALEGYNGTIFAYGQTGSGKTYTMLGPdPEQRGIIPRALEDIFERIDKRKETKSS-------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 219 llrqikevtihndsydvlcghltnsltipefeesvnscdqsslnvdnikYSVWVSFFEIYNESIYDLFVPVsskfqKRKM 298
Cdd:cd00106 127 -------------------------------------------------FSVSASYLEIYNEKIYDLLSPV-----PKKP 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 299 LRLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRVTRVSELSLC 378
Cdd:cd00106 153 LSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGESVTSSKLNLV 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 379 DLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLknSEKSKVqHVPFRESKLTHYFQSFFTGKGKICMIINISQSC 458
Cdd:cd00106 233 DLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISAL--ADGQNK-HIPYRDSKLTRLLQDSLGGNSKTIMIACISPSS 309
|
410
....*....|....*..
gi 569007259 459 SAYDETLNVLKFSTTAQ 475
Cdd:cd00106 310 ENFEETLSTLRFASRAK 326
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
64-477 |
9.10e-68 |
|
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: 232.10 E-value: 9.10e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 64 RIRPFTQSEKEHEAeGCVQVLDSqsvllkDPQSIlgHLSEKSSGQvaQKFSFSKVFGPETSQKEFFlGCIMQPVKDLLEG 143
Cdd:cd01366 9 RVRPLLPSEENEDT-SHITFPDE------DGQTI--ELTSIGAKQ--KEFSFDKVFDPEASQEDVF-EEVSPLVQSALDG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 144 HSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERlytkmsfkphrcreylklssdqekeesankntllrqi 223
Cdd:cd01366 77 YNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKEL------------------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 224 KEVTIhndsydvlcghltnsltipefeesvnscdqsslnvdniKYSVWVSFFEIYNESIYDLfvpVSSKFQKRKMLRLSQ 303
Cdd:cd01366 120 KEKGW--------------------------------------SYTIKASMLEIYNETIRDL---LAPGNAPQKKLEIRH 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 304 D-IKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRIlQIEDSEIPRVTRvSELSLCDLAG 382
Cdd:cd01366 159 DsEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI-SGRNLQTGEISV-GKLNLVDLAG 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 383 SERSMKTQNEGERLREAGNINTSLLTLGKCINVLKNseksKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYD 462
Cdd:cd01366 237 SERLNKSGATGDRLKETQAINKSLSALGDVISALRQ----KQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLN 312
|
410
....*....|....*
gi 569007259 463 ETLNVLKFsttAQRV 477
Cdd:cd01366 313 ETLNSLRF---ASKV 324
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
59-474 |
6.32e-66 |
|
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: 227.61 E-value: 6.32e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 59 LQVCLRIRPFTQSEKEHEAEGCVQVLDSQSVLLKDPQSILGHLSEKSSGQVAQ-------KFSFSKVFGPETSQKEFFLG 131
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFDPKDEEDGFFHGGSNNRDRRkrrnkelKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 132 CIMQPVKDLLEGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmsfkphrcreylkLSSDQEke 211
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIES------------------LKDEKE-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 212 esankntllrqikevtihndsydvlcghltnsltipefeesvnscdqsslnvdnikYSVWVSFFEIYNESIYDLFVPVSs 291
Cdd:cd01370 142 --------------------------------------------------------FEVSMSYLEIYNETIRDLLNPSS- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 292 kfqkrKMLRLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIE-DSEIPRVT 370
Cdd:cd01370 165 -----GPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDkTASINQQV 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 371 RVSELSLCDLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLKNSeKSKVQHVPFRESKLTHYFQSFFTGKGKICM 450
Cdd:cd01370 240 RQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADP-GKKNKHIPYRDSKLTRLLKDSLGGNCRTVM 318
|
410 420
....*....|....*....|....
gi 569007259 451 IINISQSCSAYDETLNVLKFSTTA 474
Cdd:cd01370 319 IANISPSSSSYEETHNTLKYANRA 342
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
60-476 |
5.38e-64 |
|
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: 221.82 E-value: 5.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 60 QVCLRIRPFTQSEKEHEAEGCVQVLDSQsvllkdPQSILGHlsekssgqvAQKFSFSKVFGPETSQKEFFLGCIMQPVKD 139
Cdd:cd01372 4 RVAVRVRPLLPKEIIEGCRICVSFVPGE------PQVTVGT---------DKSFTFDYVFDPSTEQEEVYNTCVAPLVDG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 140 LLEGHSRLIFTYGLTNSGKTYTFQGT------EENIGILPRTLNVLFDSLQERlytkmsfkphrcreylklssdqekees 213
Cdd:cd01372 69 LFEGYNATVLAYGQTGSGKTYTMGTAytaeedEEQVGIIPRAIQHIFKKIEKK--------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 214 ankntllrqikevtihndsydvlcghltnsltipefeesvnscdqsslnVDNIKYSVWVSFFEIYNESIYDLFvpvSSKF 293
Cdd:cd01372 122 -------------------------------------------------KDTFEFQLKVSFLEIYNEEIRDLL---DPET 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 294 QKRKMLRLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQ-IEDSEIPR---- 368
Cdd:cd01372 150 DKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQtKKNGPIAPmsad 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 369 ---VTRVSELSLCDLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLkNSEKSKVQHVPFRESKLTHYFQSFFTGK 445
Cdd:cd01372 230 dknSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISAL-GDESKKGAHVPYRDSKLTRLLQDSLGGN 308
|
410 420 430
....*....|....*....|....*....|.
gi 569007259 446 GKICMIINISQSCSAYDETLNVLKFsttAQR 476
Cdd:cd01372 309 SHTLMIACVSPADSNFEETLNTLKY---ANR 336
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
60-477 |
1.68e-62 |
|
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: 216.82 E-value: 1.68e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 60 QVCLRIRPFTQSEKEHEaEGCVQVLDSQSVLLKDPQSilghlsekssgqvaQKFSFSKVFGPETSQKEFFLGCIMQPVKD 139
Cdd:cd01374 3 TVTVRVRPLNSREIGIN-EQVAWEIDNDTIYLVEPPS--------------TSFTFDHVFGGDSTNREVYELIAKPVVKS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 140 LLEGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmsfkphrcreylklssdqekeeSANKNTL 219
Cdd:cd01374 68 ALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD---------------------------TPDREFL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 220 LRqikevtihndsydvlcghltnsltipefeesvnscdqsslnvdnikysvwVSFFEIYNESIYDLFVPVSskfqkrKML 299
Cdd:cd01374 121 LR--------------------------------------------------VSYLEIYNEKINDLLSPTS------QNL 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 300 RLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRVT-RVSELSLC 378
Cdd:cd01374 145 KIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGTvRVSTLNLI 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 379 DLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLknSEKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSC 458
Cdd:cd01374 225 DLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKL--SEGKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAE 302
|
410
....*....|....*....
gi 569007259 459 SAYDETLNVLKFSTTAQRV 477
Cdd:cd01374 303 SHVEETLNTLKFASRAKKI 321
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
59-474 |
2.20e-61 |
|
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: 214.88 E-value: 2.20e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 59 LQVCLRIRPFTQSEKEHEAEGCVQVLDSQSVLLKDPQSILGHLSEKssgqvaqKFSFSKVFGPETSQKEFFLGCIMQPVK 138
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVRTGGLADKSSTK-------TYTFDMVFGPEAKQIDVYRSVVCPILD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 139 DLLEGHSRLIFTYGLTNSGKTYTFQGTE-----------ENIGILPRTLNVLFDSLqerlytkmsfkphrcreylklsSD 207
Cdd:cd01364 77 EVLMGYNCTIFAYGQTGTGKTYTMEGDRspneeytweldPLAGIIPRTLHQLFEKL----------------------ED 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 208 QEKEesankntllrqikevtihndsydvlcghltnsltipefeesvnscdqsslnvdnikYSVWVSFFEIYNESIYDLFV 287
Cdd:cd01364 135 NGTE--------------------------------------------------------YSVKVSYLEIYNEELFDLLS 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 288 PvSSKFQKRkmLRLSQDI--KGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIE-DS 364
Cdd:cd01364 159 P-SSDVSER--LRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKEtTI 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 365 EIPRVTRVSELSLCDLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLknSEKSKvqHVPFRESKLTHYFQSFFTG 444
Cdd:cd01364 236 DGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITAL--VERAP--HVPYRESKLTRLLQDSLGG 311
|
410 420 430
....*....|....*....|....*....|
gi 569007259 445 KGKICMIINISQSCSAYDETLNVLKFSTTA 474
Cdd:cd01364 312 RTKTSIIATISPASVNLEETLSTLEYAHRA 341
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
60-477 |
1.15e-59 |
|
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: 209.90 E-value: 1.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 60 QVCLRIRPFTQSEKEHEAEGCVQVLDSQSVLLKDPQSilgHLSEKSSGQVAQKFSFSKVF---GPE----TSQKEFFLGC 132
Cdd:cd01365 4 KVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQA---DKNNKATREVPKSFSFDYSYwshDSEdpnyASQEQVYEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 133 IMQPVKDLLEGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTlnvlfdslqerlytkmsfkphrCREylklssdqekee 212
Cdd:cd01365 81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRL----------------------CED------------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 213 sankntLLRQIkevtihndsydvlcghltnsltipefeESVNScdqsslnvDNIKYSVWVSFFEIYNESIYDLFVPvsSK 292
Cdd:cd01365 127 ------LFSRI---------------------------ADTTN--------QNMSYSVEVSYMEIYNEKVRDLLNP--KP 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 293 FQKRKMLRLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQI--EDSEIPRVT 370
Cdd:cd01365 164 KKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKrhDAETNLTTE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 371 RVSELSLCDLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVL----KNSEKSKVQHVPFRESKLTHYFQSFFTGKG 446
Cdd:cd01365 244 KVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALadmsSGKSKKKSSFIPYRDSVLTWLLKENLGGNS 323
|
410 420 430
....*....|....*....|....*....|.
gi 569007259 447 KICMIINISQSCSAYDETLNVLKFSTTAQRV 477
Cdd:cd01365 324 KTAMIAAISPADINYEETLSTLRYADRAKKI 354
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
59-477 |
1.67e-57 |
|
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: 202.56 E-value: 1.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 59 LQVCLRIRPFTQSEKEHEAEGCVQVLDSQSVLLKDpqsilghlSEKSSgqvaqKFSFSKVFGPETSQKEFFLGCIMQPVK 138
Cdd:cd01369 4 IKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIAT--------SETGK-----TFSFDRVFDPNTTQEDVYNFAAKPIVD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 139 DLLEGHSRLIFTYGLTNSGKTYTFQGT---EENIGILPRTLNVLFDSLqerlytkmsfkphrcreylklssdqekeesan 215
Cdd:cd01369 71 DVLNGYNGTIFAYGQTSSGKTYTMEGKlgdPESMGIIPRIVQDIFETI-------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 216 kntllrqikevtihndsydvlcghltnsltipefeesvnscdqsSLNVDNIKYSVWVSFFEIYNESIYDLFVPvsskfqK 295
Cdd:cd01369 119 --------------------------------------------YSMDENLEFHVKVSYFEIYMEKIRDLLDV------S 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 296 RKMLRLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQ--IEDSEIprvtRVS 373
Cdd:cd01369 149 KTNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQenVETEKK----KSG 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 374 ELSLCDLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLKNSEKSkvqHVPFRESKLTHYFQSFFTGKGKICMIIN 453
Cdd:cd01369 225 KLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKKT---HIPYRDSKLTRILQDSLGGNSRTTLIIC 301
|
410 420
....*....|....*....|....
gi 569007259 454 ISQSCSAYDETLNVLKFSTTAQRV 477
Cdd:cd01369 302 CSPSSYNESETLSTLRFGQRAKTI 325
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
59-477 |
7.20e-56 |
|
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: 198.07 E-value: 7.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 59 LQVCLRIRPFTQSEKeheAEGCVQVLD----SQSVLLKDPQSilghlsekSSGQVAQKFSFSKVFGPETSQKEFFLGCIM 134
Cdd:cd01371 3 VKVVVRCRPLNGKEK---AAGALQIVDvdekRGQVSVRNPKA--------TANEPPKTFTFDAVFDPNSKQLDVYDETAR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 135 QPVKDLLEGHSRLIFTYGLTNSGKTYTFQGT---EENIGILPRTLNVLFDSLqerlytkmsfkphrcreylklssdqeKE 211
Cdd:cd01371 72 PLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKredPELRGIIPNSFAHIFGHI--------------------------AR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 212 ESANKNTLLRqikevtihndsydvlcghltnsltipefeesvnscdqsslnvdnikysvwVSFFEIYNESIYDLFvpvsS 291
Cdd:cd01371 126 SQNNQQFLVR--------------------------------------------------VSYLEIYNEEIRDLL----G 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 292 KFQKRKM-LRLSQDIKGYsfIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRI---LQIEDSEip 367
Cdd:cd01371 152 KDQTKRLeLKERPDTGVY--VKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIecsEKGEDGE-- 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 368 RVTRVSELSLCDLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLKNsekSKVQHVPFRESKLTHYFQSFFTGKGK 447
Cdd:cd01371 228 NHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD---GKSTHIPYRDSKLTRLLQDSLGGNSK 304
|
410 420 430
....*....|....*....|....*....|
gi 569007259 448 ICMIINISQSCSAYDETLNVLKFSTTAQRV 477
Cdd:cd01371 305 TVMCANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
59-470 |
7.59e-53 |
|
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: 188.87 E-value: 7.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 59 LQVCLRIRPFTQSEKEHEAEGCVQVLDSQSVLLKDPQSilghlsekssGQVAQKFSFSKVFGPETSQKEFFLGCIMQPVK 138
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVELADPRN----------HGETLKYQFDAFYGEESTQEDIYAREVQPIVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 139 DLLEGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLnvlfdslqerlytkmsfkphrcREYLKLSSDQEKEESANknt 218
Cdd:cd01376 72 HLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTV----------------------MDLLQMTRKEAWALSFT--- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 219 llrqikevtihndsydvlcghltnsltipefeesvnscdqsslnvdnikysvwVSFFEIYNESIYDLFVPvsskfqKRKM 298
Cdd:cd01376 127 -----------------------------------------------------MSYLEIYQEKILDLLEP------ASKE 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 299 LRLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEdSEIPRVTRVSELSLC 378
Cdd:cd01376 148 LVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRE-RLAPFRQRTGKLNLI 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 379 DLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLKNSEKskvqHVPFRESKLTHYFQSFFTGKGKICMIINISQSC 458
Cdd:cd01376 227 DLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLP----RIPYRDSKLTRLLQDSLGGGSRCIMVANIAPER 302
|
410
....*....|..
gi 569007259 459 SAYDETLNVLKF 470
Cdd:cd01376 303 TFYQDTLSTLNF 314
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
59-477 |
3.31e-52 |
|
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: 188.10 E-value: 3.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 59 LQVCLRIRPFTQSEKEHEAEGCVQVLDSQS-VLLKDPQsilghlsekssgqvaQKFSFSKVFGPETSQKEFFLGCIMQPV 137
Cdd:cd01373 3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTlVLHSKPP---------------KTFTFDHVADSNTNQESVFQSVGKPIV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 138 KDLLEGHSRLIFTYGLTNSGKTYTFQGTEENI--------GILPRTLNVLFDSLQerlytkmsfkphrcreylklssdQE 209
Cdd:cd01373 68 ESCLSGYNGTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQ-----------------------RE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 210 KEESAnkntllrqikevtihndsydvlcghltnsltipefeesvnscdqsslnvDNIKYSVWVSFFEIYNESIYDLFVPV 289
Cdd:cd01373 125 KEKAG-------------------------------------------------EGKSFLCKCSFLEIYNEQIYDLLDPA 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 290 SSKfqkrkmLRLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRV 369
Cdd:cd01373 156 SRN------LKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKACFVN 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 370 TRVSELSLCDLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLKNSEKSKVQHVPFRESKLTHYFQSFFTGKGKIC 449
Cdd:cd01373 230 IRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGKQRHVCYRDSKLTFLLRDSLGGNAKTA 309
|
410 420
....*....|....*....|....*...
gi 569007259 450 MIINISQSCSAYDETLNVLKFsttAQRV 477
Cdd:cd01373 310 IIANVHPSSKCFGETLSTLRF---AQRA 334
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
105-643 |
5.51e-47 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 178.78 E-value: 5.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 105 SSGQVAQKFSFSKVFGPETSQKEFFLGCIMQPVKDLLEGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLq 184
Cdd:COG5059 50 LEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKL- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 185 erlytkmsfkphrcreylklssdqekeesankntllrqikevtihndsydvlcghltnsltipefeesvnscdqsSLNVD 264
Cdd:COG5059 129 ---------------------------------------------------------------------------EDLSM 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 265 NIKYSVWVSFFEIYNESIYDLFVPvsSKFQKRKMLRLSQDIKgysfIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLN 344
Cdd:COG5059 134 TKDFAVSISYLEIYNEKIYDLLSP--NEESLNIREDSLLGVK----VAGLTEKHVSSKEEILDLLRKGEKNRTTASTEIN 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 345 NASSRSHSIFTIRILQIEDSEIPRVTrvSELSLCDLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLknSEKSKV 424
Cdd:COG5059 208 DESSRSHSIFQIELASKNKVSGTSET--SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINAL--GDKKKS 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 425 QHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNVLKFSTTAQR----VYVPDTLSSSQ---EKSFASNKSL 497
Cdd:COG5059 284 GHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSiknkIQVNSSSDSSReieEIKFDLSEDR 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 498 QDVSLDSNLDNKILNVKRKTVSWENSLEDVLENEDL--VEDLEENEETQNMETELTDEdsdKSLEECRVSTCHK----KN 571
Cdd:COG5059 364 SEIEILVFREQSQLSQSSLSGIFAYMQSLKKETETLksRIDLIMKSIISGTFERKKLL---KEEGWKYKSTLQFlrieID 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569007259 572 KELLDLIEKLNKRLINENK-EKLTLELKIREEV---TQEFTQYWSQREaDFKETLLHereILEENAERRLAIFKDL 643
Cdd:COG5059 441 RLLLLREEELSKKKTKIHKlNKLRHDLSSLLSSipeETSDRVESEKAS-KLRSSAST---KLNLRSSRSHSKFRDH 512
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
61-471 |
1.85e-44 |
|
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: 164.78 E-value: 1.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 61 VCLRIRPFTQSEkeheaegcVQVLDSQSVLLKDPQSILGHLSEK----SSGQVAQKFSFSKVFGPETSQKEFFLGCIMQP 136
Cdd:cd01367 4 VCVRKRPLNKKE--------VAKKEIDVVSVPSKLTLIVHEPKLkvdlTKYIENHTFRFDYVFDESSSNETVYRSTVKPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 137 VKDLLEGHSRLIFTYGLTNSGKTYT----FQGTEENIGIlprtlnvlfdslqerlytkmsfkphrcreYLKLSSDqekee 212
Cdd:cd01367 76 VPHIFEGGKATCFAYGQTGSGKTYTmggdFSGQEESKGI-----------------------------YALAARD----- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 213 sankntLLRQIKEVTIHNDsydvlcghltnsltipefeesvnscdqsslnvdnikYSVWVSFFEIYNESIYDLfvpvssk 292
Cdd:cd01367 122 ------VFRLLNKLPYKDN------------------------------------LGVTVSFFEIYGGKVFDL------- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 293 FQKRKMLRLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIrilQIEDSEIPRVtrV 372
Cdd:cd01367 153 LNRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQI---ILRDRGTNKL--H 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 373 SELSLCDLAGSER-SMKTQNEGERLREAGNINTSLLTLGKCINVLKNSEKskvqHVPFRESKLTHYFQ-SFFTGKGKICM 450
Cdd:cd01367 228 GKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNKA----HIPFRGSKLTQVLKdSFIGENSKTCM 303
|
410 420
....*....|....*....|.
gi 569007259 451 IINISQSCSAYDETLNVLKFS 471
Cdd:cd01367 304 IATISPGASSCEHTLNTLRYA 324
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
108-477 |
1.01e-41 |
|
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: 156.97 E-value: 1.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 108 QVAQKFSFSKVFgpETSQKEFFLGCIMQPVKD-LLEGHSRLIFTYGLTNSGKTYTFQGTEENI---GILPRTLNVLFDSL 183
Cdd:cd01375 45 QEDWSFKFDGVL--HNASQELVYETVAKDVVSsALAGYNGTIFAYGQTGAGKTFTMTGGTENYkhrGIIPRALQQVFRMI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 184 QERlYTKMsfkphrcreylklssdqekeesankntllrqikevtihndsydvlcghltnsltipefeesvnscdqsslnv 263
Cdd:cd01375 123 EER-PTKA------------------------------------------------------------------------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 264 dnikYSVWVSFFEIYNESIYDLFVPVSSKFQKRKMLRLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKL 343
Cdd:cd01375 130 ----YTVHVSYLEIYNEQLYDLLSTLPYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTM 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 344 NNASSRSHSIFTIRiLQIEDSEIPRVT-RVSELSLCDLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLknSEKS 422
Cdd:cd01375 206 NKNSSRSHCIFTIH-LEAHSRTLSSEKyITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIAL--SDKD 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 569007259 423 KvQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNVLKFsttAQRV 477
Cdd:cd01375 283 R-THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRF---ASRV 333
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
81-477 |
9.81e-32 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 136.22 E-value: 9.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 81 VQVLDSQSVLLKDPQS--ILGHLSEKSSGQVAQKFSFSKVFGPETSQKEFFLGCIMQPVKDLLEGHSRLIFTYGLTNSGK 158
Cdd:PLN03188 100 VKVIVRMKPLNKGEEGemIVQKMSNDSLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 159 TYTFQG-----TEENI-----GILPRTLNVLFDSLQERlytkmsfkphrcreylklssdqekeesankntllrQIKevti 228
Cdd:PLN03188 180 TYTMWGpanglLEEHLsgdqqGLTPRVFERLFARINEE-----------------------------------QIK---- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 229 HNDSydvlcghltnsltipefeesvnscdqsslnvdNIKYSVWVSFFEIYNESIYDLFVPVsskfQKRKMLRlsQDIKGY 308
Cdd:PLN03188 221 HADR--------------------------------QLKYQCRCSFLEIYNEQITDLLDPS----QKNLQIR--EDVKSG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 309 SFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIrilqIEDSEIPRVT------RVSELSLCDLAG 382
Cdd:PLN03188 263 VYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTC----VVESRCKSVAdglssfKTSRINLVDLAG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 383 SERSMKTQNEGERLREAGNINTSLLTLGKCINVLKN-SEKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAY 461
Cdd:PLN03188 339 SERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEiSQTGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCK 418
|
410
....*....|....*.
gi 569007259 462 DETLNVLKFSTTAQRV 477
Cdd:PLN03188 419 SETFSTLRFAQRAKAI 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
673-1459 |
1.93e-21 |
|
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: 102.06 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 673 VEDIFHSLQDDVTDIKKQAELA---------------HLYITSLVDPQEAIACLQLKFNQVKAELAETKEELIKAQEEL- 736
Cdd:TIGR02168 191 LEDILNELERQLKSLERQAEKAerykelkaelrelelALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLe 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 737 -KNRESNSLVQALKTSSKVDTSLTSNKSTCNETSEMPKNSRAQTHSERKRLNEDGLQLGEPPAKKGLIL--VSPPITEEQ 813
Cdd:TIGR02168 271 eLRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELaeLEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 814 NKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASY 893
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 894 -NSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQ-MQTKIDELRSLDSPSHISKIDLLNLQDLSSGAKg 971
Cdd:TIGR02168 431 eEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQaLDAAERELAQLQARLDSLERLQENLEGFSEGVK- 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 972 dNCLNTSQQLPgGDFSSTWvkeyhtQEISRENSFHASIE-AIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKgyreE 1050
Cdd:TIGR02168 510 -ALLKNQSGLS-GILGVLS------ELISVDEGYEAAIEaALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFL----P 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1051 NSDLRAQESQGKNRdhQLKEKESLIQQLREELQEKSVSLRV-------QVQLVAEREQALSELSQDVTCYKAKIKDLEVI 1123
Cdd:TIGR02168 578 LDSIKGTEIQGNDR--EILKNIEGFLGVAKDLVKFDPKLRKalsyllgGVLVVDDLDNALELAKKLRPGYRIVTLDGDLV 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1124 ----VETQKDEckrlvELEQSILEKESAILKLEANLKECEAK-HQDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQS 1198
Cdd:TIGR02168 656 rpggVITGGSA-----KTNSSILERRREIEELEEKIEELEEKiAELEKALAELRKELEELEEELEQLRKELEELSRQISA 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1199 KEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVM--------------RD 1264
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLkeelkalrealdelRA 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1265 EEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQK---------MEEAVQQYEKVCKDLSVKEKLVEDMRLTLV 1335
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSedieslaaeIEELEELIEELESELEALLNERASLEEALA 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1336 EQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSnQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKK 1415
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL-EGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEE 969
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 569007259 1416 WLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVETLT 1459
Cdd:TIGR02168 970 ARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLT 1013
|
|
| RBD_KIF20B |
cd21786 |
RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B ... |
598-652 |
2.49e-19 |
|
RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B (also called cancer/testis antigen 90 (CT90), kinesin family member 20B, kinesin-related motor interacting with PIN1, or M-phase phosphoprotein 1 (MPP1)) is a plus-end-directed motor enzyme that is required for completion of cytokinesis. It is required for proper midbody organization and abscission in polarized cortical stem cells. KIF20B plays a role in the regulation of neuronal polarization by mediating the transport of specific cargos. It participates in the mobilization of SHTN1 (shootin 1) and in the accumulation of PIP3 in the growth cone of primary hippocampal neurons in a tubulin and actin-dependent manner. In the developing telencephalon, KIF20B cooperates with SHTN1 to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. KIF20B acts as an oncogene for promoting bladder cancer cell proliferation, apoptosis inhibition, and carcinogenic progression. This model corresponds to a conserved region in KIF20B that shows some sequence similarity to the RAB6 binding domain (RBD) of KIF20A. KIF20A-RBD is a dimer composed of two parallel alpha helices that form a right-handed coiled-coil additionally stabilized by an inter-helical cysteine bridge.
