|
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 |
7.42e-160 |
|
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: 489.98 E-value: 7.42e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 58 YLQVCLRIRPFTQSEKEHEAEGCVQVLDSQSVLLKDPQSILGHLSEKSSGQVAQKFSFSKVFGPETSQKEFFLGCIMQPV 137
Cdd:cd01368 2 PVKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHPPKGSAANKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTALPLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 138 KDLLEGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmsfkphrcreylklssdqekeesankn 217
Cdd:cd01368 82 QDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG-------------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 218 tllrqikevtihndsydvlcghltnsltipefeesvnscdqsslnvdnikYSVWVSFFEIYNESIYDLFVPV-SSKFQKR 296
Cdd:cd01368 130 --------------------------------------------------YSVFVSYIEIYNEYIYDLLEPSpSSPTKKR 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 297 KMLRLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEI------PRVT 370
Cdd:cd01368 160 QSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDgdvdqdKDQI 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 371 RVSELSLCDLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLKNSEKSK-VQHVPFRESKLTHYFQSFFTGKGKIC 449
Cdd:cd01368 240 TVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGtNKMVPFRDSKLTHLFQNYFDGEGKAS 319
|
410 420
....*....|....*....|....*.
gi 1907132433 450 MIINISQSCSAYDETLNVLKFSTTAQ 475
Cdd:cd01368 320 MIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
64-477 |
8.38e-94 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 306.81 E-value: 8.38e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 64 RIRPFTQSEKEHEAEGCVQVLDsqsvllkdPQSILGHLSEKSSGQVAQKFSFSKVFGPETSQKEFFLGCIMQPVKDLLEG 143
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVES--------VDSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 144 HSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERLytkmsfkphrcreylklssdqekeesankntllrqi 223
Cdd:pfam00225 73 YNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK------------------------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 224 kevtihndsydvlcghltnsltipefeesvnscdqsslnvDNIKYSVWVSFFEIYNESIYDLFVPVSSKFQKrkmLRLSQ 303
Cdd:pfam00225 117 ----------------------------------------ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRK---LRIRE 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 304 DIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQ-IEDSEIPRVTRVSELSLCDLAG 382
Cdd:pfam00225 154 DPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQrNRSTGGEESVKTGKLNLVDLAG 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 383 SERSMKTQN-EGERLREAGNINTSLLTLGKCINVLknSEKSKvQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAY 461
Cdd:pfam00225 234 SERASKTGAaGGQRLKEAANINKSLSALGNVISAL--ADKKS-KHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNY 310
|
410
....*....|....*.
gi 1907132433 462 DETLNVLKFSTTAQRV 477
Cdd:pfam00225 311 EETLSTLRFASRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
60-475 |
5.93e-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: 301.80 E-value: 5.93e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 60 QVCLRIRPFTQSEKEHEAEGCVQVLDSQSVllkdpQSILGHLSEKssgQVAQKFSFSKVFGPETSQKEFFLGCIMQPVKD 139
Cdd:smart00129 3 RVVVRVRPLNKREKSRKSPSVVPFPDKVGK-----TLTVRSPKNR---QGEKKFTFDKVFDATASQEDVFEETAAPLVDS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 140 LLEGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERlytkmsfkphrcreylklssdqekeesankntl 219
Cdd:smart00129 75 VLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKR--------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 220 lrqikevtihndsydvlcghltnsltipefeesvnscdqsslnVDNIKYSVWVSFFEIYNESIYDLFVPVSSKfqkrkmL 299
Cdd:smart00129 122 -------------------------------------------EEGWQFSVKVSYLEIYNEKIRDLLNPSSKK------L 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 300 RLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRVTRVSELSLCD 379
Cdd:smart00129 153 EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKASKLNLVD 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 380 LAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLknSEKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCS 459
Cdd:smart00129 233 LAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINAL--AQHSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSS 310
|
410
....*....|....*.
gi 1907132433 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 |
1.20e-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: 289.16 E-value: 1.20e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 60 QVCLRIRPFTQSEKEhEAEGCVQVLDSQSVLLKDPqsilghlseKSSGQVAQKFSFSKVFGPETSQKEFFLGCIMQPVKD 139
Cdd:cd00106 3 RVAVRVRPLNGREAR-SAKSVISVDGGKSVVLDPP---------KNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 140 LLEGHSRLIFTYGLTNSGKTYTFQGT-EENIGILPRTLNVLFDSLQERLYTKMSfkphrcreylklssdqekeesanknt 218
Cdd:cd00106 73 ALEGYNGTIFAYGQTGSGKTYTMLGPdPEQRGIIPRALEDIFERIDKRKETKSS-------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 219 llrqikevtihndsydvlcghltnsltipefeesvnscdqsslnvdnikYSVWVSFFEIYNESIYDLFVPVsskfqKRKM 298
Cdd:cd00106 127 -------------------------------------------------FSVSASYLEIYNEKIYDLLSPV-----PKKP 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 299 LRLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRVTRVSELSLC 378
Cdd:cd00106 153 LSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGESVTSSKLNLV 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 379 DLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLknSEKSKVqHVPFRESKLTHYFQSFFTGKGKICMIINISQSC 458
Cdd:cd00106 233 DLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISAL--ADGQNK-HIPYRDSKLTRLLQDSLGGNSKTIMIACISPSS 309
|
410
....*....|....*..
gi 1907132433 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 |
1.10e-67 |
|
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: 1.10e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 64 RIRPFTQSEKEHEAeGCVQVLDSqsvllkDPQSIlgHLSEKSSGQvaQKFSFSKVFGPETSQKEFFlGCIMQPVKDLLEG 143
Cdd:cd01366 9 RVRPLLPSEENEDT-SHITFPDE------DGQTI--ELTSIGAKQ--KEFSFDKVFDPEASQEDVF-EEVSPLVQSALDG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 144 HSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERlytkmsfkphrcreylklssdqekeesankntllrqi 223
Cdd:cd01366 77 YNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKEL------------------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 224 KEVTIhndsydvlcghltnsltipefeesvnscdqsslnvdniKYSVWVSFFEIYNESIYDLfvpVSSKFQKRKMLRLSQ 303
Cdd:cd01366 120 KEKGW--------------------------------------SYTIKASMLEIYNETIRDL---LAPGNAPQKKLEIRH 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 304 D-IKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRIlQIEDSEIPRVTRvSELSLCDLAG 382
Cdd:cd01366 159 DsEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI-SGRNLQTGEISV-GKLNLVDLAG 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 383 SERSMKTQNEGERLREAGNINTSLLTLGKCINVLKNseksKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYD 462
Cdd:cd01366 237 SERLNKSGATGDRLKETQAINKSLSALGDVISALRQ----KQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLN 312
|
410
....*....|....*
gi 1907132433 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 |
6.30e-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: 6.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 59 LQVCLRIRPFTQSEKEHEAEGCVQVLDSQSVLLKDPQSILGHLSEKSSGQVAQ-------KFSFSKVFGPETSQKEFFLG 131
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFDPKDEEDGFFHGGSNNRDRRkrrnkelKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 132 CIMQPVKDLLEGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmsfkphrcreylkLSSDQEke 211
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIES------------------LKDEKE-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 212 esankntllrqikevtihndsydvlcghltnsltipefeesvnscdqsslnvdnikYSVWVSFFEIYNESIYDLFVPVSs 291
Cdd:cd01370 142 --------------------------------------------------------FEVSMSYLEIYNETIRDLLNPSS- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 292 kfqkrKMLRLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIE-DSEIPRVT 370
Cdd:cd01370 165 -----GPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDkTASINQQV 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 371 RVSELSLCDLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLKNSeKSKVQHVPFRESKLTHYFQSFFTGKGKICM 450
Cdd:cd01370 240 RQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADP-GKKNKHIPYRDSKLTRLLKDSLGGNCRTVM 318
|
410 420
....*....|....*....|....
gi 1907132433 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 |
5.85e-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: 5.85e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 60 QVCLRIRPFTQSEKEHEAEGCVQVLDSQsvllkdPQSILGHlsekssgqvAQKFSFSKVFGPETSQKEFFLGCIMQPVKD 139
Cdd:cd01372 4 RVAVRVRPLLPKEIIEGCRICVSFVPGE------PQVTVGT---------DKSFTFDYVFDPSTEQEEVYNTCVAPLVDG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 140 LLEGHSRLIFTYGLTNSGKTYTFQGT------EENIGILPRTLNVLFDSLQERlytkmsfkphrcreylklssdqekees 213
Cdd:cd01372 69 LFEGYNATVLAYGQTGSGKTYTMGTAytaeedEEQVGIIPRAIQHIFKKIEKK--------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 214 ankntllrqikevtihndsydvlcghltnsltipefeesvnscdqsslnVDNIKYSVWVSFFEIYNESIYDLFvpvSSKF 293
Cdd:cd01372 122 -------------------------------------------------KDTFEFQLKVSFLEIYNEEIRDLL---DPET 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 294 QKRKMLRLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQ-IEDSEIPR---- 368
Cdd:cd01372 150 DKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQtKKNGPIAPmsad 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 369 ---VTRVSELSLCDLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLkNSEKSKVQHVPFRESKLTHYFQSFFTGK 445
Cdd:cd01372 230 dknSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISAL-GDESKKGAHVPYRDSKLTRLLQDSLGGN 308
|
410 420 430
....*....|....*....|....*....|.
gi 1907132433 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 |
2.13e-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: 216.43 E-value: 2.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 60 QVCLRIRPFTQSEKEHEaEGCVQVLDSQSVLLKDPQSilghlsekssgqvaQKFSFSKVFGPETSQKEFFLGCIMQPVKD 139
Cdd:cd01374 3 TVTVRVRPLNSREIGIN-EQVAWEIDNDTIYLVEPPS--------------TSFTFDHVFGGDSTNREVYELIAKPVVKS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 140 LLEGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmsfkphrcreylklssdqekeeSANKNTL 219
Cdd:cd01374 68 ALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD---------------------------TPDREFL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 220 LRqikevtihndsydvlcghltnsltipefeesvnscdqsslnvdnikysvwVSFFEIYNESIYDLFVPVSskfqkrKML 299
Cdd:cd01374 121 LR--------------------------------------------------VSYLEIYNEKINDLLSPTS------QNL 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 300 RLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRVT-RVSELSLC 378
Cdd:cd01374 145 KIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGTvRVSTLNLI 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 379 DLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLknSEKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSC 458
Cdd:cd01374 225 DLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKL--SEGKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAE 302
|
410
....*....|....*....
gi 1907132433 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 |
2.90e-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: 214.50 E-value: 2.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 59 LQVCLRIRPFTQSEKEHEAEGCVQVLDSQSVLLKDPQSILGHLSEKssgqvaqKFSFSKVFGPETSQKEFFLGCIMQPVK 138
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVRTGGLADKSSTK-------TYTFDMVFGPEAKQIDVYRSVVCPILD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 139 DLLEGHSRLIFTYGLTNSGKTYTFQGTE-----------ENIGILPRTLNVLFDSLqerlytkmsfkphrcreylklsSD 207
Cdd:cd01364 77 EVLMGYNCTIFAYGQTGTGKTYTMEGDRspneeytweldPLAGIIPRTLHQLFEKL----------------------ED 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 208 QEKEesankntllrqikevtihndsydvlcghltnsltipefeesvnscdqsslnvdnikYSVWVSFFEIYNESIYDLFV 287
Cdd:cd01364 135 NGTE--------------------------------------------------------YSVKVSYLEIYNEELFDLLS 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 288 PvSSKFQKRkmLRLSQDI--KGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIE-DS 364
Cdd:cd01364 159 P-SSDVSER--LRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKEtTI 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 365 EIPRVTRVSELSLCDLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLknSEKSKvqHVPFRESKLTHYFQSFFTG 444
Cdd:cd01364 236 DGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITAL--VERAP--HVPYRESKLTRLLQDSLGG 311
|
410 420 430
....*....|....*....|....*....|
gi 1907132433 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 1907132433 60 QVCLRIRPFTQSEKEHEAEGCVQVLDSQSVLLKDPQSilgHLSEKSSGQVAQKFSFSKVF---GPE----TSQKEFFLGC 132
Cdd:cd01365 4 KVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQA---DKNNKATREVPKSFSFDYSYwshDSEdpnyASQEQVYEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 133 IMQPVKDLLEGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTlnvlfdslqerlytkmsfkphrCREylklssdqekee 212
Cdd:cd01365 81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRL----------------------CED------------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 213 sankntLLRQIkevtihndsydvlcghltnsltipefeESVNScdqsslnvDNIKYSVWVSFFEIYNESIYDLFVPvsSK 292
Cdd:cd01365 127 ------LFSRI---------------------------ADTTN--------QNMSYSVEVSYMEIYNEKVRDLLNP--KP 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 293 FQKRKMLRLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQI--EDSEIPRVT 370
Cdd:cd01365 164 KKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKrhDAETNLTTE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 371 RVSELSLCDLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVL----KNSEKSKVQHVPFRESKLTHYFQSFFTGKG 446
Cdd:cd01365 244 KVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALadmsSGKSKKKSSFIPYRDSVLTWLLKENLGGNS 323
|
410 420 430
....*....|....*....|....*....|.
gi 1907132433 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 |
1.65e-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: 1.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 59 LQVCLRIRPFTQSEKEHEAEGCVQVLDSQSVLLKDpqsilghlSEKSSgqvaqKFSFSKVFGPETSQKEFFLGCIMQPVK 138
Cdd:cd01369 4 IKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIAT--------SETGK-----TFSFDRVFDPNTTQEDVYNFAAKPIVD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 139 DLLEGHSRLIFTYGLTNSGKTYTFQGT---EENIGILPRTLNVLFDSLqerlytkmsfkphrcreylklssdqekeesan 215
Cdd:cd01369 71 DVLNGYNGTIFAYGQTSSGKTYTMEGKlgdPESMGIIPRIVQDIFETI-------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 216 kntllrqikevtihndsydvlcghltnsltipefeesvnscdqsSLNVDNIKYSVWVSFFEIYNESIYDLFVPvsskfqK 295
Cdd:cd01369 119 --------------------------------------------YSMDENLEFHVKVSYFEIYMEKIRDLLDV------S 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 296 RKMLRLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQ--IEDSEIprvtRVS 373
Cdd:cd01369 149 KTNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQenVETEKK----KSG 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 374 ELSLCDLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLKNSEKSkvqHVPFRESKLTHYFQSFFTGKGKICMIIN 453
Cdd:cd01369 225 KLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKKT---HIPYRDSKLTRILQDSLGGNSRTTLIIC 301
|
410 420
....*....|....*....|....