Pssm-ID: 409644 [Multi-domain] Cd Length: 56 Bit Score: 82.91 E-value: 2.49e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 569007259 598 KIREEVTQEFTQYWSQREADFKETLLHEREILEENAERRLAIFKDLVGKCDSQDE 652
Cdd:cd21786 1 KIREEVTQEFTELFSEMEKDYSERLEREREILEERAEKRLEIFKNLVNKTAKEEE 55
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
527-1331 |
1.80e-16 |
|
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: 85.88 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 527 VLENEDLVEDLEENEETQN-METELTDEDSDKSLEECRVSTCHKKNKELLDLIEKLNKRLINENKEKLTLELKIREEvtq 605
Cdd:TIGR02168 231 VLRLEELREELEELQEELKeAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL--- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 606 eftqywSQREADFKETLLHEREILEENAERRlaifkdlvgkcdsqdeptnricdIELETEEAHnyvgVEDIFHSLQDDVT 685
Cdd:TIGR02168 308 ------RERLANLERQLEELEAQLEELESKL-----------------------DELAEELAE----LEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 686 DIKKQAElahlyitslvdpqeaiaclqlKFNQVKAELaetkEELIKAQEELKNRESNSLVQALKTSSKVDTSLTSNKSTC 765
Cdd:TIGR02168 355 SLEAELE---------------------ELEAELEEL----ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 766 NETSEMPKNSRAQTHSERKRLNEDGLQlgeppakkglilvsppitEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLT 845
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEAELK------------------ELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 846 IGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRA--DVEQIQASYNSAVAEL-----QTQKAVNQEQRDRILKLS 918
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllKNQSGLSGILGVLSELisvdeGYEAAIEAALGGRLQAVV 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 919 QEMETAARSIESNVSQIKQMQTKIDELRSLdSPSHISKIDLLNLQDLSSGAK-GDNCLNTSQQLPG--GDFSST--WVKE 993
Cdd:TIGR02168 552 VENLNAAKKAIAFLKQNELGRVTFLPLDSI-KGTEIQGNDREILKNIEGFLGvAKDLVKFDPKLRKalSYLLGGvlVVDD 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 994 YHT-QEISRENSFHASI----EAIWEECKEIVKASSKKSHQIQG-------LEEQIEKLQVEVKGYREENSDLRAQESQG 1061
Cdd:TIGR02168 631 LDNaLELAKKLRPGYRIvtldGDLVRPGGVITGGSAKTNSSILErrreieeLEEKIEELEEKIAELEKALAELRKELEEL 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1062 KNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKR-LVELEQS 1140
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAeIEELEAQ 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1141 ILEKESAILKLEANLKECEAKHQdhirtnDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAN 1220
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELT------LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1221 SILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQ 1300
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
810 820 830
....*....|....*....|....*....|....
gi 569007259 1301 LSNQ---KMEEAVQQYEKVCKDLSVKEKLVEDMR 1331
Cdd:TIGR02168 945 LSEEyslTLEEAEALENKIEDDEEEARRRLKRLE 978
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
833-1479 |
2.34e-16 |
|
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: 85.49 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 833 LKEKNEELKRLLTIGE-----NELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVN 907
Cdd:TIGR02168 218 LKAELRELELALLVLRleelrEELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 908 QEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSldspshiskiDLLNLQDLSSGAKGdNCLNTSQQLpggdfs 987
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE----------ELAELEEKLEELKE-ELESLEAEL------ 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 988 stwvKEYHTQEISRENSFHASIEAIWEECKEIVKASSKK---SHQIQGLEEQIEKLQVEVKGYREENSDL--RAQESQGK 1062
Cdd:TIGR02168 361 ----EELEAELEELESRLEELEEQLETLRSKVAQLELQIaslNNEIERLEARLERLEDRRERLQQEIEELlkKLEEAELK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1063 NRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSiL 1142
Cdd:TIGR02168 437 ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN-Q 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1143 EKESAILKLEANLKECEAKHQ-----------------------------------------------DHIRTNDLSAKE 1175
Cdd:TIGR02168 516 SGLSGILGVLSELISVDEGYEaaieaalggrlqavvvenlnaakkaiaflkqnelgrvtflpldsikgTEIQGNDREILK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1176 ------------VKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKL------------------KEELAANSILtq 1225
Cdd:TIGR02168 596 niegflgvakdlVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYrivtldgdlvrpggvitgGSAKTNSSIL-- 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1226 NLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQK 1305
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1306 MEEAVQQYEKvckdlSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNTGTM 1385
Cdd:TIGR02168 754 KELTELEAEI-----EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1386 ---------DDLDVLTRKFSKLQ----------DELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRE 1446
Cdd:TIGR02168 829 lerriaateRRLEDLEEQIEELSedieslaaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
730 740 750
....*....|....*....|....*....|...
gi 569007259 1447 RCLKLQNEVETLTAQLAEKNSELQKWREERDQL 1479
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
833-1508 |
4.23e-16 |
|
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: 84.72 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 833 LKEKNEELKRL-LTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQR 911
Cdd:TIGR02168 215 YKELKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 912 DRILKLSQEMETAARSIESNVSQIKQMQTKIDELrslDSPSHISKIDLLNLQDLSSGAKGdNCLNTSQQLpggdfsstwv 991
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEEL---ESKLDELAEELAELEEKLEELKE-ELESLEAEL---------- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 992 KEYHTQEISRENSFHASIEAIWEECKEIVKASSKK---SHQIQGLEEQIEKLQVEVKGYREENSDL--RAQESQGKNRDH 1066
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIaslNNEIERLEARLERLEDRRERLQQEIEELlkKLEEAELKELQA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1067 QLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSiLEKES 1146
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN-QSGLS 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1147 AILKLEANLKECEAK-----------HQDHIRTNDLSA--KEVKFREE-----VTRLANNLHDTKQLLQSKEEENE---- 1204
Cdd:TIGR02168 520 GILGVLSELISVDEGyeaaieaalggRLQAVVVENLNAakKAIAFLKQnelgrVTFLPLDSIKGTEIQGNDREILKnieg 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1205 ----ISRQETEKLKEELAANSILTQNLKAD-LQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKL------LRIKI 1273
Cdd:TIGR02168 600 flgvAKDLVKFDPKLRKALSYLLGGVLVVDdLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTnssileRRREI 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1274 NELEKKKNQYSQDLDMKQRTIQQLKEQLSN---------QKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQ 1344
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEEleeeleqlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1345 DRVLEAKSEEADWLATELDKWKEKFKDLETRSNQrlntgTMDDLDVLTRKFSKLQDELQESEEKYKADRkkwlEEKAVLT 1424
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ-----LKEELKALREALDELRAELTLLNEEAANLR----ERLESLE 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1425 TQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLvtavETQMKALLSSCKHKDEEIQEL 1504
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL----EEALALLRSELEELSEELREL 906
|
....
gi 569007259 1505 RKAA 1508
Cdd:TIGR02168 907 ESKR 910
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1207-1479 |
2.49e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.83 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1207 RQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQrevsvmrDEEKLLRIKINELEKKKNQYSQD 1286
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-------AEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1287 LDMKQRTIQQLKEQLS--NQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQtqaeqdRVLEAKSEEADWLATELDK 1364
Cdd:COG1196 311 RRELEERLEELEEELAelEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE------ALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1365 WKEKFKDLETRSNQRlntgtmddldvltrkfsKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADD 1444
Cdd:COG1196 385 AEELLEALRAAAELA-----------------AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270
....*....|....*....|....*....|....*
gi 569007259 1445 RERCLKLQNEVETLTAQLAEKNSELQKWREERDQL 1479
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1006-1510 |
5.25e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.67 E-value: 5.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1006 HASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEK 1085
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1086 SVSLRVQVQLVAEREQALSELSQDVtcyKAKIKDLEVIVETQKDEckrLVELEQSILEKESAILKLEANLKECEAKHQDH 1165
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEEL---EEELEEAEEELEEAEAE---LAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1166 IRtndlsaKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKF 1245
Cdd:COG1196 392 LR------AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1246 IDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRtiQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEK 1325
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA--ALLLAGLRGLAGAVAVLIGVEAAYEAALEAA 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1326 LVEDMRLTLVEQEQTQAEQDRVLEAKSEEAdwlATELDKWKEKFKDLETRSNQRLntgtmddldVLTRKFSKLQDELQES 1405
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYLKAAKAGR---ATFLPLDKIRARAALAAALARG---------AIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1406 EEKYKAdrkkwLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLVTAVET 1485
Cdd:COG1196 612 DARYYV-----LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
490 500
....*....|....*....|....*
gi 569007259 1486 QMKALLSSCKHKDEEIQELRKAAAK 1510
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAE 711
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
996-1507 |
8.23e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.92 E-value: 8.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 996 TQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKG-------YREENSDLRAQ-ESQGKNRDHQ 1067
Cdd:PRK02224 219 DEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAEterereeLAEEVRDLRERlEELEEERDDL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1068 LKEKE------SLIQQLREELQEKSVSLRvqvQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKrlvELEQSI 1141
Cdd:PRK02224 299 LAEAGlddadaEAVEARREELEDRDEELR---DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAA---ELESEL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1142 LEKESAILKLEANLKECEakhqdhirtndlsakevkfrEEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAans 1221
Cdd:PRK02224 373 EEAREAVEDRREEIEELE--------------------EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA--- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1222 iltqNLKADLQKKEEDCAElKEKFIDAKK---------------QIEQVQREVSVMRDEEKLLRIKINELEKKKNQySQD 1286
Cdd:PRK02224 430 ----ELEATLRTARERVEE-AEALLEAGKcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLER-AED 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1287 LDMKQRTIQQLKEQLSNqkmeeavqqyekVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWK 1366
Cdd:PRK02224 504 LVEAEDRIERLEERRED------------LEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1367 EKFKDLETRSNQrlNTGTMDDLDvltrKFSKLQDELQESEEKYKADRKKwLEEKAVLTTQAKE---AENVRNREMRKYAD 1443
Cdd:PRK02224 572 EEVAELNSKLAE--LKERIESLE----RIRTLLAAIADAEDEIERLREK-REALAELNDERRErlaEKRERKRELEAEFD 644
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569007259 1444 DrERCLKLQNEVETLTAQLAEKNSELQKWREERDQL---VTAVETQMKALlssckhkdEEIQELRKA 1507
Cdd:PRK02224 645 E-ARIEEAREDKERAEEYLEQVEEKLDELREERDDLqaeIGAVENELEEL--------EELRERREA 702
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
569-1457 |
1.87e-12 |
|
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: 72.70 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 569 KKNKELLDLIEKLNKRLINENKEKLTLE-LKIREEVTQEFTQYWSQ-READFKETLLHEREILEENAERRLAIFKDLVgk 646
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELkLKEQAKKALEYYQLKEKlELEEEYLLYLDYLKLNEERIDLLQELLRDEQ-- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 647 cdSQDEPTNRICDIELETEEAHNYVGVEDIfhslqddvTDIKKQAELAHLYITSLVDPQEAIACLQLKFNQVKAELAETK 726
Cdd:pfam02463 251 --EEIESSKQEIEKEEEKLAQVLKENKEEE--------KEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 727 EELIKAQEELKNRESNSLVQALKTSSKVDTSLTsnkstcnETSEMPKNSRAQTHSERKRLNEDGLQLGEPPAKKGLilvs 806
Cdd:pfam02463 321 KEKKKAEKELKKEKEEIEELEKELKELEIKREA-------EEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA---- 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 807 ppITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADV 886
Cdd:pfam02463 390 --AKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 887 EQiqasynSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQDLS 966
Cdd:pfam02463 468 KK------SEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENY 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 967 SGAKGDNClntsqqlpgGDFSSTWVKEYHTQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKG 1046
Cdd:pfam02463 542 KVAISTAV---------IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKAT 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1047 YREENSDLRAQESQGKNRDHQL-KEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVE 1125
Cdd:pfam02463 613 LEADEDDKRAKVVEGILKDTELtKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1126 TQKDECKRLVELEQSI--LEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEEN 1203
Cdd:pfam02463 693 EILRRQLEIKKKEQREkeELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLK 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1204 EISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQY 1283
Cdd:pfam02463 773 EKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLA 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1284 SQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADwLATELD 1363
Cdd:pfam02463 853 EEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKE-EAEILL 931
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1364 KWKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYAD 1443
Cdd:pfam02463 932 KYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAI 1011
|
890
....*....|....
gi 569007259 1444 DRERCLKLQNEVET 1457
Cdd:pfam02463 1012 IEETCQRLKEFLEL 1025
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
778-1485 |
2.62e-12 |
|
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: 72.46 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 778 QTHSERKRLNEDGlQLGEppakKGLILVSPPITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEE 857
Cdd:pfam15921 86 QVKDLQRRLNESN-ELHE----KQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 858 KAELNKQVVSLQQQLRffeeknsslradveQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAA-RSIESNVSQI- 935
Cdd:pfam15921 161 KEDMLEDSNTQIEQLR--------------KMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHfRSLGSAISKIl 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 936 KQMQTKI-----------DELRSLDSPSHiSKIDLLNLQDLSsgakgdnclNTSQQLPGGDFSSTWVKEYHTQEISRENS 1004
Cdd:pfam15921 227 RELDTEIsylkgrifpveDQLEALKSESQ-NKIELLLQQHQD---------RIEQLISEHEVEITGLTEKASSARSQANS 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1005 FHASIEAIWEECKeivKASSKKSHQIQGLEEQIEKLQVEVKG----YREENSDLRAQ--------ESQGKNRDHQLKEKE 1072
Cdd:pfam15921 297 IQSQLEIIQEQAR---NQNSMYMRQLSDLESTVSQLRSELREakrmYEDKIEELEKQlvlanselTEARTERDQFSQESG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1073 SLIQQLREEL-----QEKSVSL-RVQVQLVAEREQA----LSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSIL 1142
Cdd:pfam15921 374 NLDDQLQKLLadlhkREKELSLeKEQNKRLWDRDTGnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAI 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1143 EKESAILKLEANLKECEAKHQDHIR--TNDLSAKEVKFrEEVTRLANNLHDTkqlLQSKEEENEISRQETEKLKEELAAN 1220
Cdd:pfam15921 454 QGKNESLEKVSSLTAQLESTKEMLRkvVEELTAKKMTL-ESSERTVSDLTAS---LQEKERAIEATNAEITKLRSRVDLK 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1221 SILTQNLKAD---LQKKEEDCAELKEKFIDAKKQIEqvqrevsvmrdeekLLRIKINELEKKKNQYSQDLDMKQRTIQQL 1297
Cdd:pfam15921 530 LQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIE--------------ILRQQIENMTQLVGQHGRTAGAMQVEKAQL 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1298 KEQLSNQKMEEAVQQYEKVCKDLSVK--EKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLEtr 1375
Cdd:pfam15921 596 EKEINDRRLELQEFKILKDKKDAKIRelEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLS-- 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1376 snqrlntgtmDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREM-------RKYADDRERC 1448
Cdd:pfam15921 674 ----------EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMkvamgmqKQITAKRGQI 743
|
730 740 750
....*....|....*....|....*....|....*..
gi 569007259 1449 LKLQNEVETLTAQLAEKNSELQKWREERDQLVTAVET 1485
Cdd:pfam15921 744 DALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELST 780
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
998-1354 |
4.20e-12 |
|
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: 71.64 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 998 EISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEvKGYREENSDLRA--QESQGKNRDHQLKEKESLI 1075
Cdd:TIGR02169 161 EIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQALLKekREYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1076 QQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVivetqkdecKRLVELEQSILEKESAILKLEANL 1155
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE---------EEQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1156 KECEAKHQDhirtndLSAKEVKFREEvtrlannLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKE 1235
Cdd:TIGR02169 311 AEKERELED------AEERLAKLEAE-------IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1236 EDCAELKEKFIDAKKQIEQVQREV-SVMRDEEKL-------------LRIKINELEKKKNQYSQDLDMKQRTIQQLKEQL 1301
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREInELKRELDRLqeelqrlseeladLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 569007259 1302 SN--QKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQE-QTQAEQDRVLEAKSEE 1354
Cdd:TIGR02169 458 EQlaADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEaQARASEERVRGGRAVE 513
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
809-1152 |
4.87e-12 |
|
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: 71.24 E-value: 4.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 809 ITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQ 888
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 889 IQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRsldspshiSKIDLLN--LQDLS 966
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR--------AELTLLNeeAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 967 SGAKGDNCLNTSQQLPGGDFSSTWVKEYHTQEISRE--NSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEV 1044
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1045 KGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEK-----SVSLRVQVQLVAEREQALSELSQDVTCYKAKIKD 1119
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlseeySLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
330 340 350
....*....|....*....|....*....|....*..
gi 569007259 1120 LEVI----VETQKDECKRLVELEQSILEKESAILKLE 1152
Cdd:TIGR02168 984 LGPVnlaaIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| RBD_KIF20A-like |
cd21744 |
RAB6 binding domain (RBD) found in kinesin-like proteins KIF20A, KIF20B, and similar proteins; ... |
598-652 |
6.03e-12 |
|
RAB6 binding domain (RBD) found in kinesin-like proteins KIF20A, KIF20B, and similar proteins; This family includes kinesin-like proteins KIF20A and KIF20B. KIF20A (also called GG10_2, mitotic kinesin-like protein 2 (MKlp2), Rab6-interacting kinesin-like protein, or rabkinesin-6) is a mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1 (polo-like kinase 1), it is involved in recruitment of PLK1 to the central spindle. KIF20A interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. It may act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. KIF20A has a microtubule plus-end-directed motility. KIF20B (also called cancer/testis antigen 90 (CT90), kinesin family member 20B, kinesin-related motor interacting with PIN1, or M-phase phosphoprotein 1 (MPP1)) is a plus-end-directed motor enzyme that is required for completion of cytokinesis. It is required for proper midbody organization and abscission in polarized cortical stem cells. KIF20B plays a role in the regulation of neuronal polarization by mediating the transport of specific cargoes. It participates in the mobilization of SHTN1 and in the accumulation of PIP3 in the growth cone of primary hippocampal neurons in a tubulin and actin-dependent manner. In the developing telencephalon, KIF20B cooperates with SHTN1 to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. This model corresponds to a conserved domain in the KIF20A subfamily, that shows RAB6 binding ability and has been called the RAB6 binding domain (RBD). KIF20A-RBD is a dimer composed of two parallel alpha helices that form a right-handed coiled-coil additionally stabilized by an inter-helical cysteine bridge.
Pssm-ID: 409643 [Multi-domain] Cd Length: 56 Bit Score: 62.09 E-value: 6.03e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 569007259 598 KIREEVTQEFTQYWSQREADFKETLLHEREILEENAERRLAIFKDLVGKCDSQDE 652
Cdd:cd21744 1 RIREEVSEEFEEQFALMEEDYEERLENEKEILEERYEKRLEIRKELIKKLSAALE 55
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
992-1510 |
8.21e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.48 E-value: 8.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 992 KEYHTQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEK 1071
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1072 ESLIQQLR---EELQEKSVSLRVQVQLVAE---REQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKE 1145
Cdd:PRK03918 258 EEKIRELEeriEELKKEIEELEEKVKELKElkeKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1146 SAILKLEANLKECEAK----HQDHIRTNDLSAKEVKFREEVTRLAN-NLHDTKQLLQSKEEENEISRQETEKLKEELAAN 1220
Cdd:PRK03918 338 ERLEELKKKLKELEKRleelEERHELYEEAKAKKEELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1221 SILTQNLKADLQK---------------KEEDCAELKEKFidaKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQ 1285
Cdd:PRK03918 418 KKEIKELKKAIEElkkakgkcpvcgrelTEEHRKELLEEY---TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1286 DLDMKQ--RTIQQLKEQLSN---QKMEEAVQQYEKVCKD---LSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADW 1357
Cdd:PRK03918 495 LIKLKElaEQLKELEEKLKKynlEELEKKAEEYEKLKEKlikLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAE 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1358 LATEL--------DKWKEKFKDLETRSNQRLN-TGTMDDLDVLTRKFSKLQDELQESEEKYkADRKKWLEEkavLTTQAK 1428
Cdd:PRK03918 575 LLKELeelgfesvEELEERLKELEPFYNEYLElKDAEKELEREEKELKKLEEELDKAFEEL-AETEKRLEE---LRKELE 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1429 EAENVRNREmrKYADDRERCLKLQNEVETLTAQLaeknSELQKWREERDQLVTAVETQMKALlsscKHKDEEIQELRKAA 1508
Cdd:PRK03918 651 ELEKKYSEE--EYEELREEYLELSRELAGLRAEL----EELEKRREEIKKTLEKLKEELEER----EKAKKELEKLEKAL 720
|
..
gi 569007259 1509 AK 1510
Cdd:PRK03918 721 ER 722
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
818-1429 |
1.65e-11 |
|
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: 69.71 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 818 EMQQSVSEVVEGNRVLKEKNEELKRLltiGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAV 897
Cdd:TIGR02169 259 EISELEKRLEEIEQLLEELNKKIKDL---GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 898 AELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSlDSPSHISKIDLLNLQDLSSGAKGDNCLNT 977
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD-ELKDYREKLEKLKREINELKRELDRLQEE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 978 SQQLpggdfsstwvkeyhTQEISRensFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQ 1057
Cdd:TIGR02169 415 LQRL--------------SEELAD---LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1058 ESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAK-IKDLE---------VIVETQ 1127
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERyATAIEvaagnrlnnVVVEDD 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1128 KDECK---------------------RLVELEQSILEKESAILKLeANLKECEAKHQ--------DHIRTNDL-SAKE-- 1175
Cdd:TIGR02169 558 AVAKEaiellkrrkagratflplnkmRDERRDLSILSEDGVIGFA-VDLVEFDPKYEpafkyvfgDTLVVEDIeAARRlm 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1176 ---------------------------------VKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSI 1222
Cdd:TIGR02169 637 gkyrmvtlegelfeksgamtggsraprggilfsRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1223 LTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDL------------DMK 1290
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndlearlshsriPEI 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1291 QRTIQQLKEQLSnqKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQ-----EQTQAEQDRVLEAKSEEADwLATELDKW 1365
Cdd:TIGR02169 797 QAELSKLEEEVS--RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQridlkEQIKSIEKEIENLNGKKEE-LEEELEEL 873
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569007259 1366 KEKFKDLETRSnqrlnTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKE 1429
Cdd:TIGR02169 874 EAALRDLESRL-----GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1134-1509 |
2.22e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1134 LVELEQSI--LEKESAI----LKLEANLKECEAKHQdHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISR 1207
Cdd:COG1196 195 LGELERQLepLERQAEKaeryRELKEELKELEAELL-LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1208 QETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDL 1287
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1288 DMKQRTIQQLKEQLSNQKMEEAVQQyekvcKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKE 1367
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAE-----EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1368 KFKDLEtrsnqrlntgtmddldvltrkfsKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRER 1447
Cdd:COG1196 429 ALAELE-----------------------EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569007259 1448 CLKLQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQMKALLSSCKHKDEEIQELRKAAA 1509
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA 547
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
991-1479 |
2.39e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.94 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 991 VKEYHTQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQesqgKNRDHQLKE 1070
Cdd:PRK03918 170 VIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL----KEEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1071 KESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILK 1150
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1151 LEANLKECEAKHQdhiRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELaansiltqnlkad 1230
Cdd:PRK03918 326 IEERIKELEEKEE---RLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKL------------- 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1231 lqkkEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKK-------------------NQYSQDLDMKQ 1291
Cdd:PRK03918 390 ----EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteehrkellEEYTAELKRIE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1292 RTIQQLKEQLSNQKME-EAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQdrvLEAKSEEADWLATELDKWKEKFK 1370
Cdd:PRK03918 466 KELKEIEEKERKLRKElRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEE---LEKKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1371 DLETRSNQrlntgtmddLDVLTRKFSKLQDELQESEEKyKADRKKWLEEKAV-----LTTQAKEAENVRNR--EMRKYAD 1443
Cdd:PRK03918 543 SLKKELEK---------LEELKKKLAELEKKLDELEEE-LAELLKELEELGFesveeLEERLKELEPFYNEylELKDAEK 612
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 569007259 1444 DRERCLK----LQNEVETLTAQLAEKNSELQKWREERDQL 1479
Cdd:PRK03918 613 ELEREEKelkkLEEELDKAFEELAETEKRLEELRKELEEL 652
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1069-1309 |
8.29e-11 |
|
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: 67.40 E-value: 8.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1069 KEKESLIQQLRE---ELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVivetqkdeckRLVELEQSILEKE 1145
Cdd:TIGR02169 688 RELSSLQSELRRienRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE----------DLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1146 SAILKLEANLKECEAK-HQDHIRTNDLSAKEV------------KFREEVTRLANNLHDTKQLLQSKEEENEISRQETEK 1212
Cdd:TIGR02169 758 SELKELEARIEELEEDlHKLEEALNDLEARLShsripeiqaelsKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1213 LKEELaansILTQNLKADLQKKEEDC----AELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLD 1288
Cdd:TIGR02169 838 LQEQR----IDLKEQIKSIEKEIENLngkkEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913
|
250 260
....*....|....*....|.
gi 569007259 1289 MKQRTIQQLKEQLSNQKMEEA 1309
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEELS 934
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1125-1552 |
1.06e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.09 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1125 ETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTND--LSAKEVKFREEVTRLANNLHDTKQLLQSKEEE 1202
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADeaKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1203 NEisRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLlriKINELEKKKNQ 1282
Cdd:PTZ00121 1328 KK--KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK---KADEAKKKAEE 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1283 YsqdldmKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATEL 1362
Cdd:PTZ00121 1403 D------KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK 1476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1363 DKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKfSKLQDELQESEEKYKADRKKWLEEK-----AVLTTQAKEAENVRNRE 1437
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKADEAKKAEEAkkadeAKKAEEKKKADELKKAE 1555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1438 MRKYADDRERCLKLQNEVETLTAQLaEKNSELQKWREERDQLVTAVETQMKALLSSCKHKDEE----IQELRKAAAKSTG 1513
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMAL-RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikAEELKKAEEEKKK 1634
|
410 420 430
....*....|....*....|....*....|....*....
gi 569007259 1514 TENQTMNPKPEYNDSVDLGGVETEPQSTSLEISRNTAED 1552
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1024-1505 |
2.73e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.45 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1024 SKKSHQIQGLEEQIEK-----LQVEVKGYREENSDLRAQ----ESQGKNRDHQLKEKESLI---QQLREELQEKSVSLRV 1091
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEkeekdLHERLNGLESELAELDEEieryEEQREQARETRDEADEVLeehEERREELETLEAEIED 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1092 QVQLVAEREQALSELSQdvtcykaKIKDLEVIVETQKDECKRLV-ELEQSILEKESAILKLEAnLKECEAKHQDHIRTND 1170
Cdd:PRK02224 263 LRETIAETEREREELAE-------EVRDLRERLEELEEERDDLLaEAGLDDADAEAVEARREE-LEDRDEELRDRLEECR 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1171 LSAKEvkFREEVTRLANNLHDTkqllqskEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKK 1250
Cdd:PRK02224 335 VAAQA--HNEEAESLREDADDL-------EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1251 QIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAvqqyEKVCKdLSVKEKLVEDM 1330
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGS----PHVET-IEEDRERVEEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1331 RLTLVEQEQTQAEQDRVLEaKSEEADWLATELDKWKEKFKDLETRSNQRLNTgtmddLDVLTRKFSKLQDELQESEEkyK 1410
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLE-RAEDLVEAEDRIERLEERREDLEELIAERRET-----IEEKRERAEELRERAAELEA--E 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1411 ADRKkwlEEKAvlTTQAKEAENVR------NREMRKYADDRERClklqNEVETLTAQLAEKNSELQKWREERDQLvTAVE 1484
Cdd:PRK02224 553 AEEK---REAA--AEAEEEAEEAReevaelNSKLAELKERIESL----ERIRTLLAAIADAEDEIERLREKREAL-AELN 622
|
490 500
....*....|....*....|.
gi 569007259 1485 TQMKALLSSckhKDEEIQELR 1505
Cdd:PRK02224 623 DERRERLAE---KRERKRELE 640
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
833-1375 |
5.36e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 5.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 833 LKEKNEELKRLltigENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRD 912
Cdd:COG1196 234 LRELEAELEEL----EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 913 RILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQDLSSGAKGDNCLNTSQQLpggdfsSTWVK 992
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE------EELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 993 EYHT--QEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKE 1070
Cdd:COG1196 384 LAEEllEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1071 KESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVEtQKDECKRLVELEQSILEKESAILK 1150
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG-LRGLAGAVAVLIGVEAAYEAALEA 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1151 LEAnlkeceAKHQDHIRTNDLSAKEV------KFREEVTRLANNLHDTKQLLQSKEEENEISR-------------QETE 1211
Cdd:COG1196 543 ALA------AALQNIVVEDDEVAAAAieylkaAKAGRATFLPLDKIRARAALAAALARGAIGAavdlvasdlreadARYY 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1212 KLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQ 1291
Cdd:COG1196 617 VLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELE 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1292 RTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADwlateLDKWKEKFKD 1371
Cdd:COG1196 697 EALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD-----LEELERELER 771
|
....
gi 569007259 1372 LETR 1375
Cdd:COG1196 772 LERE 775
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
831-1181 |
1.01e-09 |
|
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: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 831 RVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQasynsavAELQTQKAVNQEQ 910
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE-------QEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 911 RDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSL-----DSPSHiSKIDllNLQDLSSGAKGDNCLNTS--QQLPG 983
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlndleARLSH-SRIP--EIQAELSKLEEEVSRIEArlREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 984 GDFSSTWVKEYHTQEIsrensfhASIEAIWEECKEIVKASSKKSHQIQG----LEEQIEKLQVEVKGYREENSDLRAQEs 1059
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEI-------QELQEQRIDLKEQIKSIEKEIENLNGkkeeLEEELEELEAALRDLESRLGDLKKER- 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1060 qgKNRDHQLKEKESLIQQLREELQEKSvslrvqvQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKrlveLEQ 1139
Cdd:TIGR02169 892 --DELEAQLRELERKIEELEAQIEKKR-------KRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED----VQA 958
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 569007259 1140 SILEKESAILKLE-ANLKECEAKHQDHIRTNDLSAKEVKFREE 1181
Cdd:TIGR02169 959 ELQRVEEEIRALEpVNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
673-1346 |
1.37e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 673 VEDIFHSLQDDVTDIKKQAELAHLYITslvdpqeaiacLQLKFNQVKAELAETKEELIKAQEELKNRESNSLVQALKtss 752
Cdd:COG1196 191 LEDILGELERQLEPLERQAEKAERYRE-----------LKEELKELEAELLLLKLRELEAELEELEAELEELEAELE--- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 753 kvdtSLTSNKSTCNETSEmpkNSRAQTHSERKRLNEDGLQLgeppakkglilvsppiTEEQNKMGEMQQSVSEVVEGNRV 832
Cdd:COG1196 257 ----ELEAELAELEAELE---ELRLELEELELELEEAQAEE----------------YELLAELARLEQDIARLEERRRE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 833 LKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRD 912
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 913 RILKLSQEMETAARSIESNVSQIKQMQTKIDELRsldspshiskidllnlqdlssgakgdnclntsqqlpggdfsstwvk 992
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELE---------------------------------------------- 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 993 eyhtqeisrensfhASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKE 1072
Cdd:COG1196 428 --------------EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1073 SLIQQLREELQEKSVSLRVQVQLVAER--EQALSELSQDVTCYKAKIKD------LEVIVETQKDECKRLVELEQSILEK 1144
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLLAGLRglAGAVAVLIGVEAAYEAALEAalaaalQNIVVEDDEVAAAAIEYLKAAKAGR 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1145 ESAI----LKLEANLKECEAKHQDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAN 1220
Cdd:COG1196 574 ATFLpldkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1221 SILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQ 1300
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 569007259 1301 LSNQKMEEAVQQYEkvcKDLSVKEKLVEDMRLTLVEQEQTQAEQDR 1346
Cdd:COG1196 734 REELLEELLEEEEL---LEEEALEELPEPPDLEELERELERLEREI 776
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
793-1488 |
1.43e-09 |
|
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: 63.45 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 793 LGEPPAKKGLILVSPPITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLT------------IGENELRNEKEEKAE 860
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTpcmpdtyherkqVLEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 861 LNKQVVSLQQQLRFFEEKnSSLRADVEQIQASynsaVAELQTQKAVNQEQRDRILKLSQEMETAArsIESNVSQI-KQMQ 939
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQ-LKKQQLLKQLRAR----IEELRAQEAVLEETQERINRARKAAPLAA--HIKAVTQIeQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 940 TKIDELRS-LDSPSHISKIDLLNLQDLSSGAKGDNCLNTSQQ----LPGGDFSSTWVKEYHTQEISRENSFHASIEAIwE 1014
Cdd:TIGR00618 311 RIHTELQSkMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSqeihIRDAHEVATSIREISCQQHTLTQHIHTLQQQK-T 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1015 ECKEIVKASSKKSHQIQGLEEQIEKLQVEvkgYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQ 1094
Cdd:TIGR00618 390 TLTQKLQSLCKELDILQREQATIDTRTSA---FRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1095 LVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDE----CKRLVELEQsileKESAILKLEANLKECE------AKHQD 1164
Cdd:TIGR00618 467 SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcplCGSCIHPNP----ARQDIDNPGPLTRRMQrgeqtyAQLET 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1165 HIRTNDLSAKEVK-----FREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANS----ILTQNLKADLQKKE 1235
Cdd:TIGR00618 543 SEEDVYHQLTSERkqrasLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSeaedMLACEQHALLRKLQ 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1236 EDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINE----LEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQ 1311
Cdd:TIGR00618 623 PEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREhalsIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQC 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1312 QYEKVCKDLSVKE--KLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADwlatELDKWKEKFKDLE-TRSNQRLNTGTMDDl 1388
Cdd:TIGR00618 703 QTLLRELETHIEEydREFNEIENASSSLGSDLAAREDALNQSLKELM----HQARTVLKARTEAhFNNNEEVTAALQTG- 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1389 dvltRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRErclKLQNEVETLTAQLAEKNSE 1468
Cdd:TIGR00618 778 ----AELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEE---QFLSRLEEKSATLGEITHQ 850
|
730 740
....*....|....*....|
gi 569007259 1469 LQKWREERDQLVTAVETQMK 1488
Cdd:TIGR00618 851 LLKYEECSKQLAQLTQEQAK 870
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1009-1505 |
1.46e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1009 IEAIWEECKEIVKASSKKShqiQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVS 1088
Cdd:COG4717 48 LERLEKEADELFKPQGRKP---ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1089 LRVQvQLVAEREQALSELSQDVTCYKakikdlevivetqkdeckRLVELEQSILEKESAILKLEANLKECEAKHQDHIRT 1168
Cdd:COG4717 125 LQLL-PLYQELEALEAELAELPERLE------------------ELEERLEELRELEEELEELEAELAELQEELEELLEQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1169 NDLSAKE--VKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFI 1246
Cdd:COG4717 186 LSLATEEelQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1247 DAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQlsnqkmeeavqQYEKVCKDLSVKEKL 1326
Cdd:COG4717 266 GSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEE-----------ELEELLAALGLPPDL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1327 VEDMRLTLVEQEQTQAEQDRVLEAKSEEADWlateldkwkekfKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDelqese 1406
Cdd:COG4717 335 SPEELLELLDRIEELQELLREAEELEEELQL------------EELEQEIAALLAEAGVEDEEELRAALEQAEE------ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1407 ekykadRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRerclkLQNEVETLTAQLAEKNSELQKWREERDQLvtavETQ 1486
Cdd:COG4717 397 ------YQELKEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELEEELEELEEELEELREELAEL----EAE 461
|
490
....*....|....*....
gi 569007259 1487 MKALLSsckhkDEEIQELR 1505
Cdd:COG4717 462 LEQLEE-----DGELAELL 475
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1033-1509 |
2.94e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1033 LEEQIEKLQ---VEVKGYREENSDLRAQEsqgknrdHQLKEkeslIQQLREELQEKSVSLRVQVQLVAEREQALSELSQD 1109
Cdd:COG4913 223 TFEAADALVehfDDLERAHEALEDAREQI-------ELLEP----IRELAERYAAARERLAELEYLRAALRLWFAQRRLE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1110 VtcYKAKIKDLEvivetqkdecKRLVELEQSILEKESAILKLEANLKECEAKHQDH--IRTNDLSAKEVKFREEVTRLAN 1187
Cdd:COG4913 292 L--LEAELEELR----------AELARLEAELERLEARLDALREELDELEAQIRGNggDRLEQLEREIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1188 NLHDTKQLLQSKEEENEISRQETEKLKEELAAnsiLTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREvsvmrdeek 1267
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEEFAALRAEAAA---LLEALEEELEALEEALAEAEAALRDLRRELRELEAE--------- 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1268 llrikINELEKKKNQYSQDLdmkQRTIQQLKEQLS------------------NQKMEEAV---------------QQYE 1314
Cdd:COG4913 428 -----IASLERRKSNIPARL---LALRDALAEALGldeaelpfvgelievrpeEERWRGAIervlggfaltllvppEHYA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1315 KVCK---DLSVKEKLV-EDMRLTLVEQEQTQAEQD---RVLEAKSEEA-DWLATELDKWK--------EKFKDLE---TR 1375
Cdd:COG4913 500 AALRwvnRLHLRGRLVyERVRTGLPDPERPRLDPDslaGKLDFKPHPFrAWLEAELGRRFdyvcvdspEELRRHPraiTR 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1376 SNQRLNTGTM---DD-----------------LDVLTRKFSKLQDELQESEEKY---KADRKKWLEEKAVLTTQAKEAEN 1432
Cdd:COG4913 580 AGQVKGNGTRhekDDrrrirsryvlgfdnrakLAALEAELAELEEELAEAEERLealEAELDALQERREALQRLAEYSWD 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1433 VRN-----REMRKYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQL---VTAVETQMKALLSSCKHKDEEIQEL 1504
Cdd:COG4913 660 EIDvasaeREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELkgeIGRLEKELEQAEEELDELQDRLEAA 739
|
....*
gi 569007259 1505 RKAAA 1509
Cdd:COG4913 740 EDLAR 744
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
868-1524 |
7.14e-09 |
|
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: 60.99 E-value: 7.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 868 LQQQLRFFEEKNSSLRADVE----QIQASYNSAVA----ELQTQKAVNQEQRDRILKLSQEMETaarSIESNVSQIKQMQ 939
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDikesKLGSSMNSIKTfwspELKKERALRKEEAARISVLKEQYRV---TQEENQHLQLTIQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 940 TKIDELRsldspSHISKIDLLNLQDLSSGAKGDNCLNTSQQLPGGDFSSTWVKEYHTQEIS-----------RENSFHAS 1008
Cdd:pfam10174 78 ALQDELR-----AQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFllrktleemelRIETQKQT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1009 IEAIWEECKEIV-----KASSKKS--------HQIQGLEEQIEKLQVEVKGYREENSDLRaQESQGKNRDHQLKEKESLI 1075
Cdd:pfam10174 153 LGARDESIKKLLemlqsKGLPKKSgeedwertRRIAEAEMQLGHLEVLLDQKEKENIHLR-EELHRRNQLQPDPAKTKAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1076 QQLREELQEKSVSL-RVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEAN 1154
Cdd:pfam10174 232 QTVIEMKDTKISSLeRNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1155 LKECEAKHQD---HIRT--NDLSAKEVK-------------------------------FREEVTRLANNLHDTKQLLQS 1198
Cdd:pfam10174 312 LETLTNQNSDckqHIEVlkESLTAKEQRaailqtevdalrlrleekesflnkktkqlqdLTEEKSTLAGEIRDLKDMLDV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1199 KEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDC-------AELKEKFIDAKKQIE----QVQREVSVMRDEEK 1267
Cdd:pfam10174 392 KERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSsntdtalTTLEEALSEKERIIErlkeQREREDRERLEELE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1268 LLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQ------------KMEEAVQQYEKVCKDLSVKEKLVEDMRLTLV 1335
Cdd:pfam10174 472 SLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLassglkkdsklkSLEIAVEQKKEECSKLENQLKKAHNAEEAVR 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1336 EQEQTqAEQDRVLEA----KSEEADWLATELDKWKEKFKDLETRSNQRlnTGTMDDLDVLTRKFSKLQD----ELQESEE 1407
Cdd:pfam10174 552 TNPEI-NDRIRLLEQevarYKEESGKAQAEVERLLGILREVENEKNDK--DKKIAELESLTLRQMKEQNkkvaNIKHGQQ 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1408 KYKADRKKWLEEkaVLTTQAKEAENVRNREMRKYADDRErclKLQNEVETLTAQ-------LAEKNSELQKWR-EERDQL 1479
Cdd:pfam10174 629 EMKKKGAQLLEE--ARRREDNLADNSQQLQLEELMGALE---KTRQELDATKARlsstqqsLAEKDGHLTNLRaERRKQL 703
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 569007259 1480 VTAVETQMKALLSSCKHKDEEIQELRKAAAKSTGTENQTMNPKPE 1524
Cdd:pfam10174 704 EEILEMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALKRE 748
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
831-1394 |
1.27e-08 |
|
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: 60.13 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 831 RVLKEKNEELKRLltigENELRNEKEE-KAELNKQVVSLQQQLRFFEeKNSSLRADVEQIQASYNSAVAELQTQKAVNQE 909
Cdd:pfam15921 419 RELDDRNMEVQRL----EALLKAMKSEcQGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVEELTAKKMTLES 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 910 QRDRILKLSQEMETAARSIESNVSQIKQMQTKIDelrsldspshiskIDLLNLQDLSSgaKGDNCLNTSQQLPGGDFSST 989
Cdd:pfam15921 494 SERTVSDLTASLQEKERAIEATNAEITKLRSRVD-------------LKLQELQHLKN--EGDHLRNVQTECEALKLQMA 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 990 wvKEYHTQEISRENSfhasieaiwEECKEIVKASSKKSHQIQGLEEQIEKlqvEVKGYREENSDLRAQESQgknRDHQLK 1069
Cdd:pfam15921 559 --EKDKVIEILRQQI---------ENMTQLVGQHGRTAGAMQVEKAQLEK---EINDRRLELQEFKILKDK---KDAKIR 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1070 EKESLIQQLREE----LQEKSVSLRVQVQLVAEREQALSE----------LSQDVTCYKAKIKDLEVIVETQKDECKRLV 1135
Cdd:pfam15921 622 ELEARVSDLELEkvklVNAGSERLRAVKDIKQERDQLLNEvktsrnelnsLSEDYEVLKRNFRNKSEEMETTTNKLKMQL 701
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1136 ELEQSILEKEsailklEANLKECEAKHQDHIRTNDLSAKEVKF-REEVTRLANNLHDTKQLLQSKEEENEISRQETEKLK 1214
Cdd:pfam15921 702 KSAQSELEQT------RNTLKSMEGSDGHAMKVAMGMQKQITAkRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS 775
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1215 EELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVS-----VMRDEEKLLRIKINE-LEKKKNQ---YSQ 1285
Cdd:pfam15921 776 QELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAecqdiIQRQEQESVRLKLQHtLDVKELQgpgYTS 855
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1286 DLDMKQRTIQ--QLKEQLSNQKMEEAVQQY--EKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEaDWLATE 1361
Cdd:pfam15921 856 NSSMKPRLLQpaSFTRTHSNVPSSQSTASFlsHHSRKTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAED-KGRAPS 934
|
570 580 590
....*....|....*....|....*....|...
gi 569007259 1362 LDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRK 1394
Cdd:pfam15921 935 LGALDDRVRDCIIESSLRSDICHSSSNSLQTEG 967
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
705-1254 |
1.36e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 705 QEAIACLQLKFNQVKAELAETKEELIKAQEELkNRESNSLVQALKTSSKVDTSLTSNKSTCNETSEmpknSRAQTHSERK 784
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELEL-EEAQAEEYELLAELARLEQDIARLEERRRELEE----RLEELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 785 RLNEDGLQLGEppAKKGLILVsppITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELNKQ 864
Cdd:COG1196 327 ELEEELEELEE--ELEELEEE---LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 865 VVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDE 944
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 945 LRSLDSPSHISKIDLLNLQDLSSGAkgdnclntsqqlpggdfsSTWVKEYHTQEISRENSFHASIEAIWEECKE--IVKA 1022
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEGF------------------LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEaaLEAA 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1023 SSKKSHQI-----QGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVA 1097
Cdd:COG1196 544 LAAALQNIvveddEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1098 EReqALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVK 1177
Cdd:COG1196 624 GR--TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569007259 1178 FREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQ 1254
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
719-1465 |
1.89e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 719 KAELAETKEELIKAQEELKNRESNSLVQALKTSSKVDTSLTSNKSTCNETSEMPKNSRAQTHSERKRLNEdgLQLGEPPA 798
Cdd:PTZ00121 1231 KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEE--KKKADEAK 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 799 KKGlilvsppitEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRlltigENELRNEKEEKAELnkqvvslqqqlrffEEK 878
Cdd:PTZ00121 1309 KKA---------EEAKKADEAKKKAEEAKKKADAAKKKAEEAKK-----AAEAAKAEAEAAAD--------------EAE 1360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 879 NSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKqmqtKIDELRSldSPSHISKID 958
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK----KADEAKK--KAEEKKKAD 1434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 959 LLNlQDLSSGAKGDNCLNTSQQLPGGDFSSTWVKEYHTQEISRENSFHASIEaiwEECKEIVKASSKKSHQIQGLEEQIE 1038
Cdd:PTZ00121 1435 EAK-KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA---DEAKKKAEEAKKKADEAKKAAEAKK 1510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1039 KLQvEVKGYREENSDLRAQESQGKNRDHQLKEKEsliQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKik 1118
Cdd:PTZ00121 1511 KAD-EAKKAEEAKKADEAKKAEEAKKADEAKKAE---EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE-- 1584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1119 dlevivETQKDECKRLVELEQsiLEKESAILKLEANLKECEAKhqdhirtndLSAKEVKFREEVTRlannlhDTKQLLQS 1198
Cdd:PTZ00121 1585 ------EAKKAEEARIEEVMK--LYEEEKKMKAEEAKKAEEAK---------IKAEELKKAEEEKK------KVEQLKKK 1641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1199 KEEEneisRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKlLRIKINELEK 1278
Cdd:PTZ00121 1642 EAEE----KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE-LKKKEAEEKK 1716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1279 KKNQYSQDLDMKQRTIQQLKeqlsnQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADwl 1358
Cdd:PTZ00121 1717 KAEELKKAEEENKIKAEEAK-----KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED-- 1789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1359 ATELDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKfsklqdELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREM 1438
Cdd:PTZ00121 1790 EKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK------EMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGED 1863
|
730 740
....*....|....*....|....*....
gi 569007259 1439 RKYADD--RERCLKLQNEVETLTAQLAEK 1465
Cdd:PTZ00121 1864 GNKEADfnKEKDLKEDDEEEIEEADEIEK 1892
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
834-1527 |
3.21e-08 |
|
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: 58.83 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 834 KEKNEELKRLLTIGENELRNEKEEKAELNKQvvslqqqlrffEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQrdr 913
Cdd:pfam02463 264 EEKLAQVLKENKEEEKEKKLQEEELKLLAKE-----------EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKE--- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 914 ILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQDLSSgakgdnclntsqqlpggDFSSTWVKE 993
Cdd:pfam02463 330 LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES-----------------ERLSSAAKL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 994 YHTQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKES 1073
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1074 LIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELeqsILEKESAILKLEA 1153
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGV---AVENYKVAISTAV 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1154 NLKECEAKHQDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLkadLQK 1233
Cdd:pfam02463 550 IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAK---VVE 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1234 KEEDCAELKEKFIDAKKQIEQVQREVSVMRDE-EKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQK-MEEAVQ 1311
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGLRKGVSLEEGLaEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLeIKKKEQ 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1312 QYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQ------RLNTGTM 1385
Cdd:pfam02463 707 REKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEkelaeeREKTEKL 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1386 DDLDVLTRKFSKLQDELQE--SEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCL-KLQNEVETLTAQL 1462
Cdd:pfam02463 787 KVEEEKEEKLKAQEEELRAleEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAeEELERLEEEITKE 866
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569007259 1463 AEKNSELQKWREERDQLVTAVETQMKALLSSCKHKDEEIQELRKAAAKSTGTENQTMNPKPEYND 1527
Cdd:pfam02463 867 ELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILL 931
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1014-1413 |
3.76e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1014 EECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYR---------EENSDLRAQESQGKNRDHQLKEKESLIQQLREELQE 1084
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEkllqllplyQELEALEAELAELPERLEELEERLEELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1085 KSVSL-RVQVQLVAEREQALSELSQDVTCYKAKIKDLEvivetqkdecKRLVELEQSILEKESAILKLEANLKECEAKHQ 1163
Cdd:COG4717 168 LEAELaELQEELEELLEQLSLATEEELQDLAEELEELQ----------QRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1164 DHIRTNDLSAKEVKFREEVTRLA-----NNLHDTKQ---------------LLQSKEEENEISRQETEKLKEELAANSIL 1223
Cdd:COG4717 238 AAALEERLKEARLLLLIAAALLAllglgGSLLSLILtiagvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1224 TQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKllRIKINELEKKKNQYSQDLDMKqrTIQQLKEQLSN 1303
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE--ELQLEELEQEIAALLAEAGVE--DEEELRAALEQ 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1304 -QKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDrvLEAKSEEadwLATELDKWKEKFKDLETRSNQRLNT 1382
Cdd:COG4717 394 aEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEE--LEEELEE---LEEELEELREELAELEAELEQLEED 468
|
410 420 430
....*....|....*....|....*....|.