gi 1907132433 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 |
6.85e-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: 6.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 59 LQVCLRIRPFTQSEKeheAEGCVQVLD----SQSVLLKDPQSilghlsekSSGQVAQKFSFSKVFGPETSQKEFFLGCIM 134
Cdd:cd01371 3 VKVVVRCRPLNGKEK---AAGALQIVDvdekRGQVSVRNPKA--------TANEPPKTFTFDAVFDPNSKQLDVYDETAR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 135 QPVKDLLEGHSRLIFTYGLTNSGKTYTFQGT---EENIGILPRTLNVLFDSLqerlytkmsfkphrcreylklssdqeKE 211
Cdd:cd01371 72 PLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKredPELRGIIPNSFAHIFGHI--------------------------AR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 212 ESANKNTLLRqikevtihndsydvlcghltnsltipefeesvnscdqsslnvdnikysvwVSFFEIYNESIYDLFvpvsS 291
Cdd:cd01371 126 SQNNQQFLVR--------------------------------------------------VSYLEIYNEEIRDLL----G 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 292 KFQKRKM-LRLSQDIKGYsfIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRI---LQIEDSEip 367
Cdd:cd01371 152 KDQTKRLeLKERPDTGVY--VKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIecsEKGEDGE-- 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 368 RVTRVSELSLCDLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLKNsekSKVQHVPFRESKLTHYFQSFFTGKGK 447
Cdd:cd01371 228 NHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD---GKSTHIPYRDSKLTRLLQDSLGGNSK 304
|
410 420 430
....*....|....*....|....*....|
gi 1907132433 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 |
8.42e-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: 188.48 E-value: 8.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 59 LQVCLRIRPFTQSEKEHEAEGCVQVLDSQSVLLKDPQSilghlsekssGQVAQKFSFSKVFGPETSQKEFFLGCIMQPVK 138
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVELADPRN----------HGETLKYQFDAFYGEESTQEDIYAREVQPIVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 139 DLLEGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLnvlfdslqerlytkmsfkphrcREYLKLSSDQEKEESANknt 218
Cdd:cd01376 72 HLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTV----------------------MDLLQMTRKEAWALSFT--- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 219 llrqikevtihndsydvlcghltnsltipefeesvnscdqsslnvdnikysvwVSFFEIYNESIYDLFVPvsskfqKRKM 298
Cdd:cd01376 127 -----------------------------------------------------MSYLEIYQEKILDLLEP------ASKE 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 299 LRLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEdSEIPRVTRVSELSLC 378
Cdd:cd01376 148 LVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRE-RLAPFRQRTGKLNLI 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 379 DLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLKNSEKskvqHVPFRESKLTHYFQSFFTGKGKICMIINISQSC 458
Cdd:cd01376 227 DLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLP----RIPYRDSKLTRLLQDSLGGGSRCIMVANIAPER 302
|
410
....*....|..
gi 1907132433 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 |
3.81e-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: 187.72 E-value: 3.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 59 LQVCLRIRPFTQSEKEHEAEGCVQVLDSQS-VLLKDPQsilghlsekssgqvaQKFSFSKVFGPETSQKEFFLGCIMQPV 137
Cdd:cd01373 3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTlVLHSKPP---------------KTFTFDHVADSNTNQESVFQSVGKPIV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 138 KDLLEGHSRLIFTYGLTNSGKTYTFQGTEENI--------GILPRTLNVLFDSLQerlytkmsfkphrcreylklssdQE 209
Cdd:cd01373 68 ESCLSGYNGTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQ-----------------------RE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 210 KEESAnkntllrqikevtihndsydvlcghltnsltipefeesvnscdqsslnvDNIKYSVWVSFFEIYNESIYDLFVPV 289
Cdd:cd01373 125 KEKAG-------------------------------------------------EGKSFLCKCSFLEIYNEQIYDLLDPA 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 290 SSKfqkrkmLRLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRV 369
Cdd:cd01373 156 SRN------LKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKACFVN 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 370 TRVSELSLCDLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLKNSEKSKVQHVPFRESKLTHYFQSFFTGKGKIC 449
Cdd:cd01373 230 IRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGKQRHVCYRDSKLTFLLRDSLGGNAKTA 309
|
410 420
....*....|....*....|....*...
gi 1907132433 450 MIINISQSCSAYDETLNVLKFsttAQRV 477
Cdd:cd01373 310 IIANVHPSSKCFGETLSTLRF---AQRA 334
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
105-696 |
9.42e-47 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 178.01 E-value: 9.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 105 SSGQVAQKFSFSKVFGPETSQKEFFLGCIMQPVKDLLEGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLq 184
Cdd:COG5059 50 LEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKL- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 185 erlytkmsfkphrcreylklssdqekeesankntllrqikevtihndsydvlcghltnsltipefeesvnscdqsSLNVD 264
Cdd:COG5059 129 ---------------------------------------------------------------------------EDLSM 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 265 NIKYSVWVSFFEIYNESIYDLFVPvsSKFQKRKMLRLSQDIKgysfIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLN 344
Cdd:COG5059 134 TKDFAVSISYLEIYNEKIYDLLSP--NEESLNIREDSLLGVK----VAGLTEKHVSSKEEILDLLRKGEKNRTTASTEIN 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 345 NASSRSHSIFTIRILQIEdsEIPRVTRVSELSLCDLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLknSEKSKV 424
Cdd:COG5059 208 DESSRSHSIFQIELASKN--KVSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINAL--GDKKKS 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 425 QHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNVLKFSTTAQR----VYVPDTLSSSQ---EKSFASNKSL 497
Cdd:COG5059 284 GHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSiknkIQVNSSSDSSReieEIKFDLSEDR 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 498 QDVSLDSNLDNKILNVKRKTVSWENSLEDVLENEDL--VEDLEENEETQNMETELTDEdsdKSLEECRVSTCHK----KN 571
Cdd:COG5059 364 SEIEILVFREQSQLSQSSLSGIFAYMQSLKKETETLksRIDLIMKSIISGTFERKKLL---KEEGWKYKSTLQFlrieID 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 572 KELLDLIEKLNKRLINENK-EKLTLELKIREEV---TQEFTQYWSQREaDFKETLLHereILEENAERRLAIFKDLVGKc 647
Cdd:COG5059 441 RLLLLREEELSKKKTKIHKlNKLRHDLSSLLSSipeETSDRVESEKAS-KLRSSAST---KLNLRSSRSHSKFRDHLNG- 515
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1907132433 648 dsqdepTNRICDIELETEEAIACLQLKFNQVKAELAETKEELIKAQEEL 696
Cdd:COG5059 516 ------SNSSTKELSLNQVDLAGSERKVSQSVGELLRETQSLNKSLSSL 558
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
61-471 |
1.92e-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: 1.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 61 VCLRIRPFTQSEkeheaegcVQVLDSQSVLLKDPQSILGHLSEK----SSGQVAQKFSFSKVFGPETSQKEFFLGCIMQP 136
Cdd:cd01367 4 VCVRKRPLNKKE--------VAKKEIDVVSVPSKLTLIVHEPKLkvdlTKYIENHTFRFDYVFDESSSNETVYRSTVKPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 137 VKDLLEGHSRLIFTYGLTNSGKTYT----FQGTEENIGIlprtlnvlfdslqerlytkmsfkphrcreYLKLSSDqekee 212
Cdd:cd01367 76 VPHIFEGGKATCFAYGQTGSGKTYTmggdFSGQEESKGI-----------------------------YALAARD----- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 213 sankntLLRQIKEVTIHNDsydvlcghltnsltipefeesvnscdqsslnvdnikYSVWVSFFEIYNESIYDLfvpvssk 292
Cdd:cd01367 122 ------VFRLLNKLPYKDN------------------------------------LGVTVSFFEIYGGKVFDL------- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 293 FQKRKMLRLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIrilQIEDSEIPRVtrV 372
Cdd:cd01367 153 LNRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQI---ILRDRGTNKL--H 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 373 SELSLCDLAGSER-SMKTQNEGERLREAGNINTSLLTLGKCINVLKNSEKskvqHVPFRESKLTHYFQ-SFFTGKGKICM 450
Cdd:cd01367 228 GKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNKA----HIPFRGSKLTQVLKdSFIGENSKTCM 303
|
410 420
....*....|....*....|.
gi 1907132433 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 |
1.04e-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: 1.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 108 QVAQKFSFSKVFgpETSQKEFFLGCIMQPVKD-LLEGHSRLIFTYGLTNSGKTYTFQGTEENI---GILPRTLNVLFDSL 183
Cdd:cd01375 45 QEDWSFKFDGVL--HNASQELVYETVAKDVVSsALAGYNGTIFAYGQTGAGKTFTMTGGTENYkhrGIIPRALQQVFRMI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 184 QERlYTKMsfkphrcreylklssdqekeesankntllrqikevtihndsydvlcghltnsltipefeesvnscdqsslnv 263
Cdd:cd01375 123 EER-PTKA------------------------------------------------------------------------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 264 dnikYSVWVSFFEIYNESIYDLFVPVSSKFQKRKMLRLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKL 343
Cdd:cd01375 130 ----YTVHVSYLEIYNEQLYDLLSTLPYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTM 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 344 NNASSRSHSIFTIRiLQIEDSEIPRVT-RVSELSLCDLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLknSEKS 422
Cdd:cd01375 206 NKNSSRSHCIFTIH-LEAHSRTLSSEKyITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIAL--SDKD 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907132433 423 KvQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNVLKFsttAQRV 477
Cdd:cd01375 283 R-THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRF---ASRV 333
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
81-477 |
1.53e-31 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 135.45 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 81 VQVLDSQSVLLKDPQS--ILGHLSEKSSGQVAQKFSFSKVFGPETSQKEFFLGCIMQPVKDLLEGHSRLIFTYGLTNSGK 158
Cdd:PLN03188 100 VKVIVRMKPLNKGEEGemIVQKMSNDSLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 159 TYTFQG-----TEENI-----GILPRTLNVLFDSLQERlytkmsfkphrcreylklssdqekeesankntllrQIKevti 228
Cdd:PLN03188 180 TYTMWGpanglLEEHLsgdqqGLTPRVFERLFARINEE-----------------------------------QIK---- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 229 HNDSydvlcghltnsltipefeesvnscdqsslnvdNIKYSVWVSFFEIYNESIYDLFVPVsskfQKRKMLRlsQDIKGY 308
Cdd:PLN03188 221 HADR--------------------------------QLKYQCRCSFLEIYNEQITDLLDPS----QKNLQIR--EDVKSG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 309 SFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIrilqIEDSEIPRVT------RVSELSLCDLAG 382
Cdd:PLN03188 263 VYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTC----VVESRCKSVAdglssfKTSRINLVDLAG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 383 SERSMKTQNEGERLREAGNINTSLLTLGKCINVLKN-SEKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAY 461
Cdd:PLN03188 339 SERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEiSQTGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCK 418
|
410
....*....|....*.
gi 1907132433 462 DETLNVLKFSTTAQRV 477
Cdd:PLN03188 419 SETFSTLRFAQRAKAI 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
527-1291 |
2.22e-20 |
|
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: 98.59 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 527 VLENEDLVEDLEENEETQN-METELTDEDSDKSLEECRVSTCHKKNKELLDLIEKLNKRLINENKEKLTLELKIRE-EVT 604
Cdd:TIGR02168 231 VLRLEELREELEELQEELKeAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIlRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 605 QEFTQYWSQREADFKETLLHEREILEENAERRLAIFKDLVGKCDSQDEPTNRICDIELETEEAIACLQLKFNQVKAELAE 684
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 685 TKEELIKAQEELKNRESnslvqalktsskvdtsltsnkstcneTSEMPKNSRAQTHSERKRLNEDglqlgeppakkgliL 764
Cdd:TIGR02168 391 LELQIASLNNEIERLEA--------------------------RLERLEDRRERLQQEIEELLKK--------------L 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 765 VSPPITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRA 844
Cdd:TIGR02168 431 EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 845 --DVEQIQASYNSAVAEL-----QTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLdSPSHISKI 917
Cdd:TIGR02168 511 llKNQSGLSGILGVLSELisvdeGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSI-KGTEIQGN 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 918 DLLNLQDLSSGAK-GDNCLNTSQQLPG--GDFSST--WVKEYHT-QEISRENSFHASI----EAIWEECKEIVKASSKKS 987
Cdd:TIGR02168 590 DREILKNIEGFLGvAKDLVKFDPKLRKalSYLLGGvlVVDDLDNaLELAKKLRPGYRIvtldGDLVRPGGVITGGSAKTN 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 988 HQIQG-------LEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAERE 1060
Cdd:TIGR02168 670 SSILErrreieeLEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1061 QALSELSQDVTCYKAKIKDLEVIVETQKDECKR-LVELEQSILEKESAILKLEANLKECEAKHQdhirtnDLSAKEVKFR 1139
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAeIEELEAQIEQLKEELKALREALDELRAELT------LLNEEAANLR 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1140 EEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREV 1219
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907132433 1220 SVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQ---KMEEAVQQYEKVCKDLSVKEKLVEDMR 1291
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEyslTLEEAEALENKIEDDEEEARRRLKRLE 978
|
|
| RBD_KIF20B |
cd21786 |
RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B ... |
598-652 |
3.42e-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: 82.53 E-value: 3.42e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1907132433 598 KIREEVTQEFTQYWSQREADFKETLLHEREILEENAERRLAIFKDLVGKCDSQDE 652
Cdd:cd21786 1 KIREEVTQEFTELFSEMEKDYSERLEREREILEERAEKRLEIFKNLVNKTAKEEE 55
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
630-1431 |
9.36e-19 |
|
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: 93.20 E-value: 9.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 630 EENAERRLAI--FKDLVGKCDSQDEPTNRICDIELETEEAIACLQLKFNQVKAELAETKEELIKAQEELKNresnslvqa 707
Cdd:TIGR02168 222 LRELELALLVlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA--------- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 708 lktsskvdtsLTSNKSTCNETSEMPKNSRAQTHSERKRLNEDGLQLGEPPAKKGLIL--VSPPITEEQNKMGEMQQSVSE 785
Cdd:TIGR02168 293 ----------LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELaeLEEKLEELKEELESLEAELEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 786 VVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASY-NSAVAELQTQK 864
Cdd:TIGR02168 363 LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAEL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 865 AVNQEQRDRILKLSQEMETAARSIESNVSQIKQ-MQTKIDELRSLDSPSHISKIDLLNLQDLSSGAKGdncLNTSQQLPG 943
Cdd:TIGR02168 443 EELEEELEELQEELERLEEALEELREELEEAEQaLDAAERELAQLQARLDSLERLQENLEGFSEGVKA---LLKNQSGLS 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 944 GDFSSTWvkeyhtQEISRENSFHASIE-AIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKgyreENSDLRAQESQGK 1022
Cdd:TIGR02168 520 GILGVLS------ELISVDEGYEAAIEaALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFL----PLDSIKGTEIQGN 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1023 NRdhQLKEKESLIQQLREELQEKSVSLRV-------QVQLVAEREQALSELSQDVTCYKAKIKDLEVI----VETQKDEc 1091
Cdd:TIGR02168 590 DR--EILKNIEGFLGVAKDLVKFDPKLRKalsyllgGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVrpggVITGGSA- 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1092 krlvELEQSILEKESAILKLEANLKECEAKhqdhirTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETE 1171
Cdd:TIGR02168 667 ----KTNSSILERRREIEELEEKIEELEEK------IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1172 KLKEELaansiltqnlkadlQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQ 1251
Cdd:TIGR02168 737 RLEAEV--------------EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1252 RTIQQLKEQLSNQKMEEAVQQ--YEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKF 1329
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRerLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1330 KDLETRSNQRLntgtmDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCL 1409
Cdd:TIGR02168 883 ASLEEALALLR-----SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAE 957
|
810 820
....*....|....*....|..