gi 569007259 1383 GTmddLDVLTRKFSKLQDELQESEEKYKADR 1413
Cdd:COG4717 469 GE---LAELLQELEELKAELRELAEEWAALK 496
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
831-1490 |
5.26e-08 |
|
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: 58.21 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 831 RVLKEKNEELKRLLT-IGENELRNEKEeKAELNKQVVSLQQQLrffeeknsslradvEQIQASYNsAVAELQTQKAVNQE 909
Cdd:pfam15921 78 RVLEEYSHQVKDLQRrLNESNELHEKQ-KFYLRQSVIDLQTKL--------------QEMQMERD-AMADIRRRESQSQE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 910 Q-RDRILKLSQEMEtAARSIESNVsqIKQMQTKIDELRSLdSPSHISKidllnLQDLSSGAKgdnclntsqqlpggDFSS 988
Cdd:pfam15921 142 DlRNQLQNTVHELE-AAKCLKEDM--LEDSNTQIEQLRKM-MLSHEGV-----LQEIRSILV--------------DFEE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 989 TWVKEYHTQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREensdLRAQESQgkNRDHQL 1068
Cdd:pfam15921 199 ASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIE----LLLQQHQ--DRIEQL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1069 -KEKESLIQQLREELQE-KSVSLRVQVQLVAEREQALSELSQdvtcYKAKIKDLEVIV---ETQKDECKRLVELEQSILE 1143
Cdd:pfam15921 273 iSEHEVEITGLTEKASSaRSQANSIQSQLEIIQEQARNQNSM----YMRQLSDLESTVsqlRSELREAKRMYEDKIEELE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1144 KESAIlkleANLKECEAKhqdhirtndlsAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSIL 1223
Cdd:pfam15921 349 KQLVL----ANSELTEAR-----------TERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSIT 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1224 TQNLKADLQKKEEDCAELKEKFIDAKKQIE-QVQREVSVMRDEekllrikiNELEKKKNQYSQDLDMKQRTIQQLKEQLS 1302
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGK--------NESLEKVSSLTAQLESTKEMLRKVVEELT 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1303 NQKMeeAVQQYEKVCKDLSV----KEKLVE-------------DMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKW 1365
Cdd:pfam15921 486 AKKM--TLESSERTVSDLTAslqeKERAIEatnaeitklrsrvDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKV 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1366 KEKFKDletrsnqrlntgTMDDLDVLTRKFSKLQDELQESE---EKYKADRKKWLEEKAVLttqaKEAENVRNREMRKYA 1442
Cdd:pfam15921 564 IEILRQ------------QIENMTQLVGQHGRTAGAMQVEKaqlEKEINDRRLELQEFKIL----KDKKDAKIRELEARV 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 569007259 1443 DDrerclkLQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQMKAL 1490
Cdd:pfam15921 628 SD------LELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNEL 669
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1030-1316 |
5.49e-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: 58.16 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1030 IQGLEEQIEKlqvevkgYREENSDLRAQESQgknrdHQLKEKESLIQQLREELQEKSVSLRvqvqlvaEREQALSELSQD 1109
Cdd:TIGR02169 767 IEELEEDLHK-------LEEALNDLEARLSH-----SRIPEIQAELSKLEEEVSRIEARLR-------EIEQKLNRLTLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1110 VTCYKAKIKDLEVIVETQKDeckRLVELEQSILEKESAILKLEANLKECEAkhqdhiRTNDLSAKEVKFREEVTRLANNL 1189
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKE---QIKSIEKEIENLNGKKEELEEELEELEA------ALRDLESRLGDLKKERDELEAQL 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1190 HDtkqlLQSKEEENEISRQETEKLKEELAAN-SILTQNLKADLQKKEEDCAELKEKFI--DAKKQIEQVQREVSVMRD-- 1264
Cdd:TIGR02169 899 RE----LERKIEELEAQIEKKRKRLSELKAKlEALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRVEEEIRALEPvn 974
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 569007259 1265 -------EEKLLRikINELEKKKNQysqdLDMKQRTIQQLKEQLSNQKMEEAVQQYEKV 1316
Cdd:TIGR02169 975 mlaiqeyEEVLKR--LDELKEKRAK----LEEERKAILERIEEYEKKKREVFMEAFEAI 1027
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1008-1456 |
6.19e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1008 SIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLraqeSQGKNRDHQLKEKESLIQQLREELQEKSV 1087
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL----EEKEERLEELKKKLKELEKRLEELEERHE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1088 SLRVQVQLVAEREQALSELS-QDVTCYKAKIKDLEVIVETQKDECK----RLVELEQSILEKESAILKLEANLKEC---- 1158
Cdd:PRK03918 363 LYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISkitaRIGELKKEIKELKKAIEELKKAKGKCpvcg 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1159 ---EAKHQDHIrTNDLSAKEVKFREEVTRLANNLHDTKQLLqsKEEENEISRQET----EKLKEEL-AANSILTQNLKAD 1230
Cdd:PRK03918 443 relTEEHRKEL-LEEYTAELKRIEKELKEIEEKERKLRKEL--RELEKVLKKESEliklKELAEQLkELEEKLKKYNLEE 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1231 LQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEK---LLRIKINELEKKKNQYSQDLDMKQ-RTIQQLKEQLsnQKM 1306
Cdd:PRK03918 520 LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKklaELEKKLDELEEELAELLKELEELGfESVEELEERL--KEL 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1307 EEAVQQY---EKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLntg 1383
Cdd:PRK03918 598 EPFYNEYlelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRE--- 674
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569007259 1384 tmddldvLTRKFSKLQdELQESEEKYKADRKKWLEEKAVLTTQAKEAENVrNREMRKYADDRERCLKLQNEVE 1456
Cdd:PRK03918 675 -------LAGLRAELE-ELEKRREEIKKTLEKLKEELEEREKAKKELEKL-EKALERVEELREKVKKYKALLK 738
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1196-1410 |
6.53e-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: 56.70 E-value: 6.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1196 LQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINE 1275
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1276 LEKKKNQYSQDLDMKQRTIQQLKEQ------LSNQKMEEAVqqyekvcKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLE 1349
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQpplallLSPEDFLDAV-------RRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569007259 1350 AKSEEADWLATELDKWKEKFKDLETRSNQRLNTgtmddLDVLTRKFSKLQDELQESEEKYK 1410
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKL-----LARLEKELAELAAELAELQQEAE 223
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1204-1477 |
9.59e-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: 57.39 E-value: 9.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1204 EISRQETEKLKEElAANSILTQNLKADLQKKEEdcAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQY 1283
Cdd:TIGR02169 194 DEKRQQLERLRRE-REKAERYQALLKEKREYEG--YELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1284 SQDLDMKQRTIQQLKEQLSNQ---KMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLAT 1360
Cdd:TIGR02169 271 EQLLEELNKKIKDLGEEEQLRvkeKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1361 ELDKWKEKFKDLETRSN---QRL------NTGTMDDLDVLTRKFSKLQDELQESeekyKADRKKWLEEKAVLTTQAKEAE 1431
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEdlrAELeevdkeFAETRDELKDYREKLEKLKREINEL----KRELDRLQEELQRLSEELADLN 426
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 569007259 1432 NvrnremrKYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERD 1477
Cdd:TIGR02169 427 A-------AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
721-1303 |
1.22e-07 |
|
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: 56.95 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 721 ELAETKEELIKAQEELKNRE-------------------SNSLVQALKTSSK-VDTSLTSNKSTCNETSEMPKNSRAQTH 780
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEkelknldknlnkdeekinnSNNKIKILEQQIKdLNDKLKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 781 SERKRLNEDGLQLGEppAKKGLILVSPPITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAE 860
Cdd:TIGR04523 114 NDKEQKNKLEVELNK--LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 861 LNKQVVSLQQQLRFFEEKN----------SSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIES 930
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIqknkslesqiSELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 931 NVSQIKQMQTKIDELRSLdspshISKIDlLNLQDLSSGAKGDNCLNTSQQLPGGDFSSTWVKEYHTQEISRENSFHASIE 1010
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQ-----LNQLK-SEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1011 AIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQ----ESQGKNRDHQLKEKESLIQQLREELQEKS 1086
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQindlESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1087 VSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECK-----------RLVELEQSILEKESAILKLEANL 1155
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsinkikqNLEQKQKELKSKEKELKKLNEEK 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1156 KECEAKHQDHIRTNDLS-AKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLK--EELAANSILTQNLKADLQ 1232
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLkEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEknKEIEELKQTQKSLKKKQE 585
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569007259 1233 KKEEDCAELKEKFIDAKKQIE-------QVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSN 1303
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKEIEekekkisSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPE 663
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
820-1343 |
1.30e-07 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 57.01 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 820 QQSVSEVVEGNRVLKEKNEELKRLLTIGENEL---RNEKEEKAELNKQVVSLQ------QQLRFFEEKNSSLRADVeqiq 890
Cdd:COG5022 771 IKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLlslLGSRKEYRSYLACIIKLQktikreKKLRETEEVEFSLKAEV---- 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 891 aSYNSAVAELQTQKAVNQEQRDRIL-----------KLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDL 959
Cdd:COG5022 847 -LIQKFGRSLKAKKRFSLLKKETIYlqsaqrvelaeRQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEF 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 960 LNlqDLSSGAKgdnclntsQQLPGGDFSSTWVKEYHTQEISRE-NSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIE 1038
Cdd:COG5022 926 KT--ELIARLK--------KLLNNIDLEEGPSIEYVKLPELNKlHEVESKLKETSEEYEDLLKKSTILVREGNKANSELK 995
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1039 KLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQvQLVAEREQALSELSqdvtcykAKIK 1118
Cdd:COG5022 996 NFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQ-KLKGLLLLENNQLQ-------ARYK 1067
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1119 DLEVIVETQKDECKRLVELE-QSILEKesailklEANLKECEAKHQDHIrtndLSAKEVKFREEVTRLANNLHDTKQLLQ 1197
Cdd:COG5022 1068 ALKLRRENSLLDDKQLYQLEsTENLLK-------TINVKDLEVTNRNLV----KPANVLQFIVAQMIKLNLLQEISKFLS 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1198 SKEEENEISRQETEKLKEELAANSILTQN--------LKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEK-- 1267
Cdd:COG5022 1137 QLVNTLEPVFQKLSVLQLELDGLFWEANLealpspppFAALSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFsg 1216
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569007259 1268 -LLRIKINELEKKKNQYSQdldmkqrTIQQLKEQLSNQKmEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAE 1343
Cdd:COG5022 1217 wPRGDKLKKLISEGWVPTE-------YSTSLKGFNNLNK-KFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPAT 1285
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1056-1311 |
1.89e-07 |
|
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: 55.54 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1056 AQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEvivetqkdecKRLV 1135
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE----------AELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1136 ELEQSILEKESAILKLEANLKECEAKHQdhiRTNDLSAKEVKFR-EEVTRLANNLHDTKQLLQSKeeeneisRQETEKLK 1214
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALY---RLGRQPPLALLLSpEDFLDAVRRLQYLKYLAPAR-------REQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1215 EELAANSILTQNLKADLQKKEEDCAELKEKfidaKKQIEQVQREVsvmrdeekllRIKINELEKKKNQYSQDLDMKQRTI 1294
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEE----RAALEALKAER----------QKLLARLEKELAELAAELAELQQEA 222
|
250
....*....|....*..
gi 569007259 1295 QQLKEQLSNQKMEEAVQ 1311
Cdd:COG4942 223 EELEALIARLEAEAAAA 239
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1128-1477 |
2.22e-07 |
|
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: 56.13 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1128 KDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVKFRE------EVTRLANNLHDTKQLLQSKEE 1201
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEyllyldYLKLNEERIDLLQELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1202 ENEISRQETEKLKEELAansilTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKn 1281
Cdd:pfam02463 252 EIESSKQEIEKEEEKLA-----QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1282 qysqdldmkqrtiQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADwLATE 1361
Cdd:pfam02463 326 -------------AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLS-SAAK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1362 LDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKY 1441
Cdd:pfam02463 392 LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471
|
330 340 350
....*....|....*....|....*....|....*.
gi 569007259 1442 ADDRERCLKLQNEVETLTAQLAEKNSELQKWREERD 1477
Cdd:pfam02463 472 DLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS 507
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1116-1731 |
2.24e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1116 KIKDLEVIVETQKDECKRLVELEQSILE--KESAILKLEANLKECEAKHQDHIRtndlSAKEVKFREEVTRLannlHDTK 1193
Cdd:PTZ00121 1159 KAEDARKAEEARKAEDAKKAEAARKAEEvrKAEELRKAEDARKAEAARKAEEER----KAEEARKAEDAKKA----EAVK 1230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1194 QLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEdcAELKEKfIDAKKQIEQVQREVSVMRDEEKLlriKI 1273
Cdd:PTZ00121 1231 KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK--AEEARK-ADELKKAEEKKKADEAKKAEEKK---KA 1304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1274 NELEKKKNQYSQDLDMKQrtiqqlKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLvEQEQTQAEQDrvlEAKSE 1353
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEAKK------KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEA-EAAEEKAEAA---EKKKE 1374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1354 EADWLATELDK-WKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADR-KKWLEEKAVLTTQAKEAE 1431
Cdd:PTZ00121 1375 EAKKKADAAKKkAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEaKKKAEEAKKADEAKKKAE 1454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1432 NVRNRE-MRKYADDRERCLKLQNEVETltaqlAEKNSELQKWREER----DQLVTAVETQMKALLSSCKHKDEEIQELRK 1506
Cdd:PTZ00121 1455 EAKKAEeAKKKAEEAKKADEAKKKAEE-----AKKADEAKKKAEEAkkkaDEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1507 AAAKSTGTENQTMNPKPEYNDSVDLGGVETEPQSTSLEISRNTAEDGSVVLDSCEVSTENVQSTRFPKPELEIQFTPLQP 1586
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1587 NKMAVKHPGcptpvtiKIPKARKRKSGEVEEDLVKCENKKNSTPRSNVKFPVSEHRNSPVKKEQKVSVGPSSKKTYSLRS 1666
Cdd:PTZ00121 1610 EEAKKAEEA-------KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569007259 1667 QASTVSANIASKKREGTLQKFGDFLQHSPTILQSKAKKIIETMSSPKLSTVEVSKENVSQPKKAK 1731
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1231-1479 |
2.26e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1231 LQKKEEDCAELKEKFIDAKKQIEQVQREVsvmrdeeKLLRIKINELEKKKNQYSQDLDMK--QRTIQQLKEQL-----SN 1303
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAEL-------DALQERREALQRLAEYSWDEIDVAsaEREIAELEAELerldaSS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1304 QKMEEAVQQYEKVCKDLSVKEKLVEDM--RLTLVEQEQTQAE------QDRVLEAKSEEADWLATELDKWKEKFKDLETR 1375
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELkgEIGRLEKELEQAEeeldelQDRLEAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1376 SNQRLNTGtmDDLDVLTRKFSKLQDELQESEEKYKADrkkWLEEKAVLTTQAKEAENVRNREMRKYADD----RERCLKL 1451
Cdd:COG4913 765 RELRENLE--ERIDALRARLNRAEEELERAMRAFNRE---WPAETADLDADLESLPEYLALLDRLEEDGlpeyEERFKEL 839
|
250 260
....*....|....*....|....*....
gi 569007259 1452 QNevETLTAQLAEKNSELQKWREE-RDQL 1479
Cdd:COG4913 840 LN--ENSIEFVADLLSKLRRAIREiKERI 866
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
809-1374 |
3.26e-07 |
|
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: 55.41 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 809 ITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQ 888
Cdd:TIGR04523 70 INNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 889 IQASYNSAVAELQTQKAVNQEQRDRILKLSQEMEtaarSIESNVSQIKQmQTKIDELRSLDSPSHISKIDLLNLQdLSSG 968
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELENELNLLEKEKL----NIQKNIDKIKN-KLLKLELLLSNLKKKIQKNKSLESQ-ISEL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 969 AKGDNCLNTSQQLPGGDFSSTwvkeyhTQEIsreNSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYR 1048
Cdd:TIGR04523 224 KKQNNQLKDNIEKKQQEINEK------TTEI---SNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1049 EENSDLRAQESQGKNRD--HQLKEKESLIQQLREEL---QEKSVSLRVQV-QLVAEREQALSELSQDVTCYKAKIKDLEV 1122
Cdd:TIGR04523 295 SEISDLNNQKEQDWNKElkSELKNQEKKLEEIQNQIsqnNKIISQLNEQIsQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1123 IVETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVK-FREEVTRLANNLHDTKQLLQSKEE 1201
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIErLKETIIKNNSEIKDLTNQDSVKEL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1202 ENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKN 1281
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1282 QYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVED----MRLTLVEQEQTQAEQDRVLEAKSEEADW 1357
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKkqeeKQELIDQKEKEKKDLIKEIEEKEKKISS 614
|
570
....*....|....*..
gi 569007259 1358 LATELDKWKEKFKDLET 1374
Cdd:TIGR04523 615 LEKELEKAKKENEKLSS 631
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
848-1526 |
3.44e-07 |
|
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: 55.44 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 848 ENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQE---QRDRILKLSQEMETA 924
Cdd:TIGR00606 404 EDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQlegSSDRILELDQELRKA 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 925 ARSIeSNVSQIKQMQTKIDELRSLDSpshiSKIDLLnlQDLSSGAKGDNCLNTSQQLPGGDFSSTWVKEYHTQEISRENS 1004
Cdd:TIGR00606 484 EREL-SKAEKNSLTETLKKEVKSLQN----EKADLD--RKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKS 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1005 FHA----SIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEK--------- 1071
Cdd:TIGR00606 557 RHSdeltSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcgsqd 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1072 -ESLIQQLREELQEKSvslrvqvqlvaereQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEkesAILK 1150
Cdd:TIGR00606 637 eESDLERLKEEIEKSS--------------KQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQE---FISD 699
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1151 LEANLKECEAKHQDhirTNDLSAKEVKFREEVTRLANNlhdTKQLLQSKEEENEISRQETEKLKEELaansiltQNLKAD 1230
Cdd:TIGR00606 700 LQSKLRLAPDKLKS---TESELKKKEKRRDEMLGLAPG---RQSIIDLKEKEIPELRNKLQKVNRDI-------QRLKND 766
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1231 LQKKEEdcaeLKEKFIDAKKQIEQVQREVSVMRDeeklLRIKINELEKKKNQYSQDLDMK--QRTIQQLkeqlsNQKMEE 1308
Cdd:TIGR00606 767 IEEQET----LLGTIMPEEESAKVCLTDVTIMER----FQMELKDVERKIAQQAAKLQGSdlDRTVQQV-----NQEKQE 833
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1309 AVQQYEKVCKDLSVKEKLVEDmrltlvEQEQTQAEQDRVLEAKSEEADwLATELDKWKEKFKDLETRSN--QRLNTGTMD 1386
Cdd:TIGR00606 834 KQHELDTVVSKIELNRKLIQD------QQEQIQHLKSKTNELKSEKLQ-IGTNLQRRQQFEEQLVELSTevQSLIREIKD 906
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1387 DLDVLTRKFSKLQDELQESEE---KYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCLK-LQNEVETLTAQL 1462
Cdd:TIGR00606 907 AKEQDSPLETFLEKDQQEKEElisSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKqKETELNTVNAQL 986
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569007259 1463 AEKNSELQKWREERDQLVTAVETQ------MKALLSSCKHKDE--EIQELRKAAAKSTGtENQTMNPKPEYN 1526
Cdd:TIGR00606 987 EECEKHQEKINEDMRLMRQDIDTQkiqerwLQDNLTLRKRENElkEVEEELKQHLKEMG-QMQVLQMKQEHQ 1057
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1217-1475 |
7.85e-07 |
|
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: 53.61 E-value: 7.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1217 LAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQ 1296
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1297 LKEQLSNQKmeeavQQYEKVckdLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLEtrs 1376
Cdd:COG4942 95 LRAELEAQK-----EELAEL---LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1377 nqrlntgtmddldvltrkfsKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVE 1456
Cdd:COG4942 164 --------------------ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250
....*....|....*....
gi 569007259 1457 TLTAQLAEKNSELQKWREE 1475
Cdd:COG4942 224 ELEALIARLEAEAAAAAER 242
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1029-1315 |
8.14e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.99 E-value: 8.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1029 QIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKeslIQQLREELQEKSVSLRVQVQLVAEREQALSELsq 1108
Cdd:COG1340 9 SLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQ---VKELREEAQELREKRDELNEKVKELKEERDEL-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1109 dvtcyKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEanlkeceakhqDHIRTNDLS-AKEVKFREEVTRLAN 1187
Cdd:COG1340 84 -----NEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLE-----------WRQQTEVLSpEEEKELVEKIKELEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1188 NLHDTKQLLQSKEEENEIsRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEK 1267
Cdd:COG1340 148 ELEKAKKALEKNEKLKEL-RAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKAD 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 569007259 1268 LLRIKINELEKKKNQYSQDLD-MKQRTIQQLKEQLSNQKMEEAVQQYEK 1315
Cdd:COG1340 227 ELHEEIIELQKELRELRKELKkLRKKQRALKREKEKEELEEKAEEIFEK 275
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
867-1085 |
9.68e-07 |
|
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: 53.23 E-value: 9.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 867 SLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELR 946
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 947 SLDSpshiskiDLLNLQDLSSGAKGDNCLNTSQQLPGGDFSSTWVKEYHTQEISRENSFHASIEAIWEECKEIVKASSKK 1026
Cdd:COG4942 104 EELA-------ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 569007259 1027 SHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEK 1085
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
692-935 |
2.52e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 692 ELAHLYITSLVDPQEAIACLQLKFnqVKAELAETKEELIKAQEELKN-RESNSLVQALKTSSKVDTSLTSNKSTCNETse 770
Cdd:COG3206 156 ALAEAYLEQNLELRREEARKALEF--LEEQLPELRKELEEAEAALEEfRQKNGLVDLSEEAKLLLQQLSELESQLAEA-- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 771 mpknsRAQTHSERKRLNEDGLQLGEPPAKKGLILVSPPITEEQNKMGEMQQSVSEVVEG---------------NRVLKE 835
Cdd:COG3206 232 -----RAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARytpnhpdvialraqiAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 836 KNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLrffeeknsslrADVEQIQASYNsavaELQTQKAVNQEQRDRIL 915
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAREASLQAQLAQLEARL-----------AELPELEAELR----RLEREVEVARELYESLL 371
|
250 260
....*....|....*....|
gi 569007259 916 KLSQEMETAARSIESNVSQI 935
Cdd:COG3206 372 QRLEEARLAEALTVGNVRVI 391
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1230-1501 |
2.63e-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: 52.43 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1230 DLQKKEEDCAELKEK--------FIDAKKQIEQVQREVSVMRDeekllrikineLEKKKNQYSQDL-DMKQRTIQQLK-- 1298
Cdd:pfam15921 89 DLQRRLNESNELHEKqkfylrqsVIDLQTKLQEMQMERDAMAD-----------IRRRESQSQEDLrNQLQNTVHELEaa 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1299 EQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQA----EQD---------------RVLEAKSEEADWLA 1359
Cdd:pfam15921 158 KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGkkiyEHDsmstmhfrslgsaisKILRELDTEISYLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1360 TELDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMR 1439
Cdd:pfam15921 238 GRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR 317
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569007259 1440 KYADDRERCLKLQNE-----------VETLTAQLAEKNSELQKWREERDQLVTA---VETQMKALLSSCKHKDEEI 1501
Cdd:pfam15921 318 QLSDLESTVSQLRSElreakrmyedkIEELEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLHKREKEL 393
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1113-1510 |
3.13e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1113 YKAKIKDLEVIVETQKDECK-RLVELEQSILEKESAILkleanlkeceakhqdHIRTNDLSAKEVKFREEVTRLANN--- 1188
Cdd:PRK02224 167 YRERASDARLGVERVLSDQRgSLDQLKAQIEEKEEKDL---------------HERLNGLESELAELDEEIERYEEQreq 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1189 LHDTKQLLQSKEEENEISRQETEKLKEELAansiltqNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKL 1268
Cdd:PRK02224 232 ARETRDEADEVLEEHEERREELETLEAEIE-------DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1269 -------LRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNqkMEEAVQQYEKVCKDLSVK----EKLVEDMRLTLVEQ 1337
Cdd:PRK02224 305 ddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAES--LREDADDLEERAEELREEaaelESELEEAREAVEDR 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1338 EQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLEtrsnqrlntgtmDDLDVLTRKFSKLQDELQESEEKYKADRKKWL 1417
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR------------EERDELREREAELEATLRTARERVEEAEALLE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1418 EEKAVLTTQ-AKEAENVRNREmrkyaDDRERCLKLQNEVETLTAQ-------------LAEKNSELQKWREERDQLV--- 1480
Cdd:PRK02224 451 AGKCPECGQpVEGSPHVETIE-----EDRERVEELEAELEDLEEEveeveerleraedLVEAEDRIERLEERREDLEeli 525
|
410 420 430
....*....|....*....|....*....|....*..
gi 569007259 1481 ----TAVETQMKALLSSCKHKDE---EIQELRKAAAK 1510
Cdd:PRK02224 526 aerrETIEEKRERAEELRERAAEleaEAEEKREAAAE 562
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1021-1491 |
3.18e-06 |
|
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: 52.28 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1021 KASSKKSHQIQGLEEQIEKLQVE--VKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSvslrvqvqlvaE 1098
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLCTPcmPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQL-----------K 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1099 REQALSELSQDVTCYKAKIKDLEVIVETQKDECK--RLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEV 1176
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQEAVLEETQERINRARKaaPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1177 KFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAE---------------- 1240
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKEldilqreqatidtrts 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1241 ----LKEKFIDAKKQIEQVQREVSVMR-------DEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKE--QLSNQKME 1307
Cdd:TIGR00618 418 afrdLQGQLAHAKKQQELQQRYAELCAaaitctaQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRkkAVVLARLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1308 EAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADwLATELDKWKEKFKDLETRSnqrlnTGTMDD 1387
Cdd:TIGR00618 498 ELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEED-VYHQLTSERKQRASLKEQM-----QEIQQS 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1388 LDVLTRKFSKLQDELqESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEKNS 1467
Cdd:TIGR00618 572 FSILTQCDNRSKEDI-PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHA 650
|
490 500
....*....|....*....|....