gi 1907132433 1410 KLQNEVETLTAQLAEKNSELQK 1431
Cdd:TIGR02168 958 ALENKIEDDEEEARRRLKRLEN 979
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
793-1439 |
4.95e-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: 84.34 E-value: 4.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 793 LKEKNEELKRLLTIGE-----NELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVN 867
Cdd:TIGR02168 218 LKAELRELELALLVLRleelrEELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 868 QEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSldspshiskiDLLNLQDLSSGAKGdNCLNTSQQLpggdfs 947
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE----------ELAELEEKLEELKE-ELESLEAEL------ 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 948 stwvKEYHTQEISRENSFHASIEAIWEECKEIVKASSKK---SHQIQGLEEQIEKLQVEVKGYREENSDL--RAQESQGK 1022
Cdd:TIGR02168 361 ----EELEAELEELESRLEELEEQLETLRSKVAQLELQIaslNNEIERLEARLERLEDRRERLQQEIEELlkKLEEAELK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1023 NRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSiL 1102
Cdd:TIGR02168 437 ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN-Q 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1103 EKESAILKLEANLKECEAKHQ-----------------------------------------------DHIRTNDLSAKE 1135
Cdd:TIGR02168 516 SGLSGILGVLSELISVDEGYEaaieaalggrlqavvvenlnaakkaiaflkqnelgrvtflpldsikgTEIQGNDREILK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1136 ------------VKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKL------------------KEELAANSILtq 1185
Cdd:TIGR02168 596 niegflgvakdlVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYrivtldgdlvrpggvitgGSAKTNSSIL-- 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1186 NLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQK 1265
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1266 MEEAVQQYEKvckdlSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNTGTM 1345
Cdd:TIGR02168 754 KELTELEAEI-----EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1346 ---------DDLDVLTRKFSKLQ----------DELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRE 1406
Cdd:TIGR02168 829 lerriaateRRLEDLEEQIEELSedieslaaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
730 740 750
....*....|....*....|....*....|...
gi 1907132433 1407 RCLKLQNEVETLTAQLAEKNSELQKWREERDQL 1439
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
793-1468 |
8.66e-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: 83.57 E-value: 8.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 793 LKEKNEELKRL-LTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQR 871
Cdd:TIGR02168 215 YKELKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 872 DRILKLSQEMETAARSIESNVSQIKQMQTKIDELrslDSPSHISKIDLLNLQDLSSGAKGdNCLNTSQQLpggdfsstwv 951
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEEL---ESKLDELAEELAELEEKLEELKE-ELESLEAEL---------- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 952 KEYHTQEISRENSFHASIEAIWEECKEIVKASSKK---SHQIQGLEEQIEKLQVEVKGYREENSDL--RAQESQGKNRDH 1026
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIaslNNEIERLEARLERLEDRRERLQQEIEELlkKLEEAELKELQA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1027 QLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSiLEKES 1106
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN-QSGLS 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1107 AILKLEANLKECEAK-----------HQDHIRTNDLSA--KEVKFREE-----VTRLANNLHDTKQLLQSKEEENE---- 1164
Cdd:TIGR02168 520 GILGVLSELISVDEGyeaaieaalggRLQAVVVENLNAakKAIAFLKQnelgrVTFLPLDSIKGTEIQGNDREILKnieg 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1165 ----ISRQETEKLKEELAANSILTQNLKAD-LQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKL------LRIKI 1233
Cdd:TIGR02168 600 flgvAKDLVKFDPKLRKALSYLLGGVLVVDdLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTnssileRRREI 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1234 NELEKKKNQYSQDLDMKQRTIQQLKEQLSN---------QKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQ 1304
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEEleeeleqlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1305 DRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRlntgtMDDLDVLTRKFSKLQDELQESEEKYKADRkkwlEEKAVLT 1384
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL-----KEELKALREALDELRAELTLLNEEAANLR----ERLESLE 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1385 TQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLvtavETQMKALLSSCKHKDEEIQEL 1464
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL----EEALALLRSELEELSEELREL 906
|
....
gi 1907132433 1465 RKAA 1468
Cdd:TIGR02168 907 ESKR 910
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1035-1337 |
1.84e-15 |
|
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: 82.41 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1035 IQQLREELQEKSVSLRVQVQLvAEREQALSE---------LSQDVTCYKAKIKDLEVIVETQKDECK----RLVELEQSI 1101
Cdd:TIGR02168 191 LEDILNELERQLKSLERQAEK-AERYKELKAelrelelalLVLRLEELREELEELQEELKEAEEELEeltaELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1102 LEKESAILKLEANLKECEAKHQDH-IRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAN 1180
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALaNEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1181 SILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQ 1260
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907132433 1261 LSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSN 1337
Cdd:TIGR02168 430 LEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
569-1417 |
1.62e-14 |
|
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: 79.63 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 569 KKNKELLDLIEKLNKRLINENKEKLTLE-LKIREEVTQEFTQYWSQREADFKETLLHEREILEENAERRL--------AI 639
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELkLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLqellrdeqEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 640 FKDLVGKCDSQDEPTNRICDIELETEEAIACLQLKFNQVKAELAETKEELIKAqEELKNRESNSLVQALKTSSKVDTSLT 719
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL-ERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 720 SNKSTCNETSEMPKNSRAQTHSE-------RKRLNEDGLQLGEPPAKKGLILVSPPITEE--QNKMGEMQQSVSEVVEGN 790
Cdd:pfam02463 332 KEKEEIEELEKELKELEIKREAEeeeeeelEKLQEKLEQLEEELLAKKKLESERLSSAAKlkEEELELKSEEEKEAQLLL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 791 RVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQiqasynSAVAELQTQKAVNQEQ 870
Cdd:pfam02463 412 ELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK------SEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 871 RDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQDLSSGAKGDNClntsqqlpgGDFSSTW 950
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV---------IVEVSAT 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 951 VKEYHTQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQL-K 1029
Cdd:pfam02463 557 ADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELtK 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1030 EKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSI--LEKESA 1107
Cdd:pfam02463 637 LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREkeELKKLK 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1108 ILKLEANLKECEAKHQDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNL 1187
Cdd:pfam02463 717 LEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKL 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1188 KADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKME 1267
Cdd:pfam02463 797 KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1268 EAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADwLATELDKWKEKFKDLETRSNQRLNTGTMDD 1347
Cdd:pfam02463 877 EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKE-EAEILLKYEEEPEELLLEEADEKEKEENNK 955
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1348 LDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVET 1417
Cdd:pfam02463 956 EEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLEL 1025
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1167-1439 |
3.49e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.44 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1167 RQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQrevsvmrDEEKLLRIKINELEKKKNQYSQD 1246
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-------AEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1247 LDMKQRTIQQLKEQLS--NQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQtqaeqdRVLEAKSEEADWLATELDK 1324
Cdd:COG1196 311 RRELEERLEELEEELAelEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE------ALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1325 WKEKFKDLETRSNQRlntgtmddldvltrkfsKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADD 1404
Cdd:COG1196 385 AEELLEALRAAAELA-----------------AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270
....*....|....*....|....*....|....*
gi 1907132433 1405 RERCLKLQNEVETLTAQLAEKNSELQKWREERDQL 1439
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
966-1470 |
8.42e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.90 E-value: 8.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 966 HASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEK 1045
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1046 SVSLRVQVQLVAEREQALSELSQDVtcyKAKIKDLEVIVETQKDEckrLVELEQSILEKESAILKLEANLKECEAKHQDH 1125
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEEL---EEELEEAEEELEEAEAE---LAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1126 IRtndlsaKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKF 1205
Cdd:COG1196 392 LR------AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1206 IDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRtiQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEK 1285
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA--ALLLAGLRGLAGAVAVLIGVEAAYEAALEAA 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1286 LVEDMRLTLVEQEQTQAEQDRVLEAKSEEAdwlATELDKWKEKFKDLETRSNQRLntgtmddldVLTRKFSKLQDELQES 1365
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYLKAAKAGR---ATFLPLDKIRARAALAAALARG---------AIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1366 EEKYKAdrkkwLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLVTAVET 1445
Cdd:COG1196 612 DARYYV-----LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
490 500
....*....|....*....|....*
gi 1907132433 1446 QMKALLSSCKHKDEEIQELRKAAAK 1470
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAE 711
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
956-1467 |
1.66e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 72.77 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 956 TQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKG-------YREENSDLRAQ-ESQGKNRDHQ 1027
Cdd:PRK02224 219 DEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAEterereeLAEEVRDLRERlEELEEERDDL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1028 LKEKE------SLIQQLREELQEKSVSLRvqvQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKrlvELEQSI 1101
Cdd:PRK02224 299 LAEAGlddadaEAVEARREELEDRDEELR---DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAA---ELESEL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1102 LEKESAILKLEANLKECEakhqdhirtndlsakevkfrEEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAans 1181
Cdd:PRK02224 373 EEAREAVEDRREEIEELE--------------------EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA--- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1182 iltqNLKADLQKKEEDCAElKEKFIDAKK---------------QIEQVQREVSVMRDEEKLLRIKINELEKKKNQySQD 1246
Cdd:PRK02224 430 ----ELEATLRTARERVEE-AEALLEAGKcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLER-AED 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1247 LDMKQRTIQQLKEQLSNqkmeeavqqyekVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWK 1326
Cdd:PRK02224 504 LVEAEDRIERLEERRED------------LEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1327 EKFKDLETRSNQrlNTGTMDDLDvltrKFSKLQDELQESEEKYKADRKKwLEEKAVLTTQAKE---AENVRNREMRKYAD 1403
Cdd:PRK02224 572 EEVAELNSKLAE--LKERIESLE----RIRTLLAAIADAEDEIERLREK-REALAELNDERRErlaEKRERKRELEAEFD 644
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907132433 1404 DrERCLKLQNEVETLTAQLAEKNSELQKWREERDQL---VTAVETQMKALlssckhkdEEIQELRKA 1467
Cdd:PRK02224 645 E-ARIEEAREDKERAEEYLEQVEEKLDELREERDDLqaeIGAVENELEEL--------EELRERREA 702
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
738-1445 |
3.13e-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: 72.07 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 738 QTHSERKRLNEDGlQLGEppakKGLILVSPPITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEE 817
Cdd:pfam15921 86 QVKDLQRRLNESN-ELHE----KQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 818 KAELNKQVVSLQQQLRffeeknsslradveQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAA-RSIESNVSQI- 895
Cdd:pfam15921 161 KEDMLEDSNTQIEQLR--------------KMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHfRSLGSAISKIl 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 896 KQMQTKI-----------DELRSLDSPSHiSKIDLLNLQDLSsgakgdnclNTSQQLPGGDFSSTWVKEYHTQEISRENS 964
Cdd:pfam15921 227 RELDTEIsylkgrifpveDQLEALKSESQ-NKIELLLQQHQD---------RIEQLISEHEVEITGLTEKASSARSQANS 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 965 FHASIEAIWEECKeivKASSKKSHQIQGLEEQIEKLQVEVKG----YREENSDLRAQ--------ESQGKNRDHQLKEKE 1032
Cdd:pfam15921 297 IQSQLEIIQEQAR---NQNSMYMRQLSDLESTVSQLRSELREakrmYEDKIEELEKQlvlanselTEARTERDQFSQESG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1033 SLIQQLREEL-----QEKSVSL-RVQVQLVAEREQA----LSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSIL 1102
Cdd:pfam15921 374 NLDDQLQKLLadlhkREKELSLeKEQNKRLWDRDTGnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAI 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1103 EKESAILKLEANLKECEAKHQDHIR--TNDLSAKEVKFrEEVTRLANNLHDTkqlLQSKEEENEISRQETEKLKEELAAN 1180
Cdd:pfam15921 454 QGKNESLEKVSSLTAQLESTKEMLRkvVEELTAKKMTL-ESSERTVSDLTAS---LQEKERAIEATNAEITKLRSRVDLK 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1181 SILTQNLKAD---LQKKEEDCAELKEKFIDAKKQIEqvqrevsvmrdeekLLRIKINELEKKKNQYSQDLDMKQRTIQQL 1257
Cdd:pfam15921 530 LQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIE--------------ILRQQIENMTQLVGQHGRTAGAMQVEKAQL 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1258 KEQLSNQKMEEAVQQYEKVCKDLSVK--EKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLEtr 1335
Cdd:pfam15921 596 EKEINDRRLELQEFKILKDKKDAKIRelEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLS-- 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1336 snqrlntgtmDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREM-------RKYADDRERC 1408
Cdd:pfam15921 674 ----------EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMkvamgmqKQITAKRGQI 743
|
730 740 750
....*....|....*....|....*....|....*..
gi 1907132433 1409 LKLQNEVETLTAQLAEKNSELQKWREERDQLVTAVET 1445
Cdd:pfam15921 744 DALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELST 780
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
958-1314 |
6.51e-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: 70.87 E-value: 6.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 958 EISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEvKGYREENSDLRA--QESQGKNRDHQLKEKESLI 1035
Cdd:TIGR02169 161 EIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQALLKekREYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1036 QQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVivetqkdecKRLVELEQSILEKESAILKLEANL 1115
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE---------EEQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1116 KECEAKHQDhirtndLSAKEVKFREEvtrlannLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKE 1195
Cdd:TIGR02169 311 AEKERELED------AEERLAKLEAE-------IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1196 EDCAELKEKFIDAKKQIEQVQREV-SVMRDEEKL-------------LRIKINELEKKKNQYSQDLDMKQRTIQQLKEQL 1261
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREInELKRELDRLqeelqrlseeladLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907132433 1262 SN--QKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQE-QTQAEQDRVLEAKSEE 1314
Cdd:TIGR02169 458 EQlaADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEaQARASEERVRGGRAVE 513
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
769-1112 |
7.36e-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: 70.86 E-value: 7.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 769 ITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQ 848
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 849 IQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRsldspshiSKIDLLN--LQDLS 926
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR--------AELTLLNeeAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 927 SGAKGDNCLNTSQQLPGGDFSSTWVKEYHTQEISRE--NSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEV 1004
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1005 KGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEK-----SVSLRVQVQLVAEREQALSELSQDVTCYKAKIKD 1079
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlseeySLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
330 340 350
....*....|....*....|....*....|....*..
gi 1907132433 1080 LEVI----VETQKDECKRLVELEQSILEKESAILKLE 1112
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 |
9.14e-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: 61.32 E-value: 9.14e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1907132433 598 KIREEVTQEFTQYWSQREADFKETLLHEREILEENAERRLAIFKDLVGKCDSQDE 652
Cdd:cd21744 1 RIREEVSEEFEEQFALMEEDYEERLENEKEILEERYEKRLEIRKELIKKLSAALE 55
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
952-1470 |
1.63e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.32 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 952 KEYHTQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEK 1031
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1032 ESLIQQLR---EELQEKSVSLRVQVQLVAE---REQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKE 1105
Cdd:PRK03918 258 EEKIRELEeriEELKKEIEELEEKVKELKElkeKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1106 SAILKLEANLKECEAK----HQDHIRTNDLSAKEVKFREEVTRLAN-NLHDTKQLLQSKEEENEISRQETEKLKEELAAN 1180
Cdd:PRK03918 338 ERLEELKKKLKELEKRleelEERHELYEEAKAKKEELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1181 SILTQNLKADLQK---------------KEEDCAELKEKFidaKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQ 1245
Cdd:PRK03918 418 KKEIKELKKAIEElkkakgkcpvcgrelTEEHRKELLEEY---TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1246 DLDMKQ--RTIQQLKEQLSN---QKMEEAVQQYEKVCKD---LSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADW 1317
Cdd:PRK03918 495 LIKLKElaEQLKELEEKLKKynlEELEKKAEEYEKLKEKlikLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAE 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1318 LATEL--------DKWKEKFKDLETRSNQRLN-TGTMDDLDVLTRKFSKLQDELQESEEKYkADRKKWLEEkavLTTQAK 1388
Cdd:PRK03918 575 LLKELeelgfesvEELEERLKELEPFYNEYLElKDAEKELEREEKELKKLEEELDKAFEEL-AETEKRLEE---LRKELE 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1389 EAENVRNREmrKYADDRERCLKLQNEVETLTAQLaeknSELQKWREERDQLVTAVETQMKALlsscKHKDEEIQELRKAA 1468
Cdd:PRK03918 651 ELEKKYSEE--EYEELREEYLELSRELAGLRAEL----EELEKRREEIKKTLEKLKEELEER----EKAKKELEKLEKAL 720
|
..
gi 1907132433 1469 AK 1470
Cdd:PRK03918 721 ER 722
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1094-1469 |
2.94e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1094 LVELEQSI--LEKESAI----LKLEANLKECEAKHQdHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISR 1167
Cdd:COG1196 195 LGELERQLepLERQAEKaeryRELKEELKELEAELL-LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1168 QETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDL 1247
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1248 DMKQRTIQQLKEQLSNQKMEEAVQQyekvcKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKE 1327
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAE-----EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1328 KFKDLEtrsnqrlntgtmddldvltrkfsKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRER 1407
Cdd:COG1196 429 ALAELE-----------------------EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907132433 1408 CLKLQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQMKALLSSCKHKDEEIQELRKAAA 1469
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA 547
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
778-1389 |
3.36e-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: 68.56 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 778 EMQQSVSEVVEGNRVLKEKNEELKRLltiGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAV 857
Cdd:TIGR02169 259 EISELEKRLEEIEQLLEELNKKIKDL---GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 858 AELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSlDSPSHISKIDLLNLQDLSSGAKGDNCLNT 937
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD-ELKDYREKLEKLKREINELKRELDRLQEE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 938 SQQLpggdfsstwvkeyhTQEISRensFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQ 1017
Cdd:TIGR02169 415 LQRL--------------SEELAD---LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1018 ESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAK-IKDLE---------VIVETQ 1087
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERyATAIEvaagnrlnnVVVEDD 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1088 KDECK---------------------RLVELEQSILEKESAILKLeANLKECEAKHQ--------DHIRTNDL-SAKE-- 1135
Cdd:TIGR02169 558 AVAKEaiellkrrkagratflplnkmRDERRDLSILSEDGVIGFA-VDLVEFDPKYEpafkyvfgDTLVVEDIeAARRlm 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1136 ---------------------------------VKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSI 1182
Cdd:TIGR02169 637 gkyrmvtlegelfeksgamtggsraprggilfsRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1183 LTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDL------------DMK 1250
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndlearlshsriPEI 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1251 QRTIQQLKEQLSnqKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQ-----EQTQAEQDRVLEAKSEEADwLATELDKW 1325
Cdd:TIGR02169 797 QAELSKLEEEVS--RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQridlkEQIKSIEKEIENLNGKKEE-LEEELEEL 873
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907132433 1326 KEKFKDLETRSnqrlnTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKE 1389
Cdd:TIGR02169 874 EAALRDLESRL-----GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
951-1439 |
4.72e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.78 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 951 VKEYHTQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQesqgKNRDHQLKE 1030
Cdd:PRK03918 170 VIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL----KEEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1031 KESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILK 1110
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1111 LEANLKECEAKHQdhiRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELaansiltqnlkad 1190
Cdd:PRK03918 326 IEERIKELEEKEE---RLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKL------------- 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1191 lqkkEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKK-------------------NQYSQDLDMKQ 1251
Cdd:PRK03918 390 ----EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteehrkellEEYTAELKRIE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1252 RTIQQLKEQLSNQKME-EAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQdrvLEAKSEEADWLATELDKWKEKFK 1330
Cdd:PRK03918 466 KELKEIEEKERKLRKElRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEE---LEKKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1331 DLETRSNQrlntgtmddLDVLTRKFSKLQDELQESEEKyKADRKKWLEEKAV-----LTTQAKEAENVRNR--EMRKYAD 1403
Cdd:PRK03918 543 SLKKELEK---------LEELKKKLAELEKKLDELEEE-LAELLKELEELGFesveeLEERLKELEPFYNEylELKDAEK 612
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1907132433 1404 DRERCLK----LQNEVETLTAQLAEKNSELQKWREERDQL 1439
Cdd:PRK03918 613 ELEREEKelkkLEEELDKAFEELAETEKRLEELRKELEEL 652
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
769-1306 |
7.72e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 7.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 769 ITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELkrlltigENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQ 848
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRREL-------EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 849 IQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSpshiskidllnlqdlssg 928
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE------------------ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 929 akgdnclntsqqlpggdfsstwvkEYHTQEISREnsfhASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYR 1008
Cdd:COG1196 418 ------------------------RLEEELEELE----EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1009 EENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAER--EQALSELSQDVTCYKAKIKD------L 1080
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglAGAVAVLIGVEAAYEAALEAalaaalQ 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1081 EVIVETQKDECKRLVELEQSILEKESAI----LKLEANLKECEAKHQDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLL 1156
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKAGRATFLpldkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1157 QSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINEL 1236
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1237 EKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEkvcKDLSVKEKLVEDMRLTLVEQEQTQAEQDR 1306
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL---LEEEALEELPEPPDLEELERELERLEREI 776
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1085-1512 |
9.81e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.09 E-value: 9.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1085 ETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTND--LSAKEVKFREEVTRLANNLHDTKQLLQSKEEE 1162
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADeaKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1163 NEisRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLlriKINELEKKKNQ 1242
Cdd:PTZ00121 1328 KK--KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK---KADEAKKKAEE 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1243 YsqdldmKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATEL 1322
Cdd:PTZ00121 1403 D------KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK 1476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1323 DKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKfSKLQDELQESEEKYKADRKKWLEEK-----AVLTTQAKEAENVRNRE 1397
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKADEAKKAEEAkkadeAKKAEEKKKADELKKAE 1555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1398 MRKYADDRERCLKLQNEVETLTAQLaEKNSELQKWREERDQLVTAVETQMKALLSSCKHKDEE----IQELRKAAAKSTG 1473
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMAL-RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikAEELKKAEEEKKK 1634
|
410 420 430
....*....|....*....|....*....|....*....
gi 1907132433 1474 TENQTMNPKPEYNDSVDLGGVETEPQSTSLEISRNTAED 1512
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1029-1269 |
1.31e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.63 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1029 KEKESLIQQLRE---ELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVivetqkdeckRLVELEQSILEKE 1105
Cdd:TIGR02169 688 RELSSLQSELRRienRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE----------DLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1106 SAILKLEANLKECEAK-HQDHIRTNDLSAKEV------------KFREEVTRLANNLHDTKQLLQSKEEENEISRQETEK 1172
Cdd:TIGR02169 758 SELKELEARIEELEEDlHKLEEALNDLEARLShsripeiqaelsKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1173 LKEELaansILTQNLKADLQKKEEDC----AELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLD 1248
Cdd:TIGR02169 838 LQEQR----IDLKEQIKSIEKEIENLngkkEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913
|
250 260
....*....|....*....|.
gi 1907132433 1249 MKQRTIQQLKEQLSNQKMEEA 1269
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEELS 934
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
984-1465 |
4.35e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 984 SKKSHQIQGLEEQIEK-----LQVEVKGYREENSDLRAQ----ESQGKNRDHQLKEKESLI---QQLREELQEKSVSLRV 1051
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEkeekdLHERLNGLESELAELDEEieryEEQREQARETRDEADEVLeehEERREELETLEAEIED 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1052 QVQLVAEREQALSELSQdvtcykaKIKDLEVIVETQKDECKRLV-ELEQSILEKESAILKLEAnLKECEAKHQDHIRTND 1130
Cdd:PRK02224 263 LRETIAETEREREELAE-------EVRDLRERLEELEEERDDLLaEAGLDDADAEAVEARREE-LEDRDEELRDRLEECR 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1131 LSAKEvkFREEVTRLANNLHDTkqllqskEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKK 1210
Cdd:PRK02224 335 VAAQA--HNEEAESLREDADDL-------EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1211 QIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAvqqyEKVCKdLSVKEKLVEDM 1290
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGS----PHVET-IEEDRERVEEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1291 RLTLVEQEQTQAEQDRVLEaKSEEADWLATELDKWKEKFKDLETRSNQRLNTgtmddLDVLTRKFSKLQDELQESEEkyK 1370
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLE-RAEDLVEAEDRIERLEERREDLEELIAERRET-----IEEKRERAEELRERAAELEA--E 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1371 ADRKkwlEEKAvlTTQAKEAENVR------NREMRKYADDRERClklqNEVETLTAQLAEKNSELQKWREERDQLvTAVE 1444
Cdd:PRK02224 553 AEEK---REAA--AEAEEEAEEAReevaelNSKLAELKERIESL----ERIRTLLAAIADAEDEIERLREKREAL-AELN 622
|
490 500
....*....|....*....|.
gi 1907132433 1445 TQMKALLSSckhKDEEIQELR 1465
Cdd:PRK02224 623 DERRERLAE---KRERKRELE 640
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
793-1335 |
8.13e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 8.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 793 LKEKNEELKRLltigENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRD 872
Cdd:COG1196 234 LRELEAELEEL----EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 873 RILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQDLSSGAKGDNCLNTSQQLpggdfsSTWVK 952
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE------EELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 953 EYHT--QEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKE 1030
Cdd:COG1196 384 LAEEllEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1031 KESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVEtQKDECKRLVELEQSILEKESAILK 1110
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG-LRGLAGAVAVLIGVEAAYEAALEA 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1111 LEAnlkeceAKHQDHIRTNDLSAKEV------KFREEVTRLANNLHDTKQLLQSKEEENEISR-------------QETE 1171
Cdd:COG1196 543 ALA------AALQNIVVEDDEVAAAAieylkaAKAGRATFLPLDKIRARAALAAALARGAIGAavdlvasdlreadARYY 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1172 KLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQ 1251
Cdd:COG1196 617 VLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELE 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1252 RTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADwlateLDKWKEKFKD 1331
Cdd:COG1196 697 EALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD-----LEELERELER 771
|
....