gi 569007259 1468 ELQKWREERDQLVTAVETQMKALL 1491
Cdd:TIGR00618 651 LQLTLTQERVREHALSIRVLPKEL 674
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1063-1511 |
3.81e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1063 NRDHQLKEKEsLIQQLREELQEKSVSLRVQVQlvAEREQALSELSQDVTCYKAKIKDlevivETQKDECKRLVELEQSIL 1142
Cdd:PTZ00121 1037 NNDDVLKEKD-IIDEDIDGNHEGKAEAKAHVG--QDEGLKPSYKDFDFDAKEDNRAD-----EATEEAFGKAEEAKKTET 1108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1143 EK-ESAILKLEANLKECEAKHQDHIRtndlSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANS 1221
Cdd:PTZ00121 1109 GKaEEARKAEEAKKKAEDARKAEEAR----KAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKA 1184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1222 ILTQnlKADLQKKEEDCaelkeKFIDAKKQIEQVQR--EVSVMRDEEKLLRIKINELEKKKNQYSQDLDmKQRTIQQLKE 1299
Cdd:PTZ00121 1185 EEVR--KAEELRKAEDA-----RKAEAARKAEEERKaeEARKAEDAKKAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRK 1256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1300 QLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSE-EADWLATELDKWKEKFKDLETRSNQ 1378
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAKKKADAAKK 1336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1379 RLNTGTMDDlDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRN-REMRKYADDRErclKLQNEVET 1457
Cdd:PTZ00121 1337 KAEEAKKAA-EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKaDEAKKKAEEDK---KKADELKK 1412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 569007259 1458 LTAQlAEKNSELQKWREER---DQLVTAVETQMKAllSSCKHKDEEIQELRKAAAKS 1511
Cdd:PTZ00121 1413 AAAA-KKKADEAKKKAEEKkkaDEAKKKAEEAKKA--DEAKKKAEEAKKAEEAKKKA 1466
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1044-1312 |
4.31e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1044 VKGYREENSDLRAQESqgknrdhqlkekESLIQQLREELQEksvsLRVQVQlvaEREQALSELSQdvtcyKAKIKDLEvi 1123
Cdd:COG3206 158 AEAYLEQNLELRREEA------------RKALEFLEEQLPE----LRKELE---EAEAALEEFRQ-----KNGLVDLS-- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1124 vETQKDECKRLVELEQSILEKESAILKLEANLKECEAKhqdhIRTNDLSAKEVKFREEVTRLANnlhdtkQLLQSKEEEN 1203
Cdd:COG3206 212 -EEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ----LGSGPDALPELLQSPVIQQLRA------QLAELEAELA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1204 EISRQETEK------LKEELAAnsiltqnLKADLQkkeedcAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELE 1277
Cdd:COG3206 281 ELSARYTPNhpdviaLRAQIAA-------LRAQLQ------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELP 347
|
250 260 270
....*....|....*....|....*....|....*...
gi 569007259 1278 KKKNQYSQ---DLDMKQRTIQQLKEQLSNQKMEEAVQQ 1312
Cdd:COG3206 348 ELEAELRRlerEVEVARELYESLLQRLEEARLAEALTV 385
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1001-1146 |
4.91e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1001 RENSFHASIEAIWEECKEIVK-----ASSKKSHQIQGLEEQIEKLQVEV-KGYREENSDLRAQESQGKNRDHQLKEKESL 1074
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEeakkeAEAIKKEALLEAKEEIHKLRNEFeKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569007259 1075 IQQLREELQEKSVSLRVQVQLVAEREQALSELsqdvtcYKAKIKDLEVIVETQKDECKRLVeLEQsiLEKES 1146
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEEL------IEEQLQELERISGLTAEEAKEIL-LEK--VEEEA 167
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
848-1458 |
4.96e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.44 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 848 ENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAvnqeQRDRILKLSQEMETAA-- 925
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSS----LEDMKNRYESEIKTAEsd 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 926 -RSIESNVSQIKQMQTKIDELRSldSPSHISKIDLLNLQDLssgaKGDnCLNTSQQLPGGDfsstwvkeyhtQEISRENS 1004
Cdd:PRK01156 265 lSMELEKNNYYKELEERHMKIIN--DPVYKNRNYINDYFKY----KND-IENKKQILSNID-----------AEINKYHA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1005 FHASIEAIWEECKEIVKASSKKshqiqgleEQIEKLQVEVKGYREE-NSDLRAQESQGKNRDHQLKEKESLIQQLREELQ 1083
Cdd:PRK01156 327 IIKKLSVLQKDYNDYIKKKSRY--------DDLNNQILELEGYEMDyNSYLKSIESLKKKIEEYSKNIERMSAFISEILK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1084 EKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLevivETQKDECKRLVEleqsILEKESAILKLEANLKECEAKHQ 1163
Cdd:PRK01156 399 IQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRAL----RENLDELSRNME----MLNGQSVCPVCGTTLGEEKSNHI 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1164 DHIRTNDLSAKEVKFRE---EVTRLANNLHDTKQLLQSKEEEnEISRQETEKLKEElaansiltqNLKADLQKKEEDCAE 1240
Cdd:PRK01156 471 INHYNEKKSRLEEKIREieiEVKDIDEKIVDLKKRKEYLESE-EINKSINEYNKIE---------SARADLEDIKIKINE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1241 LKEKFIDAKKQIEQVQrevsvmrdeekllRIKINELEKKKNQY--------SQDLDMKQRTIQQLKEQLSNqkMEEAVQQ 1312
Cdd:PRK01156 541 LKDKHDKYEEIKNRYK-------------SLKLEDLDSKRTSWlnalavisLIDIETNRSRSNEIKKQLND--LESRLQE 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1313 YEKVCKDL-SVKEKLVEDMRltlveqeqtqaEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRlnTGTMDDLDVL 1391
Cdd:PRK01156 606 IEIGFPDDkSYIDKSIREIE-----------NEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEI--DSIIPDLKEI 672
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1392 TRKFSKLQDELQESE---EKYKADRKKWLEEKAVLTTQAKEAeNVRNREMRKYADDRERCLKLQNEVETL 1458
Cdd:PRK01156 673 TSRINDIEDNLKKSRkalDDAKANRARLESTIEILRTRINEL-SDRINDINETLESMKKIKKAIGDLKRL 741
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1027-1279 |
5.44e-06 |
|
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: 50.92 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1027 SHQIQGLEEQIEKLQVEVKgyrEENSDLRAQESQGKNRDHQLKEKESLIQQLREELQeksvslrvqvqlvaEREQALSEL 1106
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIA---ELEKELAALKKEEKALLKQLAALERRIAALARRIR--------------ALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1107 SQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANlkeceaKHQDHIRTNDLSAKEVKFREEvtrLA 1186
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPE------DFLDAVRRLQYLKYLAPARRE---QA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1187 NNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsiLTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQRevsvmrdEE 1266
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEE---ERAALEALKAERQKLLARLEKELAELAAELAELQQ-------EA 222
|
250
....*....|...
gi 569007259 1267 KLLRIKINELEKK 1279
Cdd:COG4942 223 EELEALIARLEAE 235
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1285-1513 |
7.86e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 7.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1285 QDLDMKQRTIQQLKEQLSN-QKMEEAVQQYEKVCKDLSVKEKLVEdmRLTLVEQEQTQAEQDRVLEAKSEEADWLATELD 1363
Cdd:COG4913 235 DDLERAHEALEDAREQIELlEPIRELAERYAAARERLAELEYLRA--ALRLWFAQRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1364 KWKEKFKDLETR----SNQRLNTGTmDDLDVLTRKFSKLQDELQESEEKYK--ADRKKWLEEKAVLTTQA-KEAENVRNR 1436
Cdd:COG4913 313 RLEARLDALREEldelEAQIRGNGG-DRLEQLEREIERLERELEERERRRArlEALLAALGLPLPASAEEfAALRAEAAA 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569007259 1437 EMRKYADDRERclkLQNEVETLTAQLAEKNSELQKWREERDQLvtavETQMKALlssckhkDEEIQELRKAAAKSTG 1513
Cdd:COG4913 392 LLEALEEELEA---LEEALAEAEAALRDLRRELRELEAEIASL----ERRKSNI-------PARLLALRDALAEALG 454
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1278-1510 |
8.71e-06 |
|
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: 50.15 E-value: 8.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1278 KKKNQYSQDLDMKQRTIQQLKEQLSNQKmeeavQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADW 1357
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALK-----KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1358 LATELDKWKEKFKDLeTRSNQR----------LNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQa 1427
Cdd:COG4942 95 LRAELEAQKEELAEL-LRALYRlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1428 keaenvrnremrkyaddrerclklQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQMKALLSSCKHKDEEIQELRKA 1507
Cdd:COG4942 173 ------------------------RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
...
gi 569007259 1508 AAK 1510
Cdd:COG4942 229 IAR 231
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
843-1313 |
1.13e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 843 LLTIGENELRNEKEE-------KAELN-KQVVSLQQQLRFFEEKNSSLRADVEQIQaSYNSAVAELQTQKAVNQEQRDRI 914
Cdd:COG4717 43 IRAMLLERLEKEADElfkpqgrKPELNlKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 915 LKLSQ------EMETAARSIESNVSQIKQMQTKIDELRSLdspshISKIDLLNLQdlssgakgdnclntsqqlpggdfss 988
Cdd:COG4717 122 EKLLQllplyqELEALEAELAELPERLEELEERLEELREL-----EEELEELEAE------------------------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 989 twVKEYHTQEISRENSFHASIEAIWEECKEivkasskkshQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQL 1068
Cdd:COG4717 172 --LAELQEELEELLEQLSLATEEELQDLAE----------ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1069 KEKESLIQQLRE--------ELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQS 1140
Cdd:COG4717 240 ALEERLKEARLLlliaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1141 ILEKESAILKLEANLKECEAKHQ-DHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENE--------ISRQETE 1211
Cdd:COG4717 320 ELEELLAALGLPPDLSPEELLELlDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEeelraaleQAEEYQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1212 KLKEELAANSILTQNLKADLQKKE-EDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKkknqySQDLDMK 1290
Cdd:COG4717 400 LKEELEELEEQLEELLGELEELLEaLDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE-----DGELAEL 474
|
490 500
....*....|....*....|...
gi 569007259 1291 QRTIQQLKEQLSNQKMEEAVQQY 1313
Cdd:COG4717 475 LQELEELKAELRELAEEWAALKL 497
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1033-1367 |
1.21e-05 |
|
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: 49.89 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1033 LEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREEL-------------------------QEKSV 1087
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELrqsrekheeleekykelsasseelsEEKDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1088 SLRVQvqlvAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLV-ELEQSILEKESAILKLEANLKECEAKHQDHI 1166
Cdd:pfam07888 120 LLAQR----AAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGaQRKEEEAERKQLQAKLQQTEEELRSLSKEFQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1167 RTNDLSAKE----VKFREEVTRLANNLHDTKQllqsKEEENEISRQETEKLKEELAANSILTQNLKADLQkkeedcaelk 1242
Cdd:pfam07888 196 ELRNSLAQRdtqvLQLQDTITTLTQKLTTAHR----KEAENEALLEELRSLQERLNASERKVEGLGEELS---------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1243 ekfiDAKKQIEQVQREVSVMRDEEKLLRIKINE----LEKKKNQYSQDLDMKQRTIQQLKEQLSN-----QKMEEAVQQ- 1312
Cdd:pfam07888 262 ----SMAAQRDRTQAELHQARLQAAQLTLQLADaslaLREGRARWAQERETLQQSAEADKDRIEKlsaelQRLEERLQEe 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569007259 1313 ------------YEKVCKDLSVKEKLVE------DMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELD-KWKE 1367
Cdd:pfam07888 338 rmereklevelgREKDCNRVQLSESRRElqelkaSLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVADaKWSE 411
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
828-1374 |
1.54e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 828 EGNRVLKEKNEELKRLLTIGE--NELRNEKE----EKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQ 901
Cdd:PRK02224 238 EADEVLEEHEERREELETLEAeiEDLRETIAeterEREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 902 TQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSldspshiskidllNLQDLSSGAKgdnclNTSQQL 981
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE-------------EAAELESELE-----EAREAV 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 982 pggdfsstwvkeyhtqeisreNSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQG 1061
Cdd:PRK02224 380 ---------------------EDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTA 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1062 KNRdhqLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDeckrLVELE--- 1138
Cdd:PRK02224 439 RER---VEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED----LVEAEdri 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1139 QSILEKESAILKLEANLKEceakhqdhiRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELA 1218
Cdd:PRK02224 512 ERLEERREDLEELIAERRE---------TIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1219 ANsiltqnlkadlqkKEEdcaelkekfIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLK 1298
Cdd:PRK02224 583 EL-------------KER---------IESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELE 640
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569007259 1299 EQLSNQKMEEAVQQYEKVCKDLsvkEKLVEDMRLTLVEQEQTQAEQDRVlEAKSEEADWLATELDKWKEKFKDLET 1374
Cdd:PRK02224 641 AEFDEARIEEAREDKERAEEYL---EQVEEKLDELREERDDLQAEIGAV-ENELEELEELRERREALENRVEALEA 712
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
809-1331 |
2.29e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 809 ITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQ 888
Cdd:PRK03918 205 VLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 889 IQA----------------SYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPS 952
Cdd:PRK03918 285 LKElkekaeeyiklsefyeEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELY 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 953 HISKIDLLNLQDLSSGAKGDNCLNTSQQLPggdfSSTWVKEYHTQEISRENSFHASIEAIWEECKEIVKA--SSKKSHQI 1030
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLTPEKLEKELE----ELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkKAKGKCPV 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1031 QGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQ----ALSEL 1106
Cdd:PRK03918 441 CGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKlkkyNLEEL 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1107 SQDVTCY---KAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANLKECeakhqdHIRTNDLSAKEVKFREEVT 1183
Cdd:PRK03918 521 EKKAEEYeklKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL------LKELEELGFESVEELEERL 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1184 RLANNLHDTKQLLQSKEEENEISRQETEKLKEELaansiltqnlkadlQKKEEDCAELKEKFIDAKKQIEQVQREVSVMR 1263
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKLEEEL--------------DKAFEELAETEKRLEELRKELEELEKKYSEEE 660
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569007259 1264 DEEKL-----LRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLsnQKMEEAVQQYEKVCKDLSVKEKLVEDMR 1331
Cdd:PRK03918 661 YEELReeyleLSRELAGLRAELEELEKRREEIKKTLEKLKEEL--EEREKAKKELEKLEKALERVEELREKVK 731
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1240-1490 |
2.71e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1240 ELKEKFIDAKKQIEQVQREVS---------VMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLsnQKMEEAV 1310
Cdd:PRK02224 166 EYRERASDARLGVERVLSDQRgsldqlkaqIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETR--DEADEVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1311 QQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEqdrvleakseeadwLATELDKWKEKFKDLETRSNQRLNTGTMDDLDV 1390
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETEREREE--------------LAEEVRDLRERLEELEEERDDLLAEAGLDDADA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1391 LTrkFSKLQDELQESEEKYKADrkkwLEEKAVLTTQA-KEAENVRNRemrkyADDRE-RCLKLQNEVETLTAQLAEKNSE 1468
Cdd:PRK02224 310 EA--VEARREELEDRDEELRDR----LEECRVAAQAHnEEAESLRED-----ADDLEeRAEELREEAAELESELEEAREA 378
|
250 260
....*....|....*....|..
gi 569007259 1469 LQKWREERDQLVTAVETQMKAL 1490
Cdd:PRK02224 379 VEDRREEIEELEEEIEELRERF 400
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1055-1479 |
3.18e-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: 49.02 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1055 RAQESQGKNrDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDeckRL 1134
Cdd:pfam01576 16 KVKERQQKA-ESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEE---RS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1135 VELEQSILEKESAILKLEANLKECEAKHQD-HIRTNDLSAKEVKFREEVTRLA---NNLHDTKQLLQskEEENEISRQET 1210
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLDEEEAARQKlQLEKVTTEAKIKKLEEDILLLEdqnSKLSKERKLLE--ERISEFTSNLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1211 EK--------------------LKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLR 1270
Cdd:pfam01576 170 EEeekakslsklknkheamisdLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAAL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1271 IKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAvqQYEKVCKDLS-----VKEKLVEDMRLTLVEQEQTQAEQD 1345
Cdd:pfam01576 250 ARLEEETAQKNNALKKIRELEAQISELQEDLESERAARN--KAEKQRRDLGeeleaLKTELEDTLDTTAAQQELRSKREQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1346 RVLEAK---SEEADWLATELDKWKEK-FKDLETRSNQ-----RLNTGTMDDLDVLTRKFSKLQDELQE-SEEKYKADRKK 1415
Cdd:pfam01576 328 EVTELKkalEEETRSHEAQLQEMRQKhTQALEELTEQleqakRNKANLEKAKQALESENAELQAELRTlQQAKQDSEHKR 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569007259 1416 WLEEKAVLTTQAKEAENVRNRemrkyADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQL 1479
Cdd:pfam01576 408 KKLEGQLQELQARLSESERQR-----AELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSL 466
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
561-1279 |
3.63e-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: 48.86 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 561 ECRVSTCHKKNKELLDLIEKLNKRLINENKE-KLTLELKIREEVtqeftqywsqreadfkeTLLHEREILEENAERRLAI 639
Cdd:TIGR04523 81 EQQIKDLNDKLKKNKDKINKLNSDLSKINSEiKNDKEQKNKLEV-----------------ELNKLEKQKKENKKNIDKF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 640 FKDLVGKCDSQDEPTNRICDIELETEEAHNYVG-VEDIFHSLQDDVTDIKKQAELAHLYITSLVDPQEAIACLQLKFNQV 718
Cdd:TIGR04523 144 LTEIKKKEKELEKLNNKYNDLKKQKEELENELNlLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISEL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 719 KAELAETKEELIKAQEEL--KNRESNSLVQALKTSSKvdtSLTSNKSTCNETSEMPKNSRAQTHSERKRLNEDGLQLGEP 796
Cdd:TIGR04523 224 KKQNNQLKDNIEKKQQEIneKTTEISNTQTQLNQLKD---EQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 797 PAKKGLILVSPPITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLltigENELRNEKEEKAELNKQVVSLQQQLRFFE 876
Cdd:TIGR04523 301 NNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL----KKELTNSESENSEKQRELEEKQNEIEKLK 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 877 EKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISK 956
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 957 IDLLNLQDlssgakgdnclntsqqlpggdfsstwvkeyhtqeisrenSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQ 1036
Cdd:TIGR04523 457 KNLDNTRE---------------------------------------SLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1037 IEKLQVEVKGYREENSDLRAQESQGKNRDHQL----KEKESLIQQLREELQEKSVSLRVQV--QLVAEREQALSELSQDV 1110
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLesekKEKESKISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQTQ 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1111 TCYKAKIKDLEVIVETQKDECKrlvELEQSILEKESAILKLEANLKECEAKHQdhirtndlsakevKFREEVTRLANNLH 1190
Cdd:TIGR04523 578 KSLKKKQEEKQELIDQKEKEKK---DLIKEIEEKEKKISSLEKELEKAKKENE-------------KLSSIIKNIKSKKN 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1191 DTKQLLQS-KEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEK---------FIDAKKQIEQVQREVS 1260
Cdd:TIGR04523 642 KLKQEVKQiKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYitrmirikdLPKLEEKYKEIEKELK 721
|
730
....*....|....*....
gi 569007259 1261 VMRDEEKLLRIKINELEKK 1279
Cdd:TIGR04523 722 KLDEFSKELENIIKNFNKK 740
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1011-1493 |
3.84e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.68 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1011 AIWEECKEIVKASSKKSHQIQGLEEQIE-------KLQVEVKGYREensDLRAQESQGKNRDHQLKEKESLIQQLREELQ 1083
Cdd:pfam12128 224 EHWIRDIQAIAGIMKIRPEFTKLQQEFNtlesaelRLSHLHFGYKS---DETLIASRQEERQETSAELNQLLRTLDDQWK 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1084 EKSVSLR------------VQVQLVAEREQALSELSQDVTCYKAKIKDLEVI---VETQKDECKRLVELEQSILEKESA- 1147
Cdd:pfam12128 301 EKRDELNgelsaadaavakDRSELEALEDQHGAFLDADIETAAADQEQLPSWqseLENLEERLKALTGKHQDVTAKYNRr 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1148 --------------ILKLEANLKECEAKHQDHIRtNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEEneisrqetekL 1213
Cdd:pfam12128 381 rskikeqnnrdiagIKDKLAKIREARDRQLAVAE-DDLQALESELREQLEAGKLEFNEEEYRLKSRLGE----------L 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1214 KEELAAnSILTQNLKADLQKKEEDCAELKEKfidakkqIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRT 1293
Cdd:pfam12128 450 KLRLNQ-ATATPELLLQLENFDERIERAREE-------QEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSA 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1294 IQQLKEQLSNQK-------MEEAVQQYEKVCKDLSVKEKLVEDMRLTLVE---------------------------QEQ 1339
Cdd:pfam12128 522 LDELELQLFPQAgtllhflRKEAPDWEQSIGKVISPELLHRTDLDPEVWDgsvggelnlygvkldlkridvpewaasEEE 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1340 TQAEQDRVLEA------KSEEADWLATELDKWKEKFKDLETRSNQRLNtGTMDDLDVLTRKFSKLQDELQESEEKYKA-- 1411
Cdd:pfam12128 602 LRERLDKAEEAlqsareKQAAAEEQLVQANGELEKASREETFARTALK-NARLDLRRLFDEKQSEKDKKNKALAERKDsa 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1412 --DRKKWLEEKAVLTTQAKEAENVRNREMRKYAddRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQMKA 1489
Cdd:pfam12128 681 neRLNSLEAQLKQLDKKHQAWLEEQKEQKREAR--TEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKR 758
|
....
gi 569007259 1490 LLSS 1493
Cdd:pfam12128 759 DLAS 762
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1169-1384 |
4.19e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1169 NDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsiltqnLKADLQKKEEdcaELKEKFIDA 1248
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE-------AEAEIEERRE---ELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1249 KKQ-------------------IEQVQREVSVMRDEEKLLRiKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQK--ME 1307
Cdd:COG3883 96 YRSggsvsyldvllgsesfsdfLDRLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAAKaeLE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569007259 1308 EAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNTGT 1384
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
850-947 |
4.91e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 47.65 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 850 ELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAE---LQTQKAVNQEQRD----RILKLSQEME 922
Cdd:PRK09039 47 EISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAErsrLQALLAELAGAGAaaegRAGELAQELD 126
|
90 100
....*....|....*....|....*
gi 569007259 923 TAARSIESNVSQIKQMQTKIDELRS 947
Cdd:PRK09039 127 SEKQVSARALAQVELLNQQIAALRR 151
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1029-1219 |
5.32e-05 |
|
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: 47.45 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1029 QIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNR----DHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALS 1104
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRiralEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1105 ELSQ------------------DVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANLKEceakhqdhi 1166
Cdd:COG4942 115 RLGRqpplalllspedfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE--------- 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 569007259 1167 RTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAA 1219
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1029-1210 |
6.32e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1029 QIQGLEEQIEKLQVEVKGYREENSDLRAQEsQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQ 1108
Cdd:COG3206 183 QLPELRKELEEAEAALEEFRQKNGLVDLSE-EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1109 D--VTCYKAKIKDLE-----------------VIVETQKDECKRLV--ELEQSILEKESAILKLEANLKECEAKHQDH-I 1166
Cdd:COG3206 262 SpvIQQLRAQLAELEaelaelsarytpnhpdvIALRAQIAALRAQLqqEAQRILASLEAELEALQAREASLQAQLAQLeA 341
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 569007259 1167 RTNDLSAKEVKFReEVTRLANNLHDTKQLLQSKEEENEISRQET 1210
Cdd:COG3206 342 RLAELPELEAELR-RLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1230-1486 |
8.69e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 8.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1230 DLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQkmeeA 1309
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER----A 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1310 VQQYEkvckdlsvkeklvEDMRLTLVEQeqtqaeqdrVLEAKSeeadwlateldkwkekFKDLETRsnqrlntgtMDDLD 1389
Cdd:COG3883 93 RALYR-------------SGGSVSYLDV---------LLGSES----------------FSDFLDR---------LSALS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1390 VLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEKNSEL 1469
Cdd:COG3883 126 KIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
250
....*....|....*..