gi 1907132433 1332 LETR 1335
Cdd:COG1196 772 LERE 775
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
791-1141 |
1.64e-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: 63.16 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 791 RVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQasynsavAELQTQKAVNQEQ 870
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE-------QEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 871 RDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSL-----DSPSHiSKIDllNLQDLSSGAKGDNCLNTS--QQLPG 943
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlndleARLSH-SRIP--EIQAELSKLEEEVSRIEArlREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 944 GDFSSTWVKEYHTQEIsrensfhASIEAIWEECKEIVKASSKKSHQIQG----LEEQIEKLQVEVKGYREENSDLRAQEs 1019
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEI-------QELQEQRIDLKEQIKSIEKEIENLNGkkeeLEEELEELEAALRDLESRLGDLKKER- 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1020 qgKNRDHQLKEKESLIQQLREELQEKSvslrvqvQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKrlveLEQ 1099
Cdd:TIGR02169 892 --DELEAQLRELERKIEELEAQIEKKR-------KRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED----VQA 958
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1907132433 1100 SILEKESAILKLE-ANLKECEAKHQDHIRTNDLSAKEVKFREE 1141
Cdd:TIGR02169 959 ELQRVEEEIRALEpVNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
969-1465 |
2.84e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 969 IEAIWEECKEIVKASSKKShqiQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVS 1048
Cdd:COG4717 48 LERLEKEADELFKPQGRKP---ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1049 LRVQvQLVAEREQALSELSQDVTCYKakikdlevivetqkdeckRLVELEQSILEKESAILKLEANLKECEAKHQDHIRT 1128
Cdd:COG4717 125 LQLL-PLYQELEALEAELAELPERLE------------------ELEERLEELRELEEELEELEAELAELQEELEELLEQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1129 NDLSAKE--VKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFI 1206
Cdd:COG4717 186 LSLATEEelQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1207 DAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQlsnqkmeeavqQYEKVCKDLSVKEKL 1286
Cdd:COG4717 266 GSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEE-----------ELEELLAALGLPPDL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1287 VEDMRLTLVEQEQTQAEQDRVLEAKSEEADWlateldkwkekfKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDelqese 1366
Cdd:COG4717 335 SPEELLELLDRIEELQELLREAEELEEELQL------------EELEQEIAALLAEAGVEDEEELRAALEQAEE------ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1367 ekykadRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRerclkLQNEVETLTAQLAEKNSELQKWREERDQLvtavETQ 1446
Cdd:COG4717 397 ------YQELKEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELEEELEELEEELEELREELAEL----EAE 461
|
490
....*....|....*....
gi 1907132433 1447 MKALLSsckhkDEEIQELR 1465
Cdd:COG4717 462 LEQLEE-----DGELAELL 475
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
753-1448 |
3.18e-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: 61.91 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 753 LGEPPAKKGLILVSPPITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLT------------IGENELRNEKEEKAE 820
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTpcmpdtyherkqVLEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 821 LNKQVVSLQQQLRFFEEKnSSLRADVEQIQASynsaVAELQTQKAVNQEQRDRILKLSQEMETAArsIESNVSQI-KQMQ 899
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQ-LKKQQLLKQLRAR----IEELRAQEAVLEETQERINRARKAAPLAA--HIKAVTQIeQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 900 TKIDELRS-LDSPSHISKIDLLNLQDLSSGAKGDNCLNTSQQ----LPGGDFSSTWVKEYHTQEISRENSFHASIEAIwE 974
Cdd:TIGR00618 311 RIHTELQSkMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSqeihIRDAHEVATSIREISCQQHTLTQHIHTLQQQK-T 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 975 ECKEIVKASSKKSHQIQGLEEQIEKLQVEvkgYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQ 1054
Cdd:TIGR00618 390 TLTQKLQSLCKELDILQREQATIDTRTSA---FRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1055 LVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDE----CKRLVELEQsileKESAILKLEANLKECE------AKHQD 1124
Cdd:TIGR00618 467 SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcplCGSCIHPNP----ARQDIDNPGPLTRRMQrgeqtyAQLET 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1125 HIRTNDLSAKEVK-----FREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANS----ILTQNLKADLQKKE 1195
Cdd:TIGR00618 543 SEEDVYHQLTSERkqrasLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSeaedMLACEQHALLRKLQ 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1196 EDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINE----LEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQ 1271
Cdd:TIGR00618 623 PEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREhalsIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQC 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1272 QYEKVCKDLSVKE--KLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADwlatELDKWKEKFKDLE-TRSNQRLNTGTMDDl 1348
Cdd:TIGR00618 703 QTLLRELETHIEEydREFNEIENASSSLGSDLAAREDALNQSLKELM----HQARTVLKARTEAhFNNNEEVTAALQTG- 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1349 dvltRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRErclKLQNEVETLTAQLAEKNSE 1428
Cdd:TIGR00618 778 ----AELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEE---QFLSRLEEKSATLGEITHQ 850
|
730 740
....*....|....*....|
gi 1907132433 1429 LQKWREERDQLVTAVETQMK 1448
Cdd:TIGR00618 851 LLKYEECSKQLAQLTQEQAK 870
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
993-1469 |
5.13e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 993 LEEQIEKLQ---VEVKGYREENSDLRAQEsqgknrdHQLKEkeslIQQLREELQEKSVSLRVQVQLVAEREQALSELSQD 1069
Cdd:COG4913 223 TFEAADALVehfDDLERAHEALEDAREQI-------ELLEP----IRELAERYAAARERLAELEYLRAALRLWFAQRRLE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1070 VtcYKAKIKDLEvivetqkdecKRLVELEQSILEKESAILKLEANLKECEAKHQDH--IRTNDLSAKEVKFREEVTRLAN 1147
Cdd:COG4913 292 L--LEAELEELR----------AELARLEAELERLEARLDALREELDELEAQIRGNggDRLEQLEREIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1148 NLHDTKQLLQSKEEENEISRQETEKLKEELAAnsiLTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREvsvmrdeek 1227
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEEFAALRAEAAA---LLEALEEELEALEEALAEAEAALRDLRRELRELEAE--------- 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1228 llrikINELEKKKNQYSQDLdmkQRTIQQLKEQLS------------------NQKMEEAV---------------QQYE 1274
Cdd:COG4913 428 -----IASLERRKSNIPARL---LALRDALAEALGldeaelpfvgelievrpeEERWRGAIervlggfaltllvppEHYA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1275 KVCK---DLSVKEKLV-EDMRLTLVEQEQTQAEQD---RVLEAKSEEA-DWLATELDKWK--------EKFKDLE---TR 1335
Cdd:COG4913 500 AALRwvnRLHLRGRLVyERVRTGLPDPERPRLDPDslaGKLDFKPHPFrAWLEAELGRRFdyvcvdspEELRRHPraiTR 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1336 SNQRLNTGTM---DD-----------------LDVLTRKFSKLQDELQESEEKY---KADRKKWLEEKAVLTTQAKEAEN 1392
Cdd:COG4913 580 AGQVKGNGTRhekDDrrrirsryvlgfdnrakLAALEAELAELEEELAEAEERLealEAELDALQERREALQRLAEYSWD 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1393 VRN-----REMRKYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQL---VTAVETQMKALLSSCKHKDEEIQEL 1464
Cdd:COG4913 660 EIDvasaeREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELkgeIGRLEKELEQAEEELDELQDRLEAA 739
|
....*
gi 1907132433 1465 RKAAA 1469
Cdd:COG4913 740 EDLAR 744
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
663-1214 |
6.41e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 663 ETEEAIACLQLKFNQVKAELAETKEELIKAQEELkNRESNSLVQALKTSSKVDTSLTSNKSTCNETSEmpknSRAQTHSE 742
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELEL-EEAQAEEYELLAELARLEQDIARLEERRRELEE----RLEELEEE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 743 RKRLNEDGLQLGEppAKKGLILVsppITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELN 822
Cdd:COG1196 325 LAELEEELEELEE--ELEELEEE---LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 823 KQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKI 902
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 903 DELRSLDSPSHISKIDLLNLQDLSSGAkgdnclntsqqlpggdfsSTWVKEYHTQEISRENSFHASIEAIWEECKE--IV 980
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGF------------------LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEaaLE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 981 KASSKKSHQI-----QGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQL 1055
Cdd:COG1196 542 AALAAALQNIvveddEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1056 VAEReqALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKE 1135
Cdd:COG1196 622 LLGR--TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907132433 1136 VKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQ 1214
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
791-1354 |
1.24e-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: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 791 RVLKEKNEELKRLltigENELRNEKEE-KAELNKQVVSLQQQLRFFEeKNSSLRADVEQIQASYNSAVAELQTQKAVNQE 869
Cdd:pfam15921 419 RELDDRNMEVQRL----EALLKAMKSEcQGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVEELTAKKMTLES 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 870 QRDRILKLSQEMETAARSIESNVSQIKQMQTKIDelrsldspshiskIDLLNLQDLSSgaKGDNCLNTSQQLPGGDFSST 949
Cdd:pfam15921 494 SERTVSDLTASLQEKERAIEATNAEITKLRSRVD-------------LKLQELQHLKN--EGDHLRNVQTECEALKLQMA 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 950 wvKEYHTQEISRENSfhasieaiwEECKEIVKASSKKSHQIQGLEEQIEKlqvEVKGYREENSDLRAQESQgknRDHQLK 1029
Cdd:pfam15921 559 --EKDKVIEILRQQI---------ENMTQLVGQHGRTAGAMQVEKAQLEK---EINDRRLELQEFKILKDK---KDAKIR 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1030 EKESLIQQLREE----LQEKSVSLRVQVQLVAEREQALSE----------LSQDVTCYKAKIKDLEVIVETQKDECKRLV 1095
Cdd:pfam15921 622 ELEARVSDLELEkvklVNAGSERLRAVKDIKQERDQLLNEvktsrnelnsLSEDYEVLKRNFRNKSEEMETTTNKLKMQL 701
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1096 ELEQSILEKEsailklEANLKECEAKHQDHIRTNDLSAKEVKF-REEVTRLANNLHDTKQLLQSKEEENEISRQETEKLK 1174
Cdd:pfam15921 702 KSAQSELEQT------RNTLKSMEGSDGHAMKVAMGMQKQITAkRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS 775
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1175 EELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVS-----VMRDEEKLLRIKINE-LEKKKNQ---YSQ 1245
Cdd:pfam15921 776 QELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAecqdiIQRQEQESVRLKLQHtLDVKELQgpgYTS 855
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1246 DLDMKQRTIQ--QLKEQLSNQKMEEAVQQY--EKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEaDWLATE 1321
Cdd:pfam15921 856 NSSMKPRLLQpaSFTRTHSNVPSSQSTASFlsHHSRKTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAED-KGRAPS 934
|
570 580 590
....*....|....*....|....*....|...