gi 569007259 1470 QKWREERDQLVTAVETQ 1486
Cdd:COG3883 206 AAAEAAAAAAAAAAAAA 222
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
702-1479 |
9.70e-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: 47.48 E-value: 9.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 702 VDPQEAIACLQLKFNQVKAELAETKEELIKAQEELKNrESNSLVQALKTSSKvdtsLTSNKSTCNETSEMPKNSRAQTHS 781
Cdd:pfam01576 218 TDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEE-ETAQKNNALKKIRE----LEAQISELQEDLESERAARNKAEK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 782 ERKRLNEDGLQLG--------------EPPAKKG--LILVSPPITEE----QNKMGEMQQSVSEVVEGnrvLKEKNEELK 841
Cdd:pfam01576 293 QRRDLGEELEALKteledtldttaaqqELRSKREqeVTELKKALEEEtrshEAQLQEMRQKHTQALEE---LTEQLEQAK 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 842 RLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAvaelqtqKAVNQEQRDRILKLSQEM 921
Cdd:pfam01576 370 RNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSES-------ERQRAELAEKLSKLQSEL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 922 ETAARSIESNVSQIKQMQTkidELRSLDSPSHiskiDLLNLQDLSSGAKgdncLNTSQQLPGGDFSSTWVKEYHTQEISR 1001
Cdd:pfam01576 443 ESVSSLLNEAEGKNIKLSK---DVSSLESQLQ----DTQELLQEETRQK----LNLSTRLRQLEDERNSLQEQLEEEEEA 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1002 ENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQvevkgyreenSDLRAQESQGKNRDHQLKEKESLIQQLREE 1081
Cdd:pfam01576 512 KRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQ----------RELEALTQQLEEKAAAYDKLEKTKNRLQQE 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1082 LQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAkikdlevIVETQKDECKRLvelEQSILEKESAILKLEANLKECEAK 1161
Cdd:pfam01576 582 LDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKA-------ISARYAEERDRA---EAEAREKETRALSLARALEEALEA 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1162 HQDHIRTNDLSAKE----VKFREEVTRLANNLHDTKQLLQSKEEEneiSRQETEKLKEELAANS----ILTQNLKADLQK 1233
Cdd:pfam01576 652 KEELERTNKQLRAEmedlVSSKDDVGKNVHELERSKRALEQQVEE---MKTQLEELEDELQATEdaklRLEVNMQALKAQ 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1234 KEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKknqysqdLDMKqrtIQQLKEQL--SNQKMEEAVQ 1311
Cdd:pfam01576 729 FERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKK-------LELD---LKELEAQIdaANKGREEAVK 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1312 QYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRvlEAKSEEADWLATEldkwkekfKDLETRSNQRlntgtmddldvl 1391
Cdd:pfam01576 799 QLKKLQAQMKDLQRELEEARASRDEILAQSKESEK--KLKNLEAELLQLQ--------EDLAASERAR------------ 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1392 tRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEKNSELQK 1471
Cdd:pfam01576 857 -RQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQK 935
|
....*...
gi 569007259 1472 WREERDQL 1479
Cdd:pfam01576 936 SESARQQL 943
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1246-1506 |
1.11e-04 |
|
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: 47.04 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1246 IDAKKQIEQVQREVSVMRDEeklLRIKINELEKKKNQYSQDL---DMKQRTIQQLKEQLSNQKMEEAV--QQYEKVCKDL 1320
Cdd:pfam17380 236 MERRKESFNLAEDVTTMTPE---YTVRYNGQTMTENEFLNQLlhiVQHQKAVSERQQQEKFEKMEQERlrQEKEEKAREV 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1321 SVKEKLVEDMRLTLVE---QEQTQAEQDRVLEAKSEEADWLATEldkwkEKFKDLETRSNQRL--NTGTMDDLDVLT--- 1392
Cdd:pfam17380 313 ERRRKLEEAEKARQAEmdrQAAIYAEQERMAMERERELERIRQE-----ERKRELERIRQEEIamEISRMRELERLQmer 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1393 -RKFSKLQDELqESEEKYK---ADRKKWLEEKAVLTTQA-KEAENVRNREMRKYADDRERCL--------KLQNEVETLT 1459
Cdd:pfam17380 388 qQKNERVRQEL-EAARKVKileEERQRKIQQQKVEMEQIrAEQEEARQREVRRLEEERAREMervrleeqERQQQVERLR 466
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 569007259 1460 AQLAE-KNSELQKWREERDQLVTAVETQMKALLSSCKHKDEEIQELRK 1506
Cdd:pfam17380 467 QQEEErKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERK 514
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
695-922 |
1.19e-04 |
|
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: 47.25 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 695 HLYITSLVDPQEAIACLQLKFNQVKAELAETKEELIKAQEELKN-RESNSLVQALKTSSKV--DTSLTSNKSTCNETSEM 771
Cdd:COG3096 825 HLAVAFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQlKEQLQLLNKLLPQANLlaDETLADRLEELREELDA 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 772 PKNSRA--QTHSERKRLNEDGLQlgeppakkglILVSPPITEEQnkmgeMQQSVSEVVEGNRVLKEKNEELK----RLLT 845
Cdd:COG3096 905 AQEAQAfiQQHGKALAQLEPLVA----------VLQSDPEQFEQ-----LQADYLQAKEQQRRLKQQIFALSevvqRRPH 969
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569007259 846 IGENELRNEKEEKAELNKQvvsLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEME 922
Cdd:COG3096 970 FSYEDAVGLLGENSDLNEK---LRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELE 1043
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
832-1408 |
1.26e-04 |
|
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: 47.04 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 832 VLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEK----NSSLRADVEQIQASYNSAVAELQTQKAVN 907
Cdd:pfam15921 261 LLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQarnqNSMYMRQLSDLESTVSQLRSELREAKRMY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 908 Q---EQRDRILKLSQEMETAARSIESNVSQikQMQTKIDELRSLDSPSHISKIDLlnlqdlsSGAKGDNclntsQQLPGG 984
Cdd:pfam15921 341 EdkiEELEKQLVLANSELTEARTERDQFSQ--ESGNLDDQLQKLLADLHKREKEL-------SLEKEQN-----KRLWDR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 985 DFSSTWVKEYHTQEISRENSFHASIEAIWEECK-EIVKASSKKSHQIQGLEEQIEKLqvevkgyreenSDLRAQesqgkn 1063
Cdd:pfam15921 407 DTGNSITIDHLRRELDDRNMEVQRLEALLKAMKsECQGQMERQMAAIQGKNESLEKV-----------SSLTAQ------ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1064 rdhqLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVE------- 1136
Cdd:pfam15921 470 ----LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNegdhlrn 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1137 -------LEQSILEKESAILKLEANLKECEAKHQDHIRT-NDLSAKEVKFREEVTRLANNLHDTKQLLQSK-----EEEN 1203
Cdd:pfam15921 546 vqteceaLKLQMAEKDKVIEILRQQIENMTQLVGQHGRTaGAMQVEKAQLEKEINDRRLELQEFKILKDKKdakirELEA 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1204 EISRQETEKLKeELAANSILTQNLKADLQKKEEDCAELKekfiDAKKQIEQVQREVSVMRdeeKLLRIKINELEKKKNQY 1283
Cdd:pfam15921 626 RVSDLELEKVK-LVNAGSERLRAVKDIKQERDQLLNEVK----TSRNELNSLSEDYEVLK---RNFRNKSEEMETTTNKL 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1284 SQDLDMKQRTIQQLKEQLsnQKMEEAVQQYEKVC----KDLSVKEKLVEDM--RLTLVEQEQTQAEQDR--VLEAK---S 1352
Cdd:pfam15921 698 KMQLKSAQSELEQTRNTL--KSMEGSDGHAMKVAmgmqKQITAKRGQIDALqsKIQFLEEAMTNANKEKhfLKEEKnklS 775
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 569007259 1353 EEADWLATELDKWKEKFKDLETRSnQRLNTGTMD---DLDVLTRKFSKLQDELQESEEK 1408
Cdd:pfam15921 776 QELSTVATEKNKMAGELEVLRSQE-RRLKEKVANmevALDKASLQFAECQDIIQRQEQE 833
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
811-1219 |
1.43e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 811 EEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGE--NELRNEKEEKAELNKQVVSLQQQLRFFEE---KNSSLRAD 885
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELREleeELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 886 VEQIQASYNSAVAELQTQKAVN-QEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQD 964
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 965 LSSGA-------KGDNCLNTSQQLPGGDFSSTWVKEYHTQEISRENSFHAsieaiwEECKEIVKASSKKSHQIQGLEEQI 1037
Cdd:COG4717 252 LLIAAallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG------KEAEELQALPALEELEEEELEELL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1038 EKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELsqdvtcykaki 1117
Cdd:COG4717 326 AALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA----------- 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1118 kdlevivETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEvkfrEEVTRLANNLHDTKQLLQ 1197
Cdd:COG4717 395 -------EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELE----EELEELREELAELEAELE 463
|
410 420
....*....|....*....|....
gi 569007259 1198 SKEEENEIS--RQETEKLKEELAA 1219
Cdd:COG4717 464 QLEEDGELAelLQELEELKAELRE 487
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1180-1465 |
1.50e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1180 EEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREV 1259
Cdd:COG4372 38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1260 SVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQ 1339
Cdd:COG4372 118 EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1340 TQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEE 1419
Cdd:COG4372 198 KEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEE 277
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 569007259 1420 KAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEK 1465
Cdd:COG4372 278 LEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1051-1375 |
1.58e-04 |
|
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: 46.66 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1051 NSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALselsqdvtcyKAKIKDLEVIVETQKDE 1130
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQEL----------QKRIRLLEKREAEAEEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1131 CKRLVELEQSILEKESAILKLeanLKECEAKHQDhirtndlsAKEVK--FREEVTRLANNLHDTKQLLQSKEEENEISRQ 1208
Cdd:pfam05557 71 LREQAELNRLKKKYLEALNKK---LNEKESQLAD--------AREVIscLKNELSELRRQIQRAELELQSTNSELEELQE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1209 ETEKLKEELAANSILTQNLKA-----------------DLQKKEEDCAELKekfiDAKKQIEQV---QREVSVMRDEEKL 1268
Cdd:pfam05557 140 RLDLLKAKASEAEQLRQNLEKqqsslaeaeqrikelefEIQSQEQDSEIVK----NSKSELARIpelEKELERLREHNKH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1269 LRIKINE---LEKKKNQYSQDLDMKQRTIQQL-KEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMR----------LTL 1334
Cdd:pfam05557 216 LNENIENkllLKEEVEDLKRKLEREEKYREEAaTLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSrrieqlqqreIVL 295
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 569007259 1335 VEQEQTQAEQDRVLEAKSEEadwLATELDKWKEKFKDLETR 1375
Cdd:pfam05557 296 KEENSSLTSSARQLEKARRE---LEQELAQYLKKIEDLNKK 333
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1061-1312 |
1.79e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1061 GKNRDHQLKEKESLIQQLREEL---QEKSVSLRVQVQLVAEREQALSELSQdvtcYKAKIKDLEVIVEtqkdeckRLVEL 1137
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELaeaEERLEALEAELDALQERREALQRLAE----YSWDEIDVASAER-------EIAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1138 EQSI--LEKESAILK-LEANLKECEAKHQDHIRT-NDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQET--E 1211
Cdd:COG4913 674 EAELerLDASSDDLAaLEEQLEELEAELEELEEElDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALleE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1212 KLKEELAANSI--LTQNLKADLQKKEEDCAELKEKFIDAKKQ--------IEQVQREVSVMRD-EEKLLRIKINELEKKK 1280
Cdd:COG4913 754 RFAAALGDAVEreLRENLEERIDALRARLNRAEEELERAMRAfnrewpaeTADLDADLESLPEyLALLDRLEEDGLPEYE 833
|
250 260 270
....*....|....*....|....*....|..
gi 569007259 1281 NQYsqdLDMKQRTIQQLKEQLsNQKMEEAVQQ 1312
Cdd:COG4913 834 ERF---KELLNENSIEFVADL-LSKLRRAIRE 861
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
100-190 |
1.82e-04 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 43.36 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 100 HLSEKSSGQVAQKFSFSKVFGPETSQKEFF--LGCIMQPVkdlLEGHSRLIFTYGLTNSGktytfqgteENIGILPRTLN 177
Cdd:pfam16796 44 TSSDGKIGSKNKSFSFDRVFPPESEQEDVFqeISQLVQSC---LDGYNVCIFAYGQTGSG---------SNDGMIPRARE 111
|
90
....*....|...
gi 569007259 178 VLFDSLQERLYTK 190
Cdd:pfam16796 112 QIFRFISSLKKGW 124
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
660-1295 |
1.90e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 660 IELETEEAHNYVGVEDIFHSLQDDVTDIKKQAELAHlyiTSLVDPQEAIACLQLKFNQVKAELAETKEEL--IKAQEELK 737
Cdd:PRK01156 175 IDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDE---KSHSITLKEIERLSIEYNNAMDDYNNLKSALneLSSLEDMK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 738 NRESNSLVQAlktSSKVDTSLTSNKSTCNETSEMPKNSRAQTHSERKRLNEDGLQLGEPPAKKGLIlvsPPITEEQNKMG 817
Cdd:PRK01156 252 NRYESEIKTA---ESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQIL---SNIDAEINKYH 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 818 EMQQSVSEvvegnrvlkekneelkrlLTIGENELRNEKEEKAELNKQvvslqqqlrffeeknsslRADVEQIQASYNSAV 897
Cdd:PRK01156 326 AIIKKLSV------------------LQKDYNDYIKKKSRYDDLNNQ------------------ILELEGYEMDYNSYL 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 898 AELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDelRSLDSPShiSKIDLLNLQDLSSGAKGDNCLNT 977
Cdd:PRK01156 370 KSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEIN--VKLQDIS--SKVSSLNQRIRALRENLDELSRN 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 978 SQQLPG-----------GDFSSTWVKEYHTQEISRENsfhasiEAIWEECKEIVKASSKKSHQIQgLEEQIEKLQV-EVK 1045
Cdd:PRK01156 446 MEMLNGqsvcpvcgttlGEEKSNHIINHYNEKKSRLE------EKIREIEIEVKDIDEKIVDLKK-RKEYLESEEInKSI 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1046 GYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELqeKSVSLRVqvqLVAEREQALSELSQdvtcykAKIKDLEVIvE 1125
Cdd:PRK01156 519 NEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRY--KSLKLED---LDSKRTSWLNALAV------ISLIDIETN-R 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1126 TQKDeckrlveleqsilEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVKfrEEVtrlaNNLHDTKQLLQSKEEENEI 1205
Cdd:PRK01156 587 SRSN-------------EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIE--NEA----NNLNNKYNEIQENKILIEK 647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1206 SRQETEKLKEELAAnsilTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQ 1285
Cdd:PRK01156 648 LRGKIDNYKKQIAE----IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINE 723
|
650
....*....|
gi 569007259 1286 DLDMKQRTIQ 1295
Cdd:PRK01156 724 TLESMKKIKK 733
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1304-1520 |
2.19e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1304 QKMEEAVQQYEKVCKDLSVKEKLVEDMR--LTLVEQEQTQAEQDRVLEAKSEEADWLA-----TELDKWKEKFKDLETRS 1376
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELErqLKSLERQAEKAERYKELKAELRELELALlvlrlEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1377 NQRLNTGTmDDLDVLTRKFSKLQDELQESEEKYKADRKKWLE---EKAVLTTQ---AKEAENVRNREMRKYADDRERCLK 1450
Cdd:TIGR02168 252 EEELEELT-AELQELEEKLEELRLEVSELEEEIEELQKELYAlanEISRLEQQkqiLRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1451 LQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQMKALLSSCKHKDEEIQELRKAAAKSTGTENQTMN 1520
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1069-1305 |
2.22e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1069 KEKESLIQQLRE-------ELQEKSVSLRVQ--VQLVAEREQALSELSQDV--------TCYKAKIKDLEVIVETQKDEc 1131
Cdd:PRK05771 16 SYKDEVLEALHElgvvhieDLKEELSNERLRklRSLLTKLSEALDKLRSYLpklnplreEKKKVSVKSLEELIKDVEEE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1132 krLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVKFREE--VTRLANNLHDTKQLLQSKEEENEISrQE 1209
Cdd:PRK05771 95 --LEKIEKEIKELEEEISELENEIKELEQEIERLEPWGNFDLDLSLLLGFkyVSVFVGTVPEDKLEELKLESDVENV-EY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1210 TEKLKEEL---------AANSILTQNLKADLQKKE-EDCAELKEKFIDAKKQIEQVQREvsvmrdEEKLlrikINELEKK 1279
Cdd:PRK05771 172 ISTDKGYVyvvvvvlkeLSDEVEEELKKLGFERLElEEEGTPSELIREIKEELEEIEKE------RESL----LEELKEL 241
|
250 260
....*....|....*....|....*.
gi 569007259 1280 KNQYSQDldmkqrtIQQLKEQLSNQK 1305
Cdd:PRK05771 242 AKKYLEE-------LLALYEYLEIEL 260
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
855-1093 |
2.48e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 855 KEEKAELNKQVVSLQQQLRFFEEKNSSLRAD-----VEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIE 929
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLVDLSeeaklLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 930 SN------VSQIKQMQTKIDELRSLDSPSHISKIDLLnlqdlssgakgdnclntsqqlpggdfsstwvkeyhtQEIsren 1003
Cdd:COG3206 261 QSpviqqlRAQLAELEAELAELSARYTPNHPDVIALR------------------------------------AQI---- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1004 sfhASIEAIWEEckEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGK--NRDHQLKEK--ESLIQQLR 1079
Cdd:COG3206 301 ---AALRAQLQQ--EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRrlEREVEVARElyESLLQRLE 375
|
250
....*....|....*
gi 569007259 1080 E-ELQEKSVSLRVQV 1093
Cdd:COG3206 376 EaRLAEALTVGNVRV 390
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1179-1447 |
2.95e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1179 REEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQRE 1258
Cdd:COG4372 51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1259 VSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQE 1338
Cdd:COG4372 131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1339 QTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLE 1418
Cdd:COG4372 211 SLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
250 260
....*....|....*....|....*....
gi 569007259 1419 EKAVLTTQAKEAENVRNREMRKYADDRER 1447
Cdd:COG4372 291 AALELKLLALLLNLAALSLIGALEDALLA 319
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
720-1510 |
3.14e-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: 45.94 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 720 AELAETKEELIKAQEELKNRESNSlVQALKTSSKVDTSLTSNKSTCNETSEMPKNSRAQTHSERKRLNEDGLQLGEPPAK 799
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKH-QQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 800 kglilvSPPITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELK------------RLLTIGENELRNEKEEKAeLNKQVVS 867
Cdd:pfam01576 91 ------SQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKvtteakikkleeDILLLEDQNSKLSKERKL-LEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 868 LQQQLRFFEEKNSSLradvEQIQASYNSAVAELqtqkavnQEQRDRILKLSQEMETAARSIESNVS----QIKQMQTKID 943
Cdd:pfam01576 164 FTSNLAEEEEKAKSL----SKLKNKHEAMISDL-------EERLKKEEKGRQELEKAKRKLEGESTdlqeQIAELQAQIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 944 ELRSLDSPSHISKIDLLNLQDLSSGAKgdnclntsqqlpggdfsstwvkeyhTQEISRENSFHASIEAIWEECKEIVKAS 1023
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLEEETAQK-------------------------NNALKKIRELEAQISELQEDLESERAAR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1024 SKKSHQIQGLEEQIEKLQVEVkgyrEENSDLRAQESQGKNRdhqlkeKESLIQQLREELQEKSVSLRVQVQLVAERE-QA 1102
Cdd:pfam01576 288 NKAEKQRRDLGEELEALKTEL----EDTLDTTAAQQELRSK------REQEVTELKKALEEETRSHEAQLQEMRQKHtQA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1103 LSELSQDVTCYKAKIKDLEVIVETQKDECKRLVE----LEQSILEKESAILKLEANLKECEAKHQDHIRT---------- 1168
Cdd:pfam01576 358 LEELTEQLEQAKRNKANLEKAKQALESENAELQAelrtLQQAKQDSEHKRKKLEGQLQELQARLSESERQraelaeklsk 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1169 ------------NDLSAKEVKFREEVTRLANNLHDTKQLLQS---------------KEEENEISRQ--ETEKLKEELAA 1219
Cdd:pfam01576 438 lqselesvssllNEAEGKNIKLSKDVSSLESQLQDTQELLQEetrqklnlstrlrqlEDERNSLQEQleEEEEAKRNVER 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1220 NSILTQNLKADLQKKEEDCAELKEKFIDAKKqieQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKE 1299
Cdd:pfam01576 518 QLSTLQAQLSDMKKKLEEDAGTLEALEEGKK---RLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQ 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1300 QLSNqkMEEAVQQYEKVCKDlsvkEKLVedmrltlveQEQTQAEQDRVlEAKSEEADW----LATELDKWKEKFKDLEtR 1375
Cdd:pfam01576 595 LVSN--LEKKQKKFDQMLAE----EKAI---------SARYAEERDRA-EAEAREKETralsLARALEEALEAKEELE-R 657
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1376 SNQRLNtGTMDDL-----DV--------------------LTRKFSKLQDELQESEekykaDRKKWLEekavLTTQAKEA 1430
Cdd:pfam01576 658 TNKQLR-AEMEDLvsskdDVgknvhelerskraleqqveeMKTQLEELEDELQATE-----DAKLRLE----VNMQALKA 727
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1431 ENVRNREMRKYADDRERclklqnevETLTAQLAEKNSELQKWREERDQLVTA---VETQMKALLS----SCKHKDEEIQE 1503
Cdd:pfam01576 728 QFERDLQARDEQGEEKR--------RQLVKQVRELEAELEDERKQRAQAVAAkkkLELDLKELEAqidaANKGREEAVKQ 799
|
....*..
gi 569007259 1504 LRKAAAK 1510
Cdd:pfam01576 800 LKKLQAQ 806
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
852-1081 |
3.29e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 852 RNEKEEKAELNKQVVSLQQQL----RFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMEtaarS 927
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIktynKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE----D 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 928 IESNVSQIKQMQTKIDelrsldspshiSKIDLLNlQDLSSGAKGDNCLNTSQQLPGGDfsstwvkeyhtqeisrensfhA 1007
Cdd:PHA02562 253 PSAALNKLNTAAAKIK-----------SKIEQFQ-KVIKMYEKGGVCPTCTQQISEGP---------------------D 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569007259 1008 SIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREE 1081
Cdd:PHA02562 300 RITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAE 373
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1179-1502 |
4.17e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 45.07 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1179 REEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsiltqnlkadLQKKEEDCAELKEKFIDAKKQIEQVQRE 1258
Cdd:pfam05622 6 QEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQ-----------LESGDDSGTPGGKKYLLLQKQLEQLQEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1259 VSVMRDEEKLLRIKINELEKK---KNQYSQDLDMKQRTIQQLKEQL-----SNQK---MEEAVQQYEKVCKDLSVKEKLV 1327
Cdd:pfam05622 75 NFRLETARDDYRIKCEELEKEvleLQHRNEELTSLAEEAQALKDEMdilreSSDKvkkLEATVETYKKKLEDLGDLRRQV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1328 EdmrlTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRsnqrlntgtmddLDVLTRKFSKLQDELQESEE 1407
Cdd:pfam05622 155 K----LLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGK------------LSEESKKADKLEFEYKKLEE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1408 KYKA---DRKKWLEEKAVL--------TTQAKEAENVRNREMRKYADD--------------RERCLKLQNEVETL---- 1458
Cdd:pfam05622 219 KLEAlqkEKERLIIERDTLretneelrCAQLQQAELSQADALLSPSSDpgdnlaaeimpaeiREKLIRLQHENKMLrlgq 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 569007259 1459 TAQLAEKNSELQKWREERDQLVTAVETQMKAL---LSSCKHKDEEIQ 1502
Cdd:pfam05622 299 EGSYRERLTELQQLLEDANRRKNELETQNRLAnqrILELQQQVEELQ 345
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
849-1147 |
4.38e-04 |
|
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: 44.75 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 849 NELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSI 928
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 929 ESNVSQIKQMqtkideLRSLDSPSHISKIDLLnlqdLSSgakgdnclntsqqlpggdfsstwvkeyhtqeisrensfhas 1008
Cdd:COG4942 100 EAQKEELAEL------LRALYRLGRQPPLALL----LSP----------------------------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1009 ieaiwEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQesqgknrdhqLKEKESLIQQLREELQEKSvs 1088
Cdd:COG4942 129 -----EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE----------RAELEALLAELEEERAALE-- 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 569007259 1089 lrvqvQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESA 1147
Cdd:COG4942 192 -----ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1249-1510 |
4.41e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1249 KKQIEQVQREVsvmRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQyekvcKDLSVKEKLVE 1328
Cdd:COG1196 199 ERQLEPLERQA---EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELE-----AELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1329 DMRLTLVEQEQT-QAEQDRVLEAKSEEADwLATELDKWKEKFKDLETRsnqrlntgtmddldvltrkfsklQDELQESEE 1407
Cdd:COG1196 271 ELRLELEELELElEEAQAEEYELLAELAR-LEQDIARLEERRRELEER-----------------------LEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1408 KYKADRKKWLEEKAVLTTQAKEAEnvrnremrkyADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLVTAvETQM 1487
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAE----------EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-LRAA 395
|
250 260
....*....|....*....|...
gi 569007259 1488 KALLSSCKHKDEEIQELRKAAAK 1510
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLER 418
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
931-1337 |
4.60e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 931 NVSQIKQMQTKIDELRSLDSPSHISKIDLLNLqdlssgaKGDnclntSQQLpggdFSStWVKEYhtQEISrENSFhASIE 1010
Cdd:PRK04778 27 NYKRIDELEERKQELENLPVNDELEKVKKLNL-------TGQ-----SEEK----FEE-WRQKW--DEIV-TNSL-PDIE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1011 AIWEECKEIVKAS--SKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKeslIQQLREELQEKSVS 1088
Cdd:PRK04778 86 EQLFEAEELNDKFrfRKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDL---YRELRKSLLANRFS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1089 -------LRVQV-QLVAEREQA---------------LSELSQDVTCYKAKIKDLEVIVETQKDE-----------CKRL 1134
Cdd:PRK04778 163 fgpaldeLEKQLeNLEEEFSQFveltesgdyveareiLDQLEEELAALEQIMEEIPELLKELQTElpdqlqelkagYREL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1135 VE---------LEQSILEKESAILKLEANLKECEAKH----QDHIRTN-----DLSAKEVKFREEVTRLANNLhdTKQLL 1196
Cdd:PRK04778 243 VEegyhldhldIEKEIQDLKEQIDENLALLEELDLDEaeekNEEIQERidqlyDILEREVKARKYVEKNSDTL--PDFLE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1197 QSKEEENEIsRQETEKLKE--ELAANSILTQ--------NLKADLQKKEEDCA-------ELKEKFIDAKKQIEQVQRE- 1258
Cdd:PRK04778 321 HAKEQNKEL-KEEIDRVKQsyTLNESELESVrqlekqleSLEKQYDEITERIAeqeiaysELQEELEEILKQLEEIEKEq 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1259 ------VSVMRDEEKLLRIKINELEKKK----------------NQYSQDLDMKQRTIQQLKEQLSNQK--MEEAVQQYE 1314
Cdd:PRK04778 400 eklsemLQGLRKDELEAREKLERYRNKLheikryleksnlpglpEDYLEMFFEVSDEIEALAEELEEKPinMEAVNRLLE 479
|
490 500
....*....|....*....|....*
gi 569007259 1315 KVCKDLSVKEKLVEDMR--LTLVEQ 1337
Cdd:PRK04778 480 EATEDVETLEEETEELVenATLTEQ 504
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1073-1299 |
5.40e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1073 SLIQQLREELQEKSVSLRVQVQLVAEREQALSEL----SQDVTCYKAKIKDLeviVETQKDECKRLVELEQSILEKESAI 1148
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQrkknGENIARKQNKYDEL---VEEAKTIKAEIEELTDELLNLVMDI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1149 LKLEANLKECEAKHQDHIRTNDLSAKEVKFREE-----------------VTRLANNLHDtkqlLQSKEEENEISRQETE 1211
Cdd:PHA02562 251 EDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqqisegpdrITKIKDKLKE----LQHSLEKLDTAIDELE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1212 KLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQ 1291
Cdd:PHA02562 327 EIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRG 406
|
....*...