gi 1907132433 1322 LDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRK 1354
Cdd:pfam15921 935 LGALDDRVRDCIIESSLRSDICHSSSNSLQTEG 967
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
828-1484 |
1.51e-08 |
|
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: 59.84 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 828 LQQQLRFFEEKNSSLRADVE----QIQASYNSAVA----ELQTQKAVNQEQRDRILKLSQEMETaarSIESNVSQIKQMQ 899
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDikesKLGSSMNSIKTfwspELKKERALRKEEAARISVLKEQYRV---TQEENQHLQLTIQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 900 TKIDELRsldspSHISKIDLLNLQDLSSGAKGDNCLNTSQQLPGGDFSSTWVKEYHTQEIS-----------RENSFHAS 968
Cdd:pfam10174 78 ALQDELR-----AQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFllrktleemelRIETQKQT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 969 IEAIWEECKEIV-----KASSKKS--------HQIQGLEEQIEKLQVEVKGYREENSDLRaQESQGKNRDHQLKEKESLI 1035
Cdd:pfam10174 153 LGARDESIKKLLemlqsKGLPKKSgeedwertRRIAEAEMQLGHLEVLLDQKEKENIHLR-EELHRRNQLQPDPAKTKAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1036 QQLREELQEKSVSL-RVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEAN 1114
Cdd:pfam10174 232 QTVIEMKDTKISSLeRNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1115 LKECEAKHQD---HIRT--NDLSAKEVK-------------------------------FREEVTRLANNLHDTKQLLQS 1158
Cdd:pfam10174 312 LETLTNQNSDckqHIEVlkESLTAKEQRaailqtevdalrlrleekesflnkktkqlqdLTEEKSTLAGEIRDLKDMLDV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1159 KEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDC-------AELKEKFIDAKKQIE----QVQREVSVMRDEEK 1227
Cdd:pfam10174 392 KERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSsntdtalTTLEEALSEKERIIErlkeQREREDRERLEELE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1228 LLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQ------------KMEEAVQQYEKVCKDLSVKEKLVEDMRLTLV 1295
Cdd:pfam10174 472 SLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLassglkkdsklkSLEIAVEQKKEECSKLENQLKKAHNAEEAVR 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1296 EQEQTqAEQDRVLEA----KSEEADWLATELDKWKEKFKDLETRSNQRlnTGTMDDLDVLTRKFSKLQD----ELQESEE 1367
Cdd:pfam10174 552 TNPEI-NDRIRLLEQevarYKEESGKAQAEVERLLGILREVENEKNDK--DKKIAELESLTLRQMKEQNkkvaNIKHGQQ 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1368 KYKADRKKWLEEkaVLTTQAKEAENVRNREMRKYADDRErclKLQNEVETLTAQ-------LAEKNSELQKWR-EERDQL 1439
Cdd:pfam10174 629 EMKKKGAQLLEE--ARRREDNLADNSQQLQLEELMGALE---KTRQELDATKARlsstqqsLAEKDGHLTNLRaERRKQL 703
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1907132433 1440 VTAVETQMKALLSSCKHKDEEIQELRKAAAKSTGTENQTMNPKPE 1484
Cdd:pfam10174 704 EEILEMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALKRE 748
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
794-1487 |
6.47e-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: 57.67 E-value: 6.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 794 KEKNEELKRLLTIGENELRNEKEEKAELNKQvvslqqqlrffEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQrdr 873
Cdd:pfam02463 264 EEKLAQVLKENKEEEKEKKLQEEELKLLAKE-----------EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKE--- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 874 ILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQDLSSgakgdnclntsqqlpggDFSSTWVKE 953
Cdd:pfam02463 330 LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES-----------------ERLSSAAKL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 954 YHTQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKES 1033
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1034 LIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELeqsILEKESAILKLEA 1113
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGV---AVENYKVAISTAV 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1114 NLKECEAKHQDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLkadLQK 1193
Cdd:pfam02463 550 IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAK---VVE 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1194 KEEDCAELKEKFIDAKKQIEQVQREVSVMRDE-EKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQK-MEEAVQ 1271
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGLRKGVSLEEGLaEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLeIKKKEQ 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1272 QYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQ------RLNTGTM 1345
Cdd:pfam02463 707 REKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEkelaeeREKTEKL 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1346 DDLDVLTRKFSKLQDELQE--SEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCL-KLQNEVETLTAQL 1422
Cdd:pfam02463 787 KVEEEKEEKLKAQEEELRAleEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAeEELERLEEEITKE 866
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907132433 1423 AEKNSELQKWREERDQLVTAVETQMKALLSSCKHKDEEIQELRKAAAKSTGTENQTMNPKPEYND 1487
Cdd:pfam02463 867 ELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILL 931
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
791-1450 |
6.62e-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: 57.82 E-value: 6.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 791 RVLKEKNEELKRLLT-IGENELRNEKEeKAELNKQVVSLQQQLrffeeknsslradvEQIQASYNsAVAELQTQKAVNQE 869
Cdd:pfam15921 78 RVLEEYSHQVKDLQRrLNESNELHEKQ-KFYLRQSVIDLQTKL--------------QEMQMERD-AMADIRRRESQSQE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 870 Q-RDRILKLSQEMEtAARSIESNVsqIKQMQTKIDELRSLdSPSHISKidllnLQDLSSGAKgdnclntsqqlpggDFSS 948
Cdd:pfam15921 142 DlRNQLQNTVHELE-AAKCLKEDM--LEDSNTQIEQLRKM-MLSHEGV-----LQEIRSILV--------------DFEE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 949 TWVKEYHTQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREensdLRAQESQgkNRDHQL 1028
Cdd:pfam15921 199 ASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIE----LLLQQHQ--DRIEQL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1029 -KEKESLIQQLREELQE-KSVSLRVQVQLVAEREQALSELSQdvtcYKAKIKDLEVIV---ETQKDECKRLVELEQSILE 1103
Cdd:pfam15921 273 iSEHEVEITGLTEKASSaRSQANSIQSQLEIIQEQARNQNSM----YMRQLSDLESTVsqlRSELREAKRMYEDKIEELE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1104 KESAIlkleANLKECEAKHQDHirtndlsakevKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSIL 1183
Cdd:pfam15921 349 KQLVL----ANSELTEARTERD-----------QFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSIT 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1184 TQNLKADLQKKEEDCAELKEKFIDAKKQIE-QVQREVSVMRDEekllrikiNELEKKKNQYSQDLDMKQRTIQQLKEQLS 1262
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGK--------NESLEKVSSLTAQLESTKEMLRKVVEELT 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1263 NQKMeeAVQQYEKVCKDLSV----KEKLVE-------------DMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKW 1325
Cdd:pfam15921 486 AKKM--TLESSERTVSDLTAslqeKERAIEatnaeitklrsrvDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKV 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1326 KEKFKDletrsnqrlntgTMDDLDVLTRKFSKLQDELQESE---EKYKADRKKWLEEKAVLttqaKEAENVRNREMRKYA 1402
Cdd:pfam15921 564 IEILRQ------------QIENMTQLVGQHGRTAGAMQVEKaqlEKEINDRRLELQEFKIL----KDKKDAKIRELEARV 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1907132433 1403 DDrerclkLQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQMKAL 1450
Cdd:pfam15921 628 SD------LELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNEL 669
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
974-1373 |
7.39e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 7.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 974 EECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYR---------EENSDLRAQESQGKNRDHQLKEKESLIQQLREELQE 1044
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEkllqllplyQELEALEAELAELPERLEELEERLEELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1045 KSVSL-RVQVQLVAEREQALSELSQDVTCYKAKIKDLEvivetqkdecKRLVELEQSILEKESAILKLEANLKECEAKHQ 1123
Cdd:COG4717 168 LEAELaELQEELEELLEQLSLATEEELQDLAEELEELQ----------QRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1124 DHIRTNDLSAKEVKFREEVTRLA-----NNLHDTKQ---------------LLQSKEEENEISRQETEKLKEELAANSIL 1183
Cdd:COG4717 238 AAALEERLKEARLLLLIAAALLAllglgGSLLSLILtiagvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1184 TQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKllRIKINELEKKKNQYSQDLDMKqrTIQQLKEQLSN 1263
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE--ELQLEELEQEIAALLAEAGVE--DEEELRAALEQ 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1264 -QKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDrvLEAKSEEadwLATELDKWKEKFKDLETRSNQRLNT 1342
Cdd:COG4717 394 aEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEE--LEEELEE---LEEELEELREELAELEAELEQLEED 468
|
410 420 430
....*....|....*....|....*....|.
gi 1907132433 1343 GTmddLDVLTRKFSKLQDELQESEEKYKADR 1373
Cdd:COG4717 469 GE---LAELLQELEELKAELRELAEEWAALK 496
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
990-1276 |
8.18e-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: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 990 IQGLEEQIEKlqvevkgYREENSDLRAQESQgknrdHQLKEKESLIQQLREELQEKSVSLRvqvqlvaEREQALSELSQD 1069
Cdd:TIGR02169 767 IEELEEDLHK-------LEEALNDLEARLSH-----SRIPEIQAELSKLEEEVSRIEARLR-------EIEQKLNRLTLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1070 VTCYKAKIKDLEVIVETQKDeckRLVELEQSILEKESAILKLEANLKECEAkhqdhiRTNDLSAKEVKFREEVTRLANNL 1149
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKE---QIKSIEKEIENLNGKKEELEEELEELEA------ALRDLESRLGDLKKERDELEAQL 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1150 HDtkqlLQSKEEENEISRQETEKLKEELAAN-SILTQNLKADLQKKEEDCAELKEKFI--DAKKQIEQVQREVSVMRD-- 1224
Cdd:TIGR02169 899 RE----LERKIEELEAQIEKKRKRLSELKAKlEALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRVEEEIRALEPvn 974
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907132433 1225 -------EEKLLRikINELEKKKNQysqdLDMKQRTIQQLKEQLSNQKMEEAVQQYEKV 1276
Cdd:TIGR02169 975 mlaiqeyEEVLKR--LDELKEKRAK----LEEERKAILERIEEYEKKKREVFMEAFEAI 1027
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1156-1370 |
8.61e-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: 56.31 E-value: 8.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1156 LQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINE 1235
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1236 LEKKKNQYSQDLDMKQRTIQQLKEQ------LSNQKMEEAVqqyekvcKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLE 1309
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQpplallLSPEDFLDAV-------RRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907132433 1310 AKSEEADWLATELDKWKEKFKDLETRSNQRLNTgtmddLDVLTRKFSKLQDELQESEEKYK 1370
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKL-----LARLEKELAELAAELAELQQEAE 223
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1164-1437 |
1.17e-07 |
|
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: 57.00 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1164 EISRQETEKLKEElAANSILTQNLKADLQKKEEdcAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQY 1243
Cdd:TIGR02169 194 DEKRQQLERLRRE-REKAERYQALLKEKREYEG--YELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1244 SQDLDMKQRTIQQLKEQLSNQ---KMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLAT 1320
Cdd:TIGR02169 271 EQLLEELNKKIKDLGEEEQLRvkeKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1321 ELDKWKEKFKDLETRSN---QRL------NTGTMDDLDVLTRKFSKLQDELQESeekyKADRKKWLEEKAVLTTQAKEAE 1391
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEdlrAELeevdkeFAETRDELKDYREKLEKLKREINEL----KRELDRLQEELQRLSEELADLN 426
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1907132433 1392 NvrnremrKYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERD 1437
Cdd:TIGR02169 427 A-------AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
681-1263 |
1.37e-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: 56.57 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 681 ELAETKEELIKAQEELKNRE-------------------SNSLVQALKTSSK-VDTSLTSNKSTCNETSEMPKNSRAQTH 740
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEkelknldknlnkdeekinnSNNKIKILEQQIKdLNDKLKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 741 SERKRLNEDGLQLGEppAKKGLILVSPPITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAE 820
Cdd:TIGR04523 114 NDKEQKNKLEVELNK--LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 821 LNKQVVSLQQQLRFFEEKN----------SSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIES 890
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIqknkslesqiSELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 891 NVSQIKQMQTKIDELRSLdspshISKIDlLNLQDLSSGAKGDNCLNTSQQLPGGDFSSTWVKEYHTQEISRENSFHASIE 970
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQ-----LNQLK-SEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 971 AIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQ----ESQGKNRDHQLKEKESLIQQLREELQEKS 1046
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQindlESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1047 VSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECK-----------RLVELEQSILEKESAILKLEANL 1115
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsinkikqNLEQKQKELKSKEKELKKLNEEK 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1116 KECEAKHQDHIRTNDLS-AKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLK--EELAANSILTQNLKADLQ 1192
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLkEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEknKEIEELKQTQKSLKKKQE 585
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907132433 1193 KKEEDCAELKEKFIDAKKQIE-------QVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSN 1263
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKEIEekekkisSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPE 663
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
780-1303 |
1.50e-07 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 56.62 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 780 QQSVSEVVEGNRVLKEKNEELKRLLTIGENEL---RNEKEEKAELNKQVVSLQ------QQLRFFEEKNSSLRADVeqiq 850
Cdd:COG5022 771 IKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLlslLGSRKEYRSYLACIIKLQktikreKKLRETEEVEFSLKAEV---- 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 851 aSYNSAVAELQTQKAVNQEQRDRIL-----------KLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDL 919
Cdd:COG5022 847 -LIQKFGRSLKAKKRFSLLKKETIYlqsaqrvelaeRQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEF 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 920 LNlqDLSSGAKgdnclntsQQLPGGDFSSTWVKEYHTQEISRE-NSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIE 998
Cdd:COG5022 926 KT--ELIARLK--------KLLNNIDLEEGPSIEYVKLPELNKlHEVESKLKETSEEYEDLLKKSTILVREGNKANSELK 995
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 999 KLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQvQLVAEREQALSELSqdvtcykAKIK 1078
Cdd:COG5022 996 NFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQ-KLKGLLLLENNQLQ-------ARYK 1067
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1079 DLEVIVETQKDECKRLVELE-QSILEKesailklEANLKECEAKHQDHIrtndLSAKEVKFREEVTRLANNLHDTKQLLQ 1157
Cdd:COG5022 1068 ALKLRRENSLLDDKQLYQLEsTENLLK-------TINVKDLEVTNRNLV----KPANVLQFIVAQMIKLNLLQEISKFLS 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1158 SKEEENEISRQETEKLKEELAANSILTQN--------LKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEK-- 1227
Cdd:COG5022 1137 QLVNTLEPVFQKLSVLQLELDGLFWEANLealpspppFAALSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFsg 1216
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907132433 1228 -LLRIKINELEKKKNQYSQdldmkqrTIQQLKEQLSNQKmEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAE 1303
Cdd:COG5022 1217 wPRGDKLKKLISEGWVPTE-------YSTSLKGFNNLNK-KFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPAT 1285
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1016-1271 |
2.64e-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: 54.77 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1016 AQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEvivetqkdecKRLV 1095
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE----------AELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1096 ELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLsaKEVKFREEVTRLANNLHDTKQLLQSKeeeneisRQETEKLKE 1175
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPL--ALLLSPEDFLDAVRRLQYLKYLAPAR-------REQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1176 ELAANSILTQNLKADLQKKEEDCAELKEKfidaKKQIEQVQREVsvmrdeekllRIKINELEKKKNQYSQDLDMKQRTIQ 1255
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEE----RAALEALKAER----------QKLLARLEKELAELAAELAELQQEAE 223
|
250
....*....|....*.
gi 1907132433 1256 QLKEQLSNQKMEEAVQ 1271
Cdd:COG4942 224 ELEALIARLEAEAAAA 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1191-1439 |
2.87e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1191 LQKKEEDCAELKEKFIDAKKQIEQVQREVsvmrdeeKLLRIKINELEKKKNQYSQDLDMK--QRTIQQLKEQL-----SN 1263
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAEL-------DALQERREALQRLAEYSWDEIDVAsaEREIAELEAELerldaSS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1264 QKMEEAVQQYEKVCKDLSVKEKLVEDM--RLTLVEQEQTQAE------QDRVLEAKSEEADWLATELDKWKEKFKDLETR 1335
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELkgEIGRLEKELEQAEeeldelQDRLEAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1336 SNQRLNTGtmDDLDVLTRKFSKLQDELQESEEKYKADrkkWLEEKAVLTTQAKEAENVRNREMRKYADD----RERCLKL 1411
Cdd:COG4913 765 RELRENLE--ERIDALRARLNRAEEELERAMRAFNRE---WPAETADLDADLESLPEYLALLDRLEEDGlpeyEERFKEL 839
|
250 260
....*....|....*....|....*....
gi 1907132433 1412 QNevETLTAQLAEKNSELQKWREE-RDQL 1439
Cdd:COG4913 840 LN--ENSIEFVADLLSKLRRAIREiKERI 866
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1088-1437 |
3.33e-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: 55.36 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1088 KDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVKFRE------EVTRLANNLHDTKQLLQSKEE 1161
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEyllyldYLKLNEERIDLLQELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1162 ENEISRQETEKLKEELAansilTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKn 1241
Cdd:pfam02463 252 EIESSKQEIEKEEEKLA-----QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1242 qysqdldmkqrtiQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADwLATE 1321
Cdd:pfam02463 326 -------------AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLS-SAAK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1322 LDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKY 1401
Cdd:pfam02463 392 LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907132433 1402 ADDRERCLKLQNEVETLTAQLAEKNSELQKWREERD 1437
Cdd:pfam02463 472 DLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS 507
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
769-1334 |
4.67e-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: 54.64 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 769 ITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQ 848
Cdd:TIGR04523 70 INNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 849 IQASYNSAVAELQTQKAVNQEQRDRILKLSQEMEtaarSIESNVSQIKQmQTKIDELRSLDSPSHISKIDLLNLQdLSSG 928
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELENELNLLEKEKL----NIQKNIDKIKN-KLLKLELLLSNLKKKIQKNKSLESQ-ISEL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 929 AKGDNCLNTSQQLPGGDFSSTwvkeyhTQEIsreNSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYR 1008
Cdd:TIGR04523 224 KKQNNQLKDNIEKKQQEINEK------TTEI---SNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1009 EENSDLRAQESQGKNRD--HQLKEKESLIQQLREEL---QEKSVSLRVQV-QLVAEREQALSELSQDVTCYKAKIKDLEV 1082
Cdd:TIGR04523 295 SEISDLNNQKEQDWNKElkSELKNQEKKLEEIQNQIsqnNKIISQLNEQIsQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1083 IVETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVK-FREEVTRLANNLHDTKQLLQSKEE 1161
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIErLKETIIKNNSEIKDLTNQDSVKEL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1162 ENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKN 1241
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1242 QYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVED----MRLTLVEQEQTQAEQDRVLEAKSEEADW 1317
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKkqeeKQELIDQKEKEKKDLIKEIEEKEKKISS 614
|
570
....*....|....*..