gi 569007259 1292 RTIQQLKE 1299
Cdd:PHA02562 407 IVTDLLKD 414
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1031-1577 |
5.65e-04 |
|
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: 44.81 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1031 QGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQeksvslrvqvqlvAEREQALSELSqdv 1110
Cdd:pfam10174 70 QHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQ-------------SEHERQAKELF--- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1111 tCYKAKIKDLEVIVETQK-------DECKRLVELEQSI-LEKESAILKLEANLKECEAKHQDHIRTNDLSAKE---VKFR 1179
Cdd:pfam10174 134 -LLRKTLEEMELRIETQKqtlgardESIKKLLEMLQSKgLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEkenIHLR 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1180 EEVTR---LANNLHDTKQLLQSKE-EENEISRQETEKLKEELAANSILTQNLKADLQKKEE----DCAELKEKFIdaKKQ 1251
Cdd:pfam10174 213 EELHRrnqLQPDPAKTKALQTVIEmKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEikqmEVYKSHSKFM--KNK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1252 IEQVQREVSVMRDEEKLLRIKineLEKKKNQYSqdlDMKQRtIQQLKEQLSNQKMEEAVQQYEkvckdlsvkeklVEDMR 1331
Cdd:pfam10174 291 IDQLKQELSKKESELLALQTK---LETLTNQNS---DCKQH-IEVLKESLTAKEQRAAILQTE------------VDALR 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1332 LTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKekfkdletrsnqrlntgtmDDLDVLTRKFSKLQDELQESEEKYKa 1411
Cdd:pfam10174 352 LRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLK-------------------DMLDVKERKINVLQKKIENLQEQLR- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1412 DRKKWLEEKavlttqakeaenvrnremrkyaddRERCLKLQNE-------VETLTAQLAEKNSELQKWREERDQLvtavE 1484
Cdd:pfam10174 412 DKDKQLAGL------------------------KERVKSLQTDssntdtaLTTLEEALSEKERIIERLKEQRERE----D 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1485 TQMKALLSSCKHKDEEIQELRKAAAKSTGTENQTMNPKPEYNDSVDLGGVETEPQSTSLEISRNTAEDGSVVLDSCEVST 1564
Cdd:pfam10174 464 RERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKA 543
|
570
....*....|...
gi 569007259 1565 ENVQSTRFPKPEL 1577
Cdd:pfam10174 544 HNAEEAVRTNPEI 556
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
858-1330 |
5.90e-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: 45.04 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 858 KAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQ 937
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 938 MQTKIDELRSLDSPSHISKIDLLNLQDLSSGAKGdnclntsqqlpggdfsstwVKEYHTQEISRENSFHASIEAiweecK 1017
Cdd:TIGR00606 770 QETLLGTIMPEEESAKVCLTDVTIMERFQMELKD-------------------VERKIAQQAAKLQGSDLDRTV-----Q 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1018 EIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRvqvQLVA 1097
Cdd:TIGR00606 826 QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQ---SLIR 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1098 EREQALSELSQDVTCYKAKIKDLEVIVeTQKDECKRLVELEQSILEKEsaILKLEANLKECEAKHQDhirtndlsAKEVK 1177
Cdd:TIGR00606 903 EIKDAKEQDSPLETFLEKDQQEKEELI-SSKETSNKKAQDKVNDIKEK--VKNIHGYMKDIENKIQD--------GKDDY 971
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1178 FREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKadLQKKEEDCAELKEKFIDAKKQIEQVQr 1257
Cdd:TIGR00606 972 LKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLT--LRKRENELKEVEEELKQHLKEMGQMQ- 1048
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569007259 1258 eVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDM 1330
Cdd:TIGR00606 1049 -VLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDL 1120
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1029-1348 |
8.25e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1029 QIQGLEEQIEKLQVEVKGYREENSDLRAQESqgknrdhQLKEKESLIQQLrEELQEKSVSLRVQVQLVAEREQALSEL-- 1106
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELD-------ALQERREALQRL-AEYSWDEIDVASAEREIAELEAELERLda 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1107 -SQDVTCYKAKIKDLEVIVETQKDECKRLV----ELEQSILEKESAILKLEANLKECEAKHQDHIRTN-DLSAKEVKFRE 1180
Cdd:COG4913 683 sSDDLAALEEQLEELEAELEELEEELDELKgeigRLEKELEQAEEELDELQDRLEAAEDLARLELRALlEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1181 EVTRLANNLHDtkQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADL-----------QKKEEDCAELKEKFIDAK 1249
Cdd:COG4913 763 VERELRENLEE--RIDALRARLNRAEEELERAMRAFNREWPAETADLDADLeslpeylalldRLEEDGLPEYEERFKELL 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1250 KQ--IEQVQREVSVMRDEEKLLRIKINELEK--KKNQYSQD----LDMKQRTIQQLKE------QLSNQKMEEAVQQYEK 1315
Cdd:COG4913 841 NEnsIEFVADLLSKLRRAIREIKERIDPLNDslKRIPFGPGrylrLEARPRPDPEVREfrqelrAVTSGASLFDEELSEA 920
|
330 340 350
....*....|....*....|....*....|...
gi 569007259 1316 VCKDLsvkEKLVEdmRLTLVEQEQTQAEQDRVL 1348
Cdd:COG4913 921 RFAAL---KRLIE--RLRSEEEESDRRWRARVL 948
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1250-1478 |
8.32e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 43.09 E-value: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1250 KQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQL--SNQKMEEAVQQYEkvckDLSVKEKLV 1327
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELerTEERLAEALEKLE----EAEKAADES 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1328 EDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELD--------KWKEKFKDLE-TRSNQRLNTGTMDDLDVLTRKFSKL 1398
Cdd:pfam00261 77 ERGRKVLENRALKDEEKMEILEAQLKEAKEIAEEADrkyeevarKLVVVEGDLErAEERAELAESKIVELEEELKVVGNN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1399 QDELQESEEKYKADRKKWLEEKAVLTTQAKEAENvrnremrKYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQ 1478
Cdd:pfam00261 157 LKSLEASEEKASEREDKYEEQIRFLTEKLKEAET-------RAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQ 229
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1018-1480 |
8.98e-04 |
|
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: 44.19 E-value: 8.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1018 EIVKASSKKSHQIQGLEEQIEKLQVEVKGYREenSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVA 1097
Cdd:pfam02463 261 EKEEEKLAQVLKENKEEEKEKKLQEEELKLLA--KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1098 EREQALSELsqdvtcYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQdhirtndLSAKEVK 1177
Cdd:pfam02463 339 ELEKELKEL------EIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE-------LKSEEEK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1178 FREEVTRLANNLHDTKQLLQSKEEENEI---SRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFID-AKKQIE 1253
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEEKKEELEILEeeeESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQlVKLQEQ 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1254 QVQREVSVMRDEEKLLRIKINELEKKKNQYSQDL--------DMKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEK 1325
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGvggriisaHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQK 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1326 LVEDMRLTLVEQEQTQAE-QDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQE 1404
Cdd:pfam02463 566 LVRALTELPLGARKLRLLiPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKE 645
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569007259 1405 SEEKYKADRKKWLEEKAVLTTQAKEAENvRNREMRKYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLV 1480
Cdd:pfam02463 646 SGLRKGVSLEEGLAEKSEVKASLSELTK-ELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAE 720
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1014-1354 |
9.37e-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: 43.94 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1014 EECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYRE---ENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLR 1090
Cdd:pfam05483 377 DQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKilaEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLE 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1091 VQVQLVAEREQALSELSQDVTCY--KAKIKDLEVIVETQKdeckrlVELEQSILEKESAILKLEANlkeceaKHQDHIRT 1168
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTEleKEKLKNIELTAHCDK------LLLENKELTQEASDMTLELK------KHQEDIIN 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1169 NDlsakevKFREEVTRLANNLHDTK-QLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFID 1247
Cdd:pfam05483 525 CK------KQEERMLKQIENLEEKEmNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1248 AKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKeqlsnQKMEEAVQQYEKVCKDLSVKEK-- 1325
Cdd:pfam05483 599 LKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAK-----QKFEEIIDNYQKEIEDKKISEEkl 673
|
330 340 350
....*....|....*....|....*....|.
gi 569007259 1326 --LVEDMRLTLVEQEQTQAEQDRVLEAKSEE 1354
Cdd:pfam05483 674 leEVEKAKAIADEAVKLQKEIDKRCQHKIAE 704
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1455-1741 |
1.01e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 44.27 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1455 VETLTAQLAEKNSELQK---------WREERDQLVTAVETQMKALLssckhkdEEIQELRKAAAKSTGTENQTMNPKPEY 1525
Cdd:PTZ00108 1104 VEKLNAELEKKEKELEKlknttpkdmWLEDLDKFEEALEEQEEVEE-------KEIAKEQRLKSKTKGKASKLRKPKLKK 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1526 NDSVDLGGVETEPQSTSLEISRNTAEDGSVVLDSCEVSTENVQSTRFPKPELEIQFTplqpnKMAVKHPGCPTPVTIKIP 1605
Cdd:PTZ00108 1177 KEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKT-----KPKKSSVKRLKSKKNNSS 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1606 KARKRKSGEVEEDLVKCENKKNSTPRSNvkfpvsehrnspvkkeqkvSVGPSSKKTyslrSQASTVSANIASKKREGTLQ 1685
Cdd:PTZ00108 1252 KSSEDNDEFSSDDLSKEGKPKNAPKRVS-------------------AVQYSPPPP----SKRPDGESNGGSKPSSPTKK 1308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 569007259 1686 KFGDFLQHSPTILQSKAKKIIETMSSPKLST--VEVSKENVSQPKKAKRKLYRNEISS 1741
Cdd:PTZ00108 1309 KVKKRLEGSLAALKKKKKSEKKTARKKKSKTrvKQASASQSSRLLRRPRKKKSDSSSE 1366
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1230-1415 |
1.02e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1230 DLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEA 1309
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1310 VQQYEKvckdlsvkeklvedmRLTLVEQEQTQAEqDRVLEAKsEEADWLATELDKWKEKFKDLEtrsnqrlntgtmDDLD 1389
Cdd:COG1579 91 YEALQK---------------EIESLKRRISDLE-DEILELM-ERIEELEEELAELEAELAELE------------AELE 141
|
170 180
....*....|....*....|....*.
gi 569007259 1390 VLTRKFSKLQDELQESEEKYKADRKK 1415
Cdd:COG1579 142 EKKAELDEELAELEAELEELEAEREE 167
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
687-931 |
1.11e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 687 IKKQAELAHLYITSLVDPQ-EAIACLQLKFNQVKAELAETKEELIKAQEELKN--RESNSLVQALKTSSKVDTSLTSNKS 763
Cdd:PHA02562 193 IQQQIKTYNKNIEEQRKKNgENIARKQNKYDELVEEAKTIKAEIEELTDELLNlvMDIEDPSAALNKLNTAAAKIKSKIE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 764 TCNETSEMpknsraqthserkrlNEDGlqlGEPPAkkglilVSPPITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRL 843
Cdd:PHA02562 273 QFQKVIKM---------------YEKG---GVCPT------CTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEI 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 844 ltigENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELqtqKAVNQEQRDRILKLSQ-EME 922
Cdd:PHA02562 329 ----MDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEEL---AKLQDELDKIVKTKSElVKE 401
|
....*....
gi 569007259 923 TAARSIESN 931
Cdd:PHA02562 402 KYHRGIVTD 410
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1033-1345 |
1.18e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 43.69 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1033 LEEQIEKLQVEVkgyreensdLRAQESQGKNRDHQLKEK-ESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVT 1111
Cdd:PLN03229 434 LEGEVEKLKEQI---------LKAKESSSKPSELALNEMiEKLKKEIDLEYTEAVIAMGLQERLENLREEFSKANSQDQL 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1112 CYKAKIKDLEVIVE---------------TQKDECKRLVELEQSILEKESAILKLEAnlkECEAKHQDHIRTNDLSAKEV 1176
Cdd:PLN03229 505 MHPVLMEKIEKLKDefnkrlsrapnylslKYKLDMLNEFSRAKALSEKKSKAEKLKA---EINKKFKEVMDRPEIKEKME 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1177 KFREEVtrlannlhdTKQLLQSKEEENEISRQETEKLKEELA---ANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIE 1253
Cdd:PLN03229 582 ALKAEV---------ASSGASSGDELDDDLKEKVEKMKKEIElelAGVLKSMGLEVIGVTKKNKDTAEQTPPPNLQEKIE 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1254 QVQREVS-----VMRDEEKLLRIKINELEKKKNQYSQDLDMKQrTIQQLKEQLsNQKMEEAVQQYEkvckdlsVKEKLvE 1328
Cdd:PLN03229 653 SLNEEINkkierVIRSSDLKSKIELLKLEVAKASKTPDVTEKE-KIEALEQQI-KQKIAEALNSSE-------LKEKF-E 722
|
330
....*....|....*..
gi 569007259 1329 DMRLTLVEQEQTQAEQD 1345
Cdd:PLN03229 723 ELEAELAAARETAAESN 739
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1072-1215 |
1.28e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1072 ESLIQQLREELQEKSVSLRVQVQLVAEREQALSElsqdvtcykAKIKDLEVIVETQKDEckrLVELEQSILEKESAILKL 1151
Cdd:COG2433 379 EEALEELIEKELPEEEPEAEREKEHEERELTEEE---------EEIRRLEEQVERLEAE---VEELEAELEEKDERIERL 446
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569007259 1152 EANLKEceakhqdhIRTNdlSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKE 1215
Cdd:COG2433 447 ERELSE--------ARSE--ERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1026-1315 |
1.31e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 43.48 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1026 KSHQIQGLE------EQIEKLQVEVKGYREENSDLRAQESQ------GKNR---------------DHQLKEKESLIQQL 1078
Cdd:pfam05701 27 KAHRIQTVErrklveLELEKVQEEIPEYKKQSEAAEAAKAQvleeleSTKRlieelklnleraqteEAQAKQDSELAKLR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1079 REELQ-----EKSVSLRVQVQLVAER-EQALSELSQdvtcYKAKIKDLE---VIVETQKDECKRLVE---LEQSILEK-- 1144
Cdd:pfam05701 107 VEEMEqgiadEASVAAKAQLEVAKARhAAAVAELKS----VKEELESLRkeyASLVSERDIAIKRAEeavSASKEIEKtv 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1145 ESAILKLEANLKECEAKHQDHirtndLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQ--ETEKLKEELAANSI 1222
Cdd:pfam05701 183 EELTIELIATKESLESAHAAH-----LEAEEHRIGAALAREQDKLNWEKELKQAEEELQRLNQQllSAKDLKSKLETASA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1223 LTQNLKADL---------------QKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKI----NELEKKKnqy 1283
Cdd:pfam05701 258 LLLDLKAELaaymesklkeeadgeGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAaslrSELEKEK--- 334
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 569007259 1284 sQDLD-MKQR------TIQQLKEQLSNQKME-EAVQQYEK 1315
Cdd:pfam05701 335 -AELAsLRQRegmasiAVSSLEAELNRTKSEiALVQAKEK 373
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1076-1359 |
1.46e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.50 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1076 QQLREELQE-KSVSLRVQVQLVAEREQALSELS------QDVTCYKAKIKDLEVI-------VETQKDECKRL------V 1135
Cdd:PRK10929 26 KQITQELEQaKAAKTPAQAEIVEALQSALNWLEerkgslERAKQYQQVIDNFPKLsaelrqqLNNERDEPRSVppnmstD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1136 ELEQSILEKESAILKLEANLKEceakHQDHIRtndlsakevkfreEVTRLANNLhdTKQLLQSKEEENEISRQetekLKE 1215
Cdd:PRK10929 106 ALEQEILQVSSQLLEKSRQAQQ----EQDRAR-------------EISDSLSQL--PQQQTEARRQLNEIERR----LQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1216 ELAANSILTQNLKADLQkkeedcAELKEKfidaKKQIEQVQREVSVMRDEEKLLRIKInELEKKKnqySQDLDMKqrtIQ 1295
Cdd:PRK10929 163 LGTPNTPLAQAQLTALQ------AESAAL----KALVDELELAQLSANNRQELARLRS-ELAKKR---SQQLDAY---LQ 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569007259 1296 QLKEQLSNQKMEEAVQQYEKVckdlsvkEKLVE---DMRLTLVEQEQTQAEQDRVLEAKSEEADWLA 1359
Cdd:PRK10929 226 ALRNQLNSQRQREAERALEST-------ELLAEqsgDLPKSIVAQFKINRELSQALNQQAQRMDLIA 285
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1063-1506 |
1.48e-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: 43.47 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1063 NRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVElEQSIL 1142
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNS-DLSKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1143 EKESAILKLEANLKECE-AKHQDHIRTNDlsAKEVKFREEVTRLANNLhdtkqllqsKEEENEISRQETEKlkeelaans 1221
Cdd:TIGR04523 109 NSEIKNDKEQKNKLEVElNKLEKQKKENK--KNIDKFLTEIKKKEKEL---------EKLNNKYNDLKKQK--------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1222 iltQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMR---DEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLK 1298
Cdd:TIGR04523 169 ---EELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1299 EQLSN--QKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQE-QTQAEQDRVLEAKSE-EADW---LATELDKWKEKFKD 1371
Cdd:TIGR04523 246 TEISNtqTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEkQLNQLKSEISDLNNQkEQDWnkeLKSELKNQEKKLEE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1372 LETRSNQRLNTgtmddLDVLTRKFSKLQDELQESEEKyKADRKKWLEEKavlttqakeaenvrNREMRKYADDRErclKL 1451
Cdd:TIGR04523 326 IQNQISQNNKI-----ISQLNEQISQLKKELTNSESE-NSEKQRELEEK--------------QNEIEKLKKENQ---SY 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 569007259 1452 QNEVETLTAQLAEKNSELQKWREERDQLvtavETQMKALLSSCKHKDEEIQELRK 1506
Cdd:TIGR04523 383 KQEIKNLESQINDLESKIQNQEKLNQQK----DEQIKKLQQEKELLEKEIERLKE 433
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1008-1505 |
1.68e-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: 43.50 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1008 SIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEK-ESLIQQLREELQEks 1086
Cdd:TIGR00606 228 SKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKmEKVFQGTDEQLND-- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1087 vslrvqvqlVAEREQalselsQDVTCYKAKIKDLEVIVETQKDEcKRLVELEQSILEKESAILKLEANlkeceaKHQDHI 1166
Cdd:TIGR00606 306 ---------LYHNHQ------RTVREKERELVDCQRELEKLNKE-RRLLNQEKTELLVEQGRLQLQAD------RHQEHI 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1167 RTNDLSAKEVKFREEVTRLA---------NNLHDTKQLLQSKE-----------EENEISRQET-EKLKEELAANSILTQ 1225
Cdd:TIGR00606 364 RARDSLIQSLATRLELDGFErgpfserqiKNFHTLVIERQEDEaktaaqlcadlQSKERLKQEQaDEIRDEKKGLGRTIE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1226 NLKADLQKKEEDC----AELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQ----DLDMKQRTIQQL 1297
Cdd:TIGR00606 444 LKKEILEKKQEELkfviKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQnekaDLDRKLRKLDQE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1298 KEQLSNQKmeEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQA-------EQDRVLEAKSEEADWLATELDKWKEKFK 1370
Cdd:TIGR00606 524 MEQLNHHT--TTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLgyfpnkkQLEDWLHSKSKEINQTRDRLAKLNKELA 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1371 DLETRSNQRLNtgtmdDLDVLTRKFSKLQDE----------------LQESEEKYKADRKKWLEEKAV-------LTTQA 1427
Cdd:TIGR00606 602 SLEQNKNHINN-----ELESKEEQLSSYEDKlfdvcgsqdeesdlerLKEEIEKSSKQRAMLAGATAVysqfitqLTDEN 676
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569007259 1428 KEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQMKALlsscKHKDEEIQELR 1505
Cdd:TIGR00606 677 QSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSII----DLKEKEIPELR 750
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1045-1437 |
1.74e-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: 43.02 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1045 KGYREENSDLRAQESQGKNRDHQL--KEKESLIQQLREELQEKSvslrvQVQLVAEREQALSELSQDVTCYKAKIKDLEV 1122
Cdd:COG5185 128 SEIVALKDELIKVEKLDEIADIEAsyGEVETGIIKDIFGKLTQE-----LNQNLKKLEIFGLTLGLLKGISELKKAEPSG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1123 IVETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVKFREEVTRL-ANNLHDTKQLLQSKEE 1201
Cdd:COG5185 203 TVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLrLEKLGENAESSKRLNE 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1202 ENEISRQETEKLKEELAANSILTQNLKADLQKKEED-CAELKEKFIDAKKQIEQ-VQREVSVMRDEEKLLRIKINELEKK 1279
Cdd:COG5185 283 NANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLaAAEAEQELEESKRETETgIQNLTAEIEQGQESLTENLEAIKEE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1280 KNQ--YSQDLDMKQRTIQQLKEQLSNQK--MEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQ-DRVLEAKSEE 1354
Cdd:COG5185 363 IENivGEVELSKSSEELDSFKDTIESTKesLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQaTSSNEEVSKL 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1355 ADWLATELDKWKEKFKDLETR----SNQRLNTGTMDDLDVLTRKFSKLQD---ELQESEEKYKADRKKWLEEKAVLTTQA 1427
Cdd:COG5185 443 LNELISELNKVMREADEESQSrleeAYDEINRSVRSKKEDLNEELTQIESrvsTLKATLEKLRAKLERQLEGVRSKLDQV 522
|
410
....*....|
gi 569007259 1428 KEAENVRNRE 1437
Cdd:COG5185 523 AESLKDFMRA 532
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1197-1475 |
2.11e-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: 42.57 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1197 QSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINEL 1276
Cdd:pfam07888 55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1277 EKKKNQYSQDLDMKQRTIQQLKE---QLSNQKMEE---------AVQQYEKVCKDLSvkeKLVEDMRLTLVEQE-QTQAE 1343
Cdd:pfam07888 135 EEDIKTLTQRVLERETELERMKErakKAGAQRKEEeaerkqlqaKLQQTEEELRSLS---KEFQELRNSLAQRDtQVLQL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1344 QDRV--LEAKSEEADWLATELDKWKEKFKDLETR--SNQRLNTGTMDDLDVLTRKFSKLQDELQESE-------EKYKAD 1412
Cdd:pfam07888 212 QDTIttLTQKLTTAHRKEAENEALLEELRSLQERlnASERKVEGLGEELSSMAAQRDRTQAELHQARlqaaqltLQLADA 291
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569007259 1413 RKKWLEEKAvltTQAKEAENV-RNREMrkyadDRERCLKLQNEVETLTAQLAEKNSELQKWREE 1475
Cdd:pfam07888 292 SLALREGRA---RWAQERETLqQSAEA-----DKDRIEKLSAELQRLEERLQEERMEREKLEVE 347
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
703-930 |
2.27e-03 |
|
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: 42.44 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 703 DPQEAIACLQLKFNQVKAELAETKEELIKAQEELKNREsNSLVQALKTSSKVDTSLTSNKSTCNETSEMPKNSRAQTHSE 782
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE-RRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 783 RKRLNE--DGLQ-LGEPPAKKglILVSPPITEEQNKMGEMQQSVsevvegNRVLKEKNEELKRLLTIGENELRNEKEEKA 859
Cdd:COG4942 103 KEELAEllRALYrLGRQPPLA--LLLSPEDFLDAVRRLQYLKYL------APARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569007259 860 ELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIES 930
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
845-1224 |
2.30e-03 |
|
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: 42.80 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 845 TIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQiQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETA 924
Cdd:pfam17380 264 TMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEE-KAREVERRRKLEEAEKARQAEMDRQAAIYAEQERM 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 925 ARSIESNVSQIKQMQTK--IDELRSLDSPSHISKIDLLNLQDLSSGAKGDnclNTSQQLPGGdfsstwvKEYHTQEISRE 1002
Cdd:pfam17380 343 AMERERELERIRQEERKreLERIRQEEIAMEISRMRELERLQMERQQKNE---RVRQELEAA-------RKVKILEEERQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1003 NSFHASIEAIWEECKEIVKAsskKSHQIQGLEE----QIEKLQVEVKGYREENSDLRAQESQGKnRDHQLKEKESLIQQL 1078
Cdd:pfam17380 413 RKIQQQKVEMEQIRAEQEEA---RQREVRRLEEerarEMERVRLEEQERQQQVERLRQQEEERK-RKKLELEKEKRDRKR 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1079 REELQEKSVslrvqvqlvaerEQALSELSQDVTCYKAKIKDLEvivetqkdecKRLVELEQSILEKESAILKLEANLKEC 1158
Cdd:pfam17380 489 AEEQRRKIL------------EKELEERKQAMIEEERKRKLLE----------KEMEERQKAIYEEERRREAEEERRKQQ 546