gi 1907132433 1318 LATELDKWKEKFKDLET 1334
Cdd:TIGR04523 615 LEKELEKAKKENEKLSS 631
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
974-1375 |
5.25e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 974 EECKEIVKASSKKSHQIQGLEEQIEKLQvEVKGYREE--NSDLRAQESQGKNRDHQLKEKESLIQQlREELQEKSVSLRV 1051
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEkkKADEAKKKAEEAKKADEAKKKAEEAKK-AEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1052 QVQLV--AEREQALSELSQDVTCYKAKIKDLEVIVETQK--DECKRLVELEqsileKESAILKLEANLKECEAKHQDHIR 1127
Cdd:PTZ00121 1472 ADEAKkkAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkaDEAKKAEEAK-----KADEAKKAEEAKKADEAKKAEEKK 1546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1128 tndlSAKEVKFREEVtRLANNLHDTKQLLQSKEEEN------EISRQETEKLKEELAANSILTQNLKADLQKKEEDC--- 1198
Cdd:PTZ00121 1547 ----KADELKKAEEL-KKAEEKKKAEEAKKAEEDKNmalrkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkik 1621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1199 -------AELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQ-------YSQDLDMKQRTIQQLKEQLSNQ 1264
Cdd:PTZ00121 1622 aeelkkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEdkkkaeeAKKAEEDEKKAAEALKKEAEEA 1701
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1265 KMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRvleAKSEEADWLATELDKWKEKFKDLETRSNQrlntgt 1344
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK---KKAEEAKKDEEEKKKIAHLKKEEEKKAEE------ 1772
|
410 420 430
....*....|....*....|....*....|.
gi 1907132433 1345 mddldVLTRKFSKLQDELQESEEKYKADRKK 1375
Cdd:PTZ00121 1773 -----IRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
808-1486 |
6.49e-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: 54.67 E-value: 6.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 808 ENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQE---QRDRILKLSQEMETA 884
Cdd:TIGR00606 404 EDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQlegSSDRILELDQELRKA 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 885 ARSIeSNVSQIKQMQTKIDELRSLDSpshiSKIDLLnlQDLSSGAKGDNCLNTSQQLPGGDFSSTWVKEYHTQEISRENS 964
Cdd:TIGR00606 484 EREL-SKAEKNSLTETLKKEVKSLQN----EKADLD--RKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKS 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 965 FHA----SIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRaqesqgknrdHQLKEKESLIQQLRE 1040
Cdd:TIGR00606 557 RHSdeltSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHIN----------NELESKEEQLSSYED 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1041 ELQEKSVSLRVQVQLVAEREQaLSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILekesailKLEANLKECEA 1120
Cdd:TIGR00606 627 KLFDVCGSQDEESDLERLKEE-IEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVF-------QTEAELQEFIS 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1121 KHQDHIRTNDLSAKEVKfrEEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEdcae 1200
Cdd:TIGR00606 699 DLQSKLRLAPDKLKSTE--SELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQET---- 772
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1201 LKEKFIDAKKQIEQVQREVSVMRDeeklLRIKINELEKKKNQYSQDLDMK--QRTIQQLkeqlsNQKMEEAVQQYEKVCK 1278
Cdd:TIGR00606 773 LLGTIMPEEESAKVCLTDVTIMER----FQMELKDVERKIAQQAAKLQGSdlDRTVQQV-----NQEKQEKQHELDTVVS 843
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1279 DLSVKEKLVEDmrltlvEQEQTQAEQDRVLEAKSEEADwLATELDKWKEKFKDLETRSN--QRLNTGTMDDLDVLTRKFS 1356
Cdd:TIGR00606 844 KIELNRKLIQD------QQEQIQHLKSKTNELKSEKLQ-IGTNLQRRQQFEEQLVELSTevQSLIREIKDAKEQDSPLET 916
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1357 KLQDELQESEE---KYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCLK-LQNEVETLTAQLAEKNSELQKW 1432
Cdd:TIGR00606 917 FLEKDQQEKEElisSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKqKETELNTVNAQLEECEKHQEKI 996
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907132433 1433 REERDQLVTAVETQ------MKALLSSCKHKDE--EIQELRKAAAKSTGtENQTMNPKPEYN 1486
Cdd:TIGR00606 997 NEDMRLMRQDIDTQkiqerwLQDNLTLRKRENElkEVEEELKQHLKEMG-QMQVLQMKQEHQ 1057
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1177-1435 |
9.98e-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: 52.84 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1177 LAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQ 1256
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1257 LKEQLSNQKmeeavQQYEKVckdLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLEtrs 1336
Cdd:COG4942 95 LRAELEAQK-----EELAEL---LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1337 nqrlntgtmddldvltrkfsKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVE 1416
Cdd:COG4942 164 --------------------ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250
....*....|....*....
gi 1907132433 1417 TLTAQLAEKNSELQKWREE 1435
Cdd:COG4942 224 ELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
827-1045 |
1.14e-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: 52.84 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 827 SLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELR 906
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 907 SLDSpshiskiDLLNLQDLSSGAKGDNCLNTSQQLPGGDFSSTWVKEYHTQEISRENSFHASIEAIWEECKEIVKASSKK 986
Cdd:COG4942 104 EELA-------ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907132433 987 SHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEK 1045
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
968-1416 |
1.14e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 968 SIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLraqeSQGKNRDHQLKEKESLIQQLREELQEKSV 1047
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL----EEKEERLEELKKKLKELEKRLEELEERHE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1048 SLRVQVQLVAEREQALSELS-QDVTCYKAKIKDLEVIVETQKDECK----RLVELEQSILEKESAILKLEANLKEC---- 1118
Cdd:PRK03918 363 LYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISkitaRIGELKKEIKELKKAIEELKKAKGKCpvcg 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1119 ---EAKHQDHIrTNDLSAKEVKFREEVTRLANNLHDTKQLLqsKEEENEISRQET----EKLKEEL-AANSILTQNLKAD 1190
Cdd:PRK03918 443 relTEEHRKEL-LEEYTAELKRIEKELKEIEEKERKLRKEL--RELEKVLKKESEliklKELAEQLkELEEKLKKYNLEE 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1191 LQKKEEDCAELKEKFIDAKKQIEQVQREVSvmrdeekllriKINELEKKKnqysQDLDMKQRTIQQLKEQLSNQKMEEAV 1270
Cdd:PRK03918 520 LEKKAEEYEKLKEKLIKLKGEIKSLKKELE-----------KLEELKKKL----AELEKKLDELEEELAELLKELEELGF 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1271 QQYEKVCKDLSVKEKLVEDMrLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNTGTMDDLDV 1350
Cdd:PRK03918 585 ESVEELEERLKELEPFYNEY-LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE 663
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907132433 1351 LTRKFSKLQDE----------LQESEEKYKADRKKWLEEKAVLTTQAKEAENVrNREMRKYADDRERCLKLQNEVE 1416
Cdd:PRK03918 664 LREEYLELSRElaglraeleeLEKRREEIKKTLEKLKEELEEREKAKKELEKL-EKALERVEELREKVKKYKALLK 738
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
989-1275 |
1.24e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.22 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 989 QIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKeslIQQLREELQEKSVSLRVQVQLVAEREQALSELsq 1068
Cdd:COG1340 9 SLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQ---VKELREEAQELREKRDELNEKVKELKEERDEL-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1069 dvtcyKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEanlkeceakhqDHIRTNDLS-AKEVKFREEVTRLAN 1147
Cdd:COG1340 84 -----NEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLE-----------WRQQTEVLSpEEEKELVEKIKELEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1148 NLHDTKQLLQSKEEENEIsRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEK 1227
Cdd:COG1340 148 ELEKAKKALEKNEKLKEL-RAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKAD 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1907132433 1228 LLRIKINELEKKKNQYSQDLD-MKQRTIQQLKEQLSNQKMEEAVQQYEK 1275
Cdd:COG1340 227 ELHEEIIELQKELRELRKELKkLRKKQRALKREKEKEELEEKAEEIFEK 275
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1190-1461 |
2.94e-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: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1190 DLQKKEEDCAELKEK--------FIDAKKQIEQVQREVSVMRDeekllrikineLEKKKNQYSQDL-DMKQRTIQQLK-- 1258
Cdd:pfam15921 89 DLQRRLNESNELHEKqkfylrqsVIDLQTKLQEMQMERDAMAD-----------IRRRESQSQEDLrNQLQNTVHELEaa 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1259 EQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQA----EQD---------------RVLEAKSEEADWLA 1319
Cdd:pfam15921 158 KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGkkiyEHDsmstmhfrslgsaisKILRELDTEISYLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1320 TELDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMR 1399
Cdd:pfam15921 238 GRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR 317
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907132433 1400 KYADDRERCLKLQNE-----------VETLTAQLAEKNSELQKWREERDQLVTA---VETQMKALLSSCKHKDEEI 1461
Cdd:pfam15921 318 QLSDLESTVSQLRSElreakrmyedkIEELEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLHKREKEL 393
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1023-1471 |
3.73e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1023 NRDHQLKEKEsLIQQLREELQEKSVSLRVQVQlvAEREQALSELSQDVTCYKAKIKDlevivETQKDECKRLVELEQSIL 1102
Cdd:PTZ00121 1037 NNDDVLKEKD-IIDEDIDGNHEGKAEAKAHVG--QDEGLKPSYKDFDFDAKEDNRAD-----EATEEAFGKAEEAKKTET 1108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1103 EK-ESAILKLEANLKECEAKHQDHIRtndlSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANS 1181
Cdd:PTZ00121 1109 GKaEEARKAEEAKKKAEDARKAEEAR----KAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKA 1184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1182 ILTQnlKADLQKKEEDCaelkeKFIDAKKQIEQVQR--EVSVMRDEEKLLRIKINELEKKKNQYSQDLDmKQRTIQQLKE 1259
Cdd:PTZ00121 1185 EEVR--KAEELRKAEDA-----RKAEAARKAEEERKaeEARKAEDAKKAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRK 1256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1260 QLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSE-EADWLATELDKWKEKFKDLETRSNQ 1338
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAKKKADAAKK 1336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1339 RLNTGTMDDlDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRN-REMRKYADDRErclKLQNEVET 1417
Cdd:PTZ00121 1337 KAEEAKKAA-EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKaDEAKKKAEEDK---KKADELKK 1412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907132433 1418 LTAQlAEKNSELQKWREER---DQLVTAVETQMKAllSSCKHKDEEIQELRKAAAKS 1471
Cdd:PTZ00121 1413 AAAA-KKKADEAKKKAEEKkkaDEAKKKAEEAKKA--DEAKKKAEEAKKAEEAKKKA 1466
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
961-1106 |
5.15e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 961 RENSFHASIEAIWEECKEIVK-----ASSKKSHQIQGLEEQIEKLQVEV-KGYREENSDLRAQESQGKNRDHQLKEKESL 1034
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEeakkeAEAIKKEALLEAKEEIHKLRNEFeKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907132433 1035 IQQLREELQEKSVSLRVQVQLVAEREQALSELsqdvtcYKAKIKDLEVIVETQKDECKRLVeLEQsiLEKES 1106
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEEL------IEEQLQELERISGLTAEEAKEIL-LEK--VEEEA 167
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
981-1451 |
5.15e-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: 51.51 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 981 KASSKKSHQIQGLEEQIEKLQVE--VKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSvslrvqvqlvaE 1058
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLCTPcmPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQL-----------K 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1059 REQALSELSQDVTCYKAKIKDLEVIVETQKDECK--RLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEV 1136
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQEAVLEETQERINRARKaaPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1137 KFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAE---------------- 1200
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKEldilqreqatidtrts 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1201 ----LKEKFIDAKKQIEQVQREVSVMR-------DEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKE--QLSNQKME 1267
Cdd:TIGR00618 418 afrdLQGQLAHAKKQQELQQRYAELCAaaitctaQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRkkAVVLARLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1268 EAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADwLATELDKWKEKFKDLETRSnqrlnTGTMDD 1347
Cdd:TIGR00618 498 ELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEED-VYHQLTSERKQRASLKEQM-----QEIQQS 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1348 LDVLTRKFSKLQDELqESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEKNS 1427
Cdd:TIGR00618 572 FSILTQCDNRSKEDI-PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHA 650
|
490 500
....*....|....*....|....
gi 1907132433 1428 ELQKWREERDQLVTAVETQMKALL 1451
Cdd:TIGR00618 651 LQLTLTQERVREHALSIRVLPKEL 674
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1073-1470 |
5.39e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1073 YKAKIKDLEVIVETQKDECK-RLVELEQSILEKESAILkleanlkeceakhqdHIRTNDLSAKEVKFREEVTRLANN--- 1148
Cdd:PRK02224 167 YRERASDARLGVERVLSDQRgSLDQLKAQIEEKEEKDL---------------HERLNGLESELAELDEEIERYEEQreq 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1149 LHDTKQLLQSKEEENEISRQETEKLKEELAansiltqNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKL 1228
Cdd:PRK02224 232 ARETRDEADEVLEEHEERREELETLEAEIE-------DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1229 -------LRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNqkMEEAVQQYEKVCKDLSVK----EKLVEDMRLTLVEQ 1297
Cdd:PRK02224 305 ddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAES--LREDADDLEERAEELREEaaelESELEEAREAVEDR 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1298 EQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLEtrsnqrlntgtmDDLDVLTRKFSKLQDELQESEEKYKADRKKWL 1377
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR------------EERDELREREAELEATLRTARERVEEAEALLE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1378 EEKAVLTTQ-AKEAENVRNREmrkyaDDRERCLKLQNEVETLTAQ-------------LAEKNSELQKWREERDQLV--- 1440
Cdd:PRK02224 451 AGKCPECGQpVEGSPHVETIE-----EDRERVEELEAELEDLEEEveeveerleraedLVEAEDRIERLEERREDLEeli 525
|
410 420 430
....*....|....*....|....*....|....*..