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569007259 1159 EAKHQDHIRTNDLSAKEVKFReevtrlannlhdtkqlLQSKEEENEISRQ--ETEKLKEELAANSILT 1224
Cdd:pfam17380 547 EMEERRRIQEQMRKATEERSR----------------LEAMEREREMMRQivESEKARAEYEATTPIT 598
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1197-1356 |
2.49e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1197 QSKEEENEISRQETEKLKEELaansiltQNLKADLQKkeedcaELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINEL 1276
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEI-------HKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLELLEKREEEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1277 EKKKNQYSQ---DLDMKQRTIQQLK-------EQLSNQKMEEAVQQYEKvckdlSVKEKLVEDMRLTLVEQEQtqaeqdr 1346
Cdd:PRK12704 113 EKKEKELEQkqqELEKKEEELEELIeeqlqelERISGLTAEEAKEILLE-----KVEEEARHEAAVLIKEIEE------- 180
|
170
....*....|
gi 569007259 1347 vlEAKsEEAD 1356
Cdd:PRK12704 181 --EAK-EEAD 187
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
521-1402 |
2.67e-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: 42.73 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 521 ENSLEDVLENEDLVEDLEeNEETQNMETELTDEDSDKSLEECRVSTCHKKNKELLDLIEKLNKRLINENKEKLTLELKI- 599
Cdd:TIGR00606 251 KNRLKEIEHNLSKIMKLD-NEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELe 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 600 -----REEVTQEFTQYWSQREADFKETLLHEREILEENAERrlaifkdLVGKCDSQDEPTNRICDIELETEEAHNYV--G 672
Cdd:TIGR00606 330 klnkeRRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLI-------QSLATRLELDGFERGPFSERQIKNFHTLVieR 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 673 VEDIFHSLQDDVTDIKKQAELAhlyitslvdpQEAIACLQLKFNQVKAELAETKEELIKAQEELKN--RESNSLVQALKT 750
Cdd:TIGR00606 403 QEDEAKTAAQLCADLQSKERLK----------QEQADEIRDEKKGLGRTIELKKEILEKKQEELKFviKELQQLEGSSDR 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 751 SSKVDTSLTSNKStcnETSEMPKNSRAQTHSERkrlnedglqlgeppakkglilvsppITEEQNKMGEMQQSVSEVVEGN 830
Cdd:TIGR00606 473 ILELDQELRKAER---ELSKAEKNSLTETLKKE-------------------------VKSLQNEKADLDRKLRKLDQEM 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 831 RVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKnsslradvEQIQASYNSAVAELqtqkavnQEQ 910
Cdd:TIGR00606 525 EQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNK--------KQLEDWLHSKSKEI-------NQT 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 911 RDRILKLSQEMEtaarSIESNVSQI-KQMQTKIDELRSLDSpshiSKIDLLNLQDLSS--GAKGDNCLNTSQQLPGGDFS 987
Cdd:TIGR00606 590 RDRLAKLNKELA----SLEQNKNHInNELESKEEQLSSYED----KLFDVCGSQDEESdlERLKEEIEKSSKQRAMLAGA 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 988 STWVKEYHTQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGyREENSDLRAQESQGKNRDHQ 1067
Cdd:TIGR00606 662 TAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKK-KEKRRDEMLGLAPGRQSIID 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1068 LKEKEslIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESA 1147
Cdd:TIGR00606 741 LKEKE--IPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGS 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1148 ILKLEANLKECEAKHQDHIRTNDLSAKEV--KFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQ 1225
Cdd:TIGR00606 819 DLDRTVQQVNQEKQEKQHELDTVVSKIELnrKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQ 898
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1226 NLKADL-QKKEEDC--AELKEKFIDAKKQIeqvqreVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLS 1302
Cdd:TIGR00606 899 SLIREIkDAKEQDSplETFLEKDQQEKEEL------ISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYL 972
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1303 NQKMEEAVQQYEKVCKDLSVKEKLVEDMRlTLVEQEQTQAEQDRVLEAKseeadwlaTELDKWKEKFKDLETRSNQRLNT 1382
Cdd:TIGR00606 973 KQKETELNTVNAQLEECEKHQEKINEDMR-LMRQDIDTQKIQERWLQDN--------LTLRKRENELKEVEEELKQHLKE 1043
|
890 900
....*....|....*....|
gi 569007259 1383 GTMDDLDVLTRKFSKLQDEL 1402
Cdd:TIGR00606 1044 MGQMQVLQMKQEHQKLEENI 1063
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1024-1408 |
3.15e-03 |
|
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: 42.42 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1024 SKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQ----------LREELQEKSVSLRVQV 1093
Cdd:pfam05557 128 QSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSqeqdseivknSKSELARIPELEKELE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1094 QLVAEREQaLSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEqsiLEKEsailKLEANLKECEAKHQDHIRT----N 1169
Cdd:pfam05557 208 RLREHNKH-LNENIENKLLLKEEVEDLKRKLEREEKYREEAATLE---LEKE----KLEQELQSWVKLAQDTGLNlrspE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1170 DLSAK-------EVKFREEVTRLAN---NLHDTKQLLQ-------SKEEENEISRQETEKLKEELA-ANSILTQN---LK 1228
Cdd:pfam05557 280 DLSRRieqlqqrEIVLKEENSSLTSsarQLEKARRELEqelaqylKKIEDLNKKLKRHKALVRRLQrRVLLLTKErdgYR 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1229 ADLQKKEEDCAElKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEE 1308
Cdd:pfam05557 360 AILESYDKELTM-SNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSY 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1309 AVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQD----------RVL-----------EAKSEEADWLATELDKWKE 1367
Cdd:pfam05557 439 SKEEVDSLRRKLETLELERQRLREQKNELEMELERRClqgdydpkktKVLhlsmnpaaeayQQRKNQLEKLQAEIERLKR 518
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 569007259 1368 KFKDLETrSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEK 1408
Cdd:pfam05557 519 LLKKLED-DLEQVLRLPETTSTMNFKEVLDLRKELESAELK 558
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
855-1500 |
3.41e-03 |
|
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: 42.35 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 855 KEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKlSQEMETAARSIESNVSQ 934
Cdd:TIGR01612 1103 KEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAIS-NDDPEEIEKKIENIVTK 1181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 935 IKQMQTKIDELRSLdsPSHISKIDllnlQDLSSGAKGDNcLNTSQqlpGGDFSSTWVKEYHTQEISRENSFHaSIEAIWE 1014
Cdd:TIGR01612 1182 IDKKKNIYDEIKKL--LNEIAEIE----KDKTSLEEVKG-INLSY---GKNLGKLFLEKIDEEKKKSEHMIK-AMEAYIE 1250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1015 ECKEIvKASSKKSHQIQGLEEQIEKlqvEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQ 1094
Cdd:TIGR01612 1251 DLDEI-KEKSPEIENEMGIEMDIKA---EMETFNISHDDDKDHHIISKKHDENISDIREKSLKIIEDFSEESDINDIKKE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1095 L---VAEREQALSE----LSQDVTCYKA-KIKDLEVIVETQKDECKRLVELEQSI---LEKESAILKL---EANLKECEA 1160
Cdd:TIGR01612 1327 LqknLLDAQKHNSDinlyLNEIANIYNIlKLNKIKKIIDEVKEYTKEIEENNKNIkdeLDKSEKLIKKikdDINLEECKS 1406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1161 KHQDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEEN----------EISRQETE---KLKEELAANSI----- 1222
Cdd:TIGR01612 1407 KIESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNenvlllfkniEMADNKSQhilKIKKDNATNDHdfnin 1486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1223 -LTQNLkaDLQKKEEDCAELKEKFIDAKKQI-EQVQREVSVMRDEEKLLRIKiNELEKKKNQYSQdldmkqrTIQQLKEq 1300
Cdd:TIGR01612 1487 eLKEHI--DKSKGCKDEADKNAKAIEKNKELfEQYKKDVTELLNKYSALAIK-NKFAKTKKDSEI-------IIKEIKD- 1555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1301 LSNQKMEEAVQQYEKVCKdlsvkeklvedmrltlVEQEQTQAEQDRVLEAKSEEADW-LATELDKWKEKF---KDLETRS 1376
Cdd:TIGR01612 1556 AHKKFILEAEKSEQKIKE----------------IKKEKFRIEDDAAKNDKSNKAAIdIQLSLENFENKFlkiSDIKKKI 1619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1377 NQRLNtgtmdDLDVLTRKFSKLQDELQESEEKYKADRKKWLEE--------KAVLTTQAKEAENVrNREMRKYADDRERC 1448
Cdd:TIGR01612 1620 NDCLK-----ETESIEKKISSFSIDSQDTELKENGDNLNSLQEfleslkdqKKNIEDKKKELDEL-DSEIEKIEIDVDQH 1693
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 569007259 1449 LKlqneveTLTAQLAEKNSELQKW-REERDQLVTAVETQMKALLSSCKHKDEE 1500
Cdd:TIGR01612 1694 KK------NYEIGIIEKIKEIAIAnKEEIESIKELIEPTIENLISSFNTNDLE 1740
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1217-1387 |
3.60e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1217 LAANSILTQNLKADLQKKEEDCAELKEKFIDAKKqiEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQ 1296
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAK--ELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1297 LKEQLSnqKMEEAVQQYEkvcKDLSVKEKLVED--MRLTLVEQEQTQAEQDRVLEAKSEEAdwLATELDKWKEKFKDLET 1374
Cdd:PRK12705 103 LENQLE--EREKALSARE---LELEELEKQLDNelYRVAGLTPEQARKLLLKLLDAELEEE--KAQRVKKIEEEADLEAE 175
|
170
....*....|...
gi 569007259 1375 RSNQRLNTGTMDD 1387
Cdd:PRK12705 176 RKAQNILAQAMQR 188
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
582-1123 |
3.62e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 582 NKRLINENKEKLTLELKIREEVTQEFTQywSQREADFKETLLHEREILEENAERRLAIFKDLVGKCDSQDEPTNRICDIE 661
Cdd:PRK01156 202 IKKQIADDEKSHSITLKEIERLSIEYNN--AMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 662 LETEEAHN---YVGVEDI--FHSLQDDVTDIKKQAELAHLYITSLVDPQEAIACLQLKFNQVKaELAETKEELIKAQEEL 736
Cdd:PRK01156 280 ERHMKIINdpvYKNRNYIndYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYI-KKKSRYDDLNNQILEL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 737 KNRESN--SLVQALKT-SSKVDTSLTSNKSTCNETSEMPKNSRAQTHSERKRLNEDGLQLGEppakkglilVSPPITEEQ 813
Cdd:PRK01156 359 EGYEMDynSYLKSIESlKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQD---------ISSKVSSLN 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 814 NKMGEMQQSVSEVVEG----------------------NRVLKEKNEELKRLltigENELRNEKEEKAELNKQVVSLQQQ 871
Cdd:PRK01156 430 QRIRALRENLDELSRNmemlngqsvcpvcgttlgeeksNHIINHYNEKKSRL----EEKIREIEIEVKDIDEKIVDLKKR 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 872 LRFFEEKnsslraDVEQIQASYN---SAVAELQTQKAVNQEQRDRILKLsqemetaarsiESNVSQIKQMQTKIDELRSL 948
Cdd:PRK01156 506 KEYLESE------EINKSINEYNkieSARADLEDIKIKINELKDKHDKY-----------EEIKNRYKSLKLEDLDSKRT 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 949 DSPSHISKIDLLNLQDLSSGAKgdnclNTSQQLPGGdfsstwvkEYHTQEISRE-NSFHASIEAIWEECKEIVKASSKKS 1027
Cdd:PRK01156 569 SWLNALAVISLIDIETNRSRSN-----EIKKQLNDL--------ESRLQEIEIGfPDDKSYIDKSIREIENEANNLNNKY 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1028 HQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELS 1107
Cdd:PRK01156 636 NEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELS 715
|
570
....*....|....*.
gi 569007259 1108 QDVTCYKAKIKDLEVI 1123
Cdd:PRK01156 716 DRINDINETLESMKKI 731
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
115-183 |
3.98e-03 |
|
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: 40.02 E-value: 3.98e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569007259 115 FSKVFGPETSQKEFFLGC--IMQPVKDLLEGHSrlIFTYGLTNSGKTYTFQgteeniGILPRTLNVLFDSL 183
Cdd:cd01363 22 FYRGFRRSESQPHVFAIAdpAYQSMLDGYNNQS--IFAYGESGAGKTETMK------GVIPYLASVAFNGI 84
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1024-1314 |
4.17e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1024 SKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNrdhQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQAL 1103
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEE---ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1104 SELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVKFREEVT 1183
Cdd:COG4372 104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1184 RLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMR 1263
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 569007259 1264 DEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYE 1314
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
1215-1313 |
4.26e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 39.82 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1215 EELAANSILTQNLKADLQKKEEDC-AELKEKFIDAKKQIEQVQREVSVMRDEEKllRIKINELEKKKNQYSQDLDMKQRT 1293
Cdd:COG2825 32 QRILQESPEGKAAQKKLEKEFKKRqAELQKLEKELQALQEKLQKEAATLSEEER--QKKERELQKKQQELQRKQQEAQQD 109
|
90 100
....*....|....*....|...
gi 569007259 1294 IQQLKEQLSNQ---KMEEAVQQY 1313
Cdd:COG2825 110 LQKRQQELLQPileKIQKAIKEV 132
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1072-1302 |
4.56e-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: 41.80 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1072 ESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKL 1151
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1152 EANLKEceakhqdhiRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADL 1231
Cdd:pfam07888 110 SEELSE---------EKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1232 QKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKIN-------ELEKKKNQYS---QDLDMKQRTIQQLKEQL 1301
Cdd:pfam07888 181 QQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTtahrkeaENEALLEELRslqERLNASERKVEGLGEEL 260
|
.
gi 569007259 1302 S 1302
Cdd:pfam07888 261 S 261
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1300-1470 |
4.64e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 41.97 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1300 QLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSnqr 1379
Cdd:pfam05911 684 KRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQLKCMAESYEDLETRL--- 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1380 lnTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLttqakeaENVRNREMRKYADDRERcLKLQNEVETLT 1459
Cdd:pfam05911 761 --TELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQL-------ERNEKKESSNCDADQED-KKLQQEKEITA 830
|
170
....*....|.
gi 569007259 1460 AqlAEKNSELQ 1470
Cdd:pfam05911 831 A--SEKLAECQ 839
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1224-1316 |
5.29e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 40.27 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1224 TQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQD-LDMKQRT--IQQLKEQ 1300
Cdd:pfam13851 21 TRNNLELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDkQSLKNLKarLKVLEKE 100
|
90
....*....|....*...
gi 569007259 1301 LSNQKMEEAV--QQYEKV 1316
Cdd:pfam13851 101 LKDLKWEHEVleQRFEKV 118
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1033-1349 |
5.42e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1033 LEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVaEREQALSELSqDVTc 1112
Cdd:PRK04863 360 LEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQAL-ERAKQLCGLP-DLT- 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1113 ykakIKDLEVIVETQKDECKRLVEleqsilekesAILKLEANLKECEAKHQDHIRTNDLSAKEV----------KFREEV 1182
Cdd:PRK04863 437 ----ADNAEDWLEEFQAKEQEATE----------ELLSLEQKLSVAQAAHSQFEQAYQLVRKIAgevsrseawdVARELL 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1183 TRLANNLHDTKQLLQSKEEENEISR-----QETEKLKEELAANSILTQNLKADLQKKEEdcaELKEKFIDAKKQIEQVQR 1257
Cdd:PRK04863 503 RRLREQRHLAEQLQQLRMRLSELEQrlrqqQRAERLLAEFCKRLGKNLDDEDELEQLQE---ELEARLESLSESVSEARE 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1258 EVSVMRDEEKLLRIKINELEKKKNQYSQdldmKQRTIQQLKEQ-----LSNQKMEEAVQQyekvckdlsvkekLVEDMRL 1332
Cdd:PRK04863 580 RRMALRQQLEQLQARIQRLAARAPAWLA----AQDALARLREQsgeefEDSQDVTEYMQQ-------------LLERERE 642
|
330
....*....|....*..
gi 569007259 1333 TLVEQEQTQAEQDRVLE 1349
Cdd:PRK04863 643 LTVERDELAARKQALDE 659
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1173-1300 |
5.52e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1173 AKEV--KFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDcaELKEKFIDAKK 1250
Cdd:PRK00409 507 AKKLigEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK--EAQQAIKEAKK 584
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 569007259 1251 QIEQVQREVSVMRDEEKlLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQ 1300
Cdd:PRK00409 585 EADEIIKELRQLQKGGY-ASVKAHELIEARKRLNKANEKKEKKKKKQKEK 633
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1344-1517 |
6.37e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1344 QDRVLEAKSEEA----DWLATELDKWKEKFKDLETRSNQ-RLNTGTMD---DLDVLTRKFSKLQDELQESEEKYKADRKK 1415
Cdd:COG3206 162 LEQNLELRREEArkalEFLEEQLPELRKELEEAEAALEEfRQKNGLVDlseEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1416 WLEEKAVLTTQAKEAENVRNREMrkYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQMKALLSSCK 1495
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPV--IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLE 319
|
170 180 190
....*....|....*....|....*....|...
gi 569007259 1496 HK-----------DEEIQELRKAAAKSTGTENQ 1517
Cdd:COG3206 320 AElealqareaslQAQLAQLEARLAELPELEAE 352
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1185-1315 |
7.03e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.89 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1185 LANNLHDTKQLlqsKEEENEISRQET--EKLKEELAANSiltQNLKADLQKKEEDCAEL----------KEKFIDAKKQI 1252
Cdd:pfam13851 21 TRNNLELIKSL---KEEIAELKKKEErnEKLMSEIQQEN---KRLTEPLQKAQEEVEELrkqlenyekdKQSLKNLKARL 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569007259 1253 EQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQ---LKEQLSNQKMEEAVQQYEK 1315
Cdd:pfam13851 95 KVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQktgLKNLLLEKKLQALGETLEK 160
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1021-1304 |
7.99e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1021 KASSKKSHQ-----------IQGLEEQIEKLQVEVKGYREENS--DLRAQESQGKNrdhQLKEKESLIQQLREELQEKSV 1087
Cdd:PRK10929 61 KGSLERAKQyqqvidnfpklSAELRQQLNNERDEPRSVPPNMStdALEQEILQVSS---QLLEKSRQAQQEQDRAREISD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1088 SLRVQVQLVAEREQALSELSQDvtcykakikdleviVETQKDECKRLVELEQSILEKESAILKLEANLKECEakhqdhir 1167
Cdd:PRK10929 138 SLSQLPQQQTEARRQLNEIERR--------------LQTLGTPNTPLAQAQLTALQAESAALKALVDELELA-------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1168 tnDLSAKEvkfREEVTRLANNLHDTK--------QLLQS-----KEEENEISRQETEKLKEELA--ANSILTQ-----NL 1227
Cdd:PRK10929 196 --QLSANN---RQELARLRSELAKKRsqqldaylQALRNqlnsqRQREAERALESTELLAEQSGdlPKSIVAQfkinrEL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1228 KADL--QKKEEDCAELKEKfiDAKKQIEQVQREVSVMRDEEK----------LLRIKINEL-EKKKNQySQDLDMKQRTI 1294
Cdd:PRK10929 271 SQALnqQAQRMDLIASQQR--QAASQTLQVRQALNTLREQSQwlgvsnalgeALRAQVARLpEMPKPQ-QLDTEMAQLRV 347
|
330
....*....|.
gi 569007259 1295 QQLK-EQLSNQ 1304
Cdd:PRK10929 348 QRLRyEDLLNK 358
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
833-946 |
8.63e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 833 LKEKNEELKRLltigENELRNEKEEKAELNKQVVSLQQQLR--------FFEEKN--------SSLRADVEQIQASyNSA 896
Cdd:COG4913 612 LAALEAELAEL----EEELAEAEERLEALEAELDALQERREalqrlaeySWDEIDvasaereiAELEAELERLDAS-SDD 686
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 569007259 897 VAELQTQKAVNQEQRDRilkLSQEMETAARSIESNVSQIKQMQTKIDELR 946
Cdd:COG4913 687 LAALEEQLEELEAELEE---LEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
811-947 |
8.83e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 811 EEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLltigENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQ 890
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKELPAELAEL----EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569007259 891 AS---------YNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRS 947
Cdd:COG1579 80 EQlgnvrnnkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1034-1369 |
8.92e-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: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1034 EEQIEKLQVEVKGYREENSDLrAQESQGKNrDH--------QLKEKeslIQQLREELQEKSVSLRVQVQLVAEREQALSE 1105
Cdd:COG3096 305 QYRLVEMARELEELSARESDL-EQDYQAAS-DHlnlvqtalRQQEK---IERYQEDLEELTERLEEQEEVVEEAAEQLAE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1106 L-------SQDVTCYKAKIKDLEVIVETQKdecKRLVELEQSI--LEKESAILKLE----ANLKECEAKHQDHI------ 1166
Cdd:COG3096 380 AearleaaEEEVDSLKSQLADYQQALDVQQ---TRAIQYQQAVqaLEKARALCGLPdltpENAEDYLAAFRAKEqqatee 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1167 ------RTNDLSAKEVKFRE----------EVTR-------------------LANNLHDTKQLLqSKEEENEISRQETE 1211
Cdd:COG3096 457 vleleqKLSVADAARRQFEKayelvckiagEVERsqawqtarellrryrsqqaLAQRLQQLRAQL-AELEQRLRQQQNAE 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1212 KLKEELAANSILTQNLKADLqkkEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQ 1291
Cdd:COG3096 536 RLLEEFCQRIGQQLDAAEEL---EELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALE 612
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569007259 1292 RTIQQLKEQLSN-QKMEEAVQQyekvckdLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADwlaTELDKWKEKF 1369
Cdd:COG3096 613 RLREQSGEALADsQEVTAAMQQ-------LLEREREATVERDELAARKQALESQIERLSQPGGAED---PRLLALAERL 681
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
612-945 |
9.13e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 612 SQREADFKETLLHEREILEENAERrlaIFKDLVGKCDSQDEPTNRICDIELETEEahnyvgvedifhsLQDDVTDIKKQA 691
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRR---IENRLDELSQELSDASRKIGEIEKEIEQ-------------LEQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 692 ELAHLYITSLVDPQEAIACLQLKFNQVKAELAETKEELIKAQEELKNRESNSLVQAL-KTSSKVDTSLTSNKSTCNETse 770
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIqAELSKLEEEVSRIEARLREI-- 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 771 mpkNSRAQTHSERKRLNEDGLQlgeppakkglilvsppitEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENE 850
Cdd:TIGR02169 818 ---EQKLNRLTLEKEYLEKEIQ------------------ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 851 LRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIqasyNSAVAELQTQKAVNQEQRDRILKLSQEMEtaarSIES 930
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK----RKRLSELKAKLEALEEELSEIEDPKGEDE----EIPE 948
|
330
....*....|....*
gi 569007259 931 NVSQIKQMQTKIDEL 945
Cdd:TIGR02169 949 EELSLEDVQAELQRV 963
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
854-1312 |
9.84e-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: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 854 EKEEKA-ELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASynsavaelqtqkavnqeqRDRILKLSQEMETAARSIEsnv 932
Cdd:pfam01576 633 EKETRAlSLARALEEALEAKEELERTNKQLRAEMEDLVSS------------------KDDVGKNVHELERSKRALE--- 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 933 SQIKQMQTKIDELRSLDSPSHISKIDL-LNLQDLSsgAKGDNCLNTSQQLpGGDFSSTWVKEYHTQEISRENSFHASIEA 1011
Cdd:pfam01576 692 QQVEEMKTQLEELEDELQATEDAKLRLeVNMQALK--AQFERDLQARDEQ-GEEKRRQLVKQVRELEAELEDERKQRAQA 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1012 IWEECK---EIVKASSKKSHQIQGLEE---QIEKLQVEVKGYREENSDLRAQE----SQGKNRDHQLKEKESLIQQLREE 1081
Cdd:pfam01576 769 VAAKKKlelDLKELEAQIDAANKGREEavkQLKKLQAQMKDLQRELEEARASRdeilAQSKESEKKLKNLEAELLQLQED 848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1082 LqekSVSLRVQVQLVAEREQALSELSQDVTCYKAkikdlevivetQKDECKRLveleqsilekESAILKLEANLKEceak 1161
Cdd:pfam01576 849 L---AASERARRQAQQERDELADEIASGASGKSA-----------LQDEKRRL----------EARIAQLEEELEE---- 900
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007259 1162 hqDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSkeeeNEISRQETEKLKEELAAN-SILTQNLKAdlqKKEEDCAE 1240
Cdd:pfam01576 901 --EQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQK----SESARQQLERQNKELKAKlQEMEGTVKS---KFKSSIAA 971
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569007259 1241 LKEKFIDAKKQIEQVQREVS-----VMRDEEKL--LRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLsnQKMEEAVQQ 1312
Cdd:pfam01576 972 LEAKIAQLEEQLEQESRERQaanklVRRTEKKLkeVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQL--EEAEEEASR 1048
|
|
| |