gi 1907132433 1441 ----TAVETQMKALLSSCKHKDE---EIQELRKAAAK 1470
Cdd:PRK02224 526 aerrETIEEKRERAEELRERAAEleaEAEEKREAAAE 562
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1004-1272 |
6.28e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1004 VKGYREENSDLRAQESqgknrdhqlkekESLIQQLREELQEksvsLRVQVQlvaEREQALSELSQdvtcyKAKIKDLEvi 1083
Cdd:COG3206 158 AEAYLEQNLELRREEA------------RKALEFLEEQLPE----LRKELE---EAEAALEEFRQ-----KNGLVDLS-- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1084 vETQKDECKRLVELEQSILEKESAILKLEANLKECEAKhqdhIRTNDLSAKEVKFREEVTRLANnlhdtkQLLQSKEEEN 1163
Cdd:COG3206 212 -EEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ----LGSGPDALPELLQSPVIQQLRA------QLAELEAELA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1164 EISRQETEK------LKEELAAnsiltqnLKADLQkkeedcAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELE 1237
Cdd:COG3206 281 ELSARYTPNhpdviaLRAQIAA-------LRAQLQ------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELP 347
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907132433 1238 KKKNQYSQ---DLDMKQRTIQQLKEQLSNQKMEEAVQQ 1272
Cdd:COG3206 348 ELEAELRRlerEVEVARELYESLLQRLEEARLAEALTV 385
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
982-1239 |
7.36e-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: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 982 ASSKKSHQIQGLEEQIEKLQVEVKgyrEENSDLRAQESQGKNRDHQLKEKESLIQQLREELQeksvslrvqvqlvaEREQ 1061
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIA---ELEKELAALKKEEKALLKQLAALERRIAALARRIR--------------ALEQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1062 ALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANlkeceaKHQDHIRTNDLSAKEVKFREE 1141
Cdd:COG4942 77 ELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPE------DFLDAVRRLQYLKYLAPARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1142 vtrLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsiLTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQRevsv 1221
Cdd:COG4942 151 ---QAEELRADLAELAALRAELEAERAELEALLAELEE---ERAALEALKAERQKLLARLEKELAELAAELAELQQ---- 220
|
250
....*....|....*...
gi 1907132433 1222 mrdEEKLLRIKINELEKK 1239
Cdd:COG4942 221 ---EAEELEALIARLEAE 235
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1245-1473 |
1.04e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1245 QDLDMKQRTIQQLKEQLSN-QKMEEAVQQYEKVCKDLSVKEKLVEdmRLTLVEQEQTQAEQDRVLEAKSEEADWLATELD 1323
Cdd:COG4913 235 DDLERAHEALEDAREQIELlEPIRELAERYAAARERLAELEYLRA--ALRLWFAQRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1324 KWKEKFKDLETR----SNQRLNTGTmDDLDVLTRKFSKLQDELQESEEKYK--ADRKKWLEEKAVLTTQA-KEAENVRNR 1396
Cdd:COG4913 313 RLEARLDALREEldelEAQIRGNGG-DRLEQLEREIERLERELEERERRRArlEALLAALGLPLPASAEEfAALRAEAAA 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907132433 1397 EMRKYADDRERclkLQNEVETLTAQLAEKNSELQKWREERDQLvtavETQMKALlssckhkDEEIQELRKAAAKSTG 1473
Cdd:COG4913 392 LLEALEEELEA---LEEALAEAEAALRDLRRELRELEAEIASL----ERRKSNI-------PARLLALRDALAEALG 454
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1238-1470 |
1.16e-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: 49.76 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1238 KKKNQYSQDLDMKQRTIQQLKEQLSNQKmeeavQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADW 1317
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALK-----KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1318 LATELDKWKEKFKDLeTRSNQR----------LNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQa 1387
Cdd:COG4942 95 LRAELEAQKEELAEL-LRALYRlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1388 keaenvrnremrkyaddrerclklQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQMKALLSSCKHKDEEIQELRKA 1467
Cdd:COG4942 173 ------------------------RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
...
gi 1907132433 1468 AAK 1470
Cdd:COG4942 229 IAR 231
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
678-895 |
2.21e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 678 VKAELAETKEELIKAQEELKN-RESNSLVQALKTSSKVDTSLTSNKSTCNETsempknsRAQTHSERKRLNEDGLQLGEP 756
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEfRQKNGLVDLSEEAKLLLQQLSELESQLAEA-------RAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 757 PAKKGLILVSPPITEEQNKMGEMQQSVSEVVEG---------------NRVLKEKNEELKRLLTIGENELRNEKEEKAEL 821
Cdd:COG3206 253 PDALPELLQSPVIQQLRAQLAELEAELAELSARytpnhpdvialraqiAALRAQLQQEAQRILASLEAELEALQAREASL 332
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907132433 822 NKQVVSLQQQLrffeeknsslrADVEQIQASYNsavaELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQI 895
Cdd:COG3206 333 QAQLAQLEARL-----------AELPELEAELR----RLEREVEVARELYESLLQRLEEARLAEALTVGNVRVI 391
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
788-1334 |
2.31e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 788 EGNRVLKEKNEELKRLLTIGE--NELRNEKE----EKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQ 861
Cdd:PRK02224 238 EADEVLEEHEERREELETLEAeiEDLRETIAeterEREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 862 TQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSldspshiskidllNLQDLSSGAKgdnclNTSQQL 941
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE-------------EAAELESELE-----EAREAV 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 942 pggdfsstwvkeyhtqeisreNSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQG 1021
Cdd:PRK02224 380 ---------------------EDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTA 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1022 KNRdhqLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDeckrLVELE--- 1098
Cdd:PRK02224 439 RER---VEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED----LVEAEdri 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1099 QSILEKESAILKLEANLKEceakhqdhiRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELA 1178
Cdd:PRK02224 512 ERLEERREDLEELIAERRE---------TIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1179 ANsiltqnlkadlqkKEEdcaelkekfIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLK 1258
Cdd:PRK02224 583 EL-------------KER---------IESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELE 640
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907132433 1259 EQLSNQKMEEAVQQYEKVCKDLsvkEKLVEDMRLTLVEQEQTQAEQDRVlEAKSEEADWLATELDKWKEKFKDLET 1334
Cdd:PRK02224 641 AEFDEARIEEAREDKERAEEYL---EQVEEKLDELREERDDLQAEIGAV-ENELEELEELRERREALENRVEALEA 712
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
803-1273 |
2.37e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 803 LLTIGENELRNEKEE-------KAELN-KQVVSLQQQLRFFEEKNSSLRADVEQIQaSYNSAVAELQTQKAVNQEQRDRI 874
Cdd:COG4717 43 IRAMLLERLEKEADElfkpqgrKPELNlKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 875 LKLSQ------EMETAARSIESNVSQIKQMQTKIDELRSLdspshISKIDLLNLQdlssgakgdnclntsqqlpggdfss 948
Cdd:COG4717 122 EKLLQllplyqELEALEAELAELPERLEELEERLEELREL-----EEELEELEAE------------------------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 949 twVKEYHTQEISRENSFHASIEAIWEECKEivkasskkshQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQL 1028
Cdd:COG4717 172 --LAELQEELEELLEQLSLATEEELQDLAE----------ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1029 KEKESLIQQLRE--------ELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQS 1100
Cdd:COG4717 240 ALEERLKEARLLlliaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1101 ILEKESAILKLEANLKECEAKHQ-DHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENE--------ISRQETE 1171
Cdd:COG4717 320 ELEELLAALGLPPDLSPEELLELlDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEeelraaleQAEEYQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1172 KLKEELAANSILTQNLKADLQKKE-EDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKkknqySQDLDMK 1250
Cdd:COG4717 400 LKEELEELEEQLEELLGELEELLEaLDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE-----DGELAEL 474
|
490 500
....*....|....*....|...
gi 1907132433 1251 QRTIQQLKEQLSNQKMEEAVQQY 1273
Cdd:COG4717 475 LQELEELKAELRELAEEWAALKL 497
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
993-1327 |
2.46e-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: 48.74 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 993 LEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREEL-------------------------QEKSV 1047
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELrqsrekheeleekykelsasseelsEEKDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1048 SLRVQvqlvAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLV-ELEQSILEKESAILKLEANLKECEAKHQDHI 1126
Cdd:pfam07888 120 LLAQR----AAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGaQRKEEEAERKQLQAKLQQTEEELRSLSKEFQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1127 RTNDLSAKE----VKFREEVTRLANNLHDTKQllqsKEEENEISRQETEKLKEELAANSILTQNLKADLQkkeedcaelk 1202
Cdd:pfam07888 196 ELRNSLAQRdtqvLQLQDTITTLTQKLTTAHR----KEAENEALLEELRSLQERLNASERKVEGLGEELS---------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1203 ekfiDAKKQIEQVQREVSVMRDEEKLLRIKINE----LEKKKNQYSQDLDMKQRTIQQLKEQLSN-----QKMEEAVQQ- 1272
Cdd:pfam07888 262 ----SMAAQRDRTQAELHQARLQAAQLTLQLADaslaLREGRARWAQERETLQQSAEADKDRIEKlsaelQRLEERLQEe 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907132433 1273 ------------YEKVCKDLSVKEKLVE------DMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELD-KWKE 1327
Cdd:pfam07888 338 rmereklevelgREKDCNRVQLSESRRElqelkaSLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVADaKWSE 411
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1200-1450 |
3.50e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1200 ELKEKFIDAKKQIEQVQREVS---------VMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLsnQKMEEAV 1270
Cdd:PRK02224 166 EYRERASDARLGVERVLSDQRgsldqlkaqIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETR--DEADEVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1271 QQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEqdrvleakseeadwLATELDKWKEKFKDLETRSNQRLNTGTMDDLDV 1350
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETEREREE--------------LAEEVRDLRERLEELEEERDDLLAEAGLDDADA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1351 LTrkFSKLQDELQESEEKYkadRKKWLEEKAVLTTQAKEAENVRNRemrkyADDRE-RCLKLQNEVETLTAQLAEKNSEL 1429
Cdd:PRK02224 310 EA--VEARREELEDRDEEL---RDRLEECRVAAQAHNEEAESLRED-----ADDLEeRAEELREEAAELESELEEAREAV 379
|
250 260
....*....|....*....|.
gi 1907132433 1430 QKWREERDQLVTAVETQMKAL 1450
Cdd:PRK02224 380 EDRREEIEELEEEIEELRERF 400
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1015-1439 |
5.34e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.25 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1015 RAQESQGKNrDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDeckRL 1094
Cdd:pfam01576 16 KVKERQQKA-ESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEE---RS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1095 VELEQSILEKESAILKLEANLKECEAKHQD-HIRTNDLSAKEVKFREEVTRLA---NNLHDTKQLLQskEEENEISRQET 1170
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLDEEEAARQKlQLEKVTTEAKIKKLEEDILLLEdqnSKLSKERKLLE--ERISEFTSNLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1171 EK--------------------LKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLR 1230
Cdd:pfam01576 170 EEeekakslsklknkheamisdLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAAL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1231 IKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAvqQYEKVCKDLS-----VKEKLVEDMRLTLVEQEQTQAEQD 1305
Cdd:pfam01576 250 ARLEEETAQKNNALKKIRELEAQISELQEDLESERAARN--KAEKQRRDLGeeleaLKTELEDTLDTTAAQQELRSKREQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1306 RVLEAK---SEEADWLATELDKWKEK-FKDLETRSNQ-----RLNTGTMDDLDVLTRKFSKLQDELQE-SEEKYKADRKK 1375
Cdd:pfam01576 328 EVTELKkalEEETRSHEAQLQEMRQKhTQALEELTEQleqakRNKANLEKAKQALESENAELQAELRTlQQAKQDSEHKR 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907132433 1376 WLEEKAVLTTQAKEAENVRNRemrkyADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQL 1439
Cdd:pfam01576 408 KKLEGQLQELQARLSESERQR-----AELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSL 466
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1129-1344 |
5.51e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1129 NDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsiltqnLKADLQKKEEdcaELKEKFIDA 1208
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE-------AEAEIEERRE---ELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1209 KKQ-------------------IEQVQREVSVMRDEEKLLRiKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQK--ME 1267
Cdd:COG3883 96 YRSggsvsyldvllgsesfsdfLDRLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAAKaeLE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907132433 1268 EAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNTGT 1344
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
810-907 |
5.68e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 47.27 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 810 ELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAE---LQTQKAVNQEQRD----RILKLSQEME 882
Cdd:PRK09039 47 EISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAErsrLQALLAELAGAGAaaegRAGELAQELD 126
|
90 100
....*....|....*....|....*
gi 1907132433 883 TAARSIESNVSQIKQMQTKIDELRS 907
Cdd:PRK09039 127 SEKQVSARALAQVELLNQQIAALRR 151
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
971-1453 |
5.73e-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: 48.30 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 971 AIWEECKEIVKASSKKSHQIQGLEEQIE-------KLQVEVKGYREensDLRAQESQGKNRDHQLKEKESLIQQLREELQ 1043
Cdd:pfam12128 224 EHWIRDIQAIAGIMKIRPEFTKLQQEFNtlesaelRLSHLHFGYKS---DETLIASRQEERQETSAELNQLLRTLDDQWK 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1044 EKSVSLR------------VQVQLVAEREQALSELSQDVTCYKAKIKDLEVI---VETQKDECKRLVELEQSILEKESA- 1107
Cdd:pfam12128 301 EKRDELNgelsaadaavakDRSELEALEDQHGAFLDADIETAAADQEQLPSWqseLENLEERLKALTGKHQDVTAKYNRr 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1108 --------------ILKLEANLKECEAKHQDHIRtNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEEneisrqetekL 1173
Cdd:pfam12128 381 rskikeqnnrdiagIKDKLAKIREARDRQLAVAE-DDLQALESELREQLEAGKLEFNEEEYRLKSRLGE----------L 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1174 KEELAAnSILTQNLKADLQKKEEDCAELKEKfidakkqIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRT 1253
Cdd:pfam12128 450 KLRLNQ-ATATPELLLQLENFDERIERAREE-------QEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSA 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1254 IQQLKEQLSNQK-------MEEAVQQYEKVCKDLSVKEKLVEDMRLTLVE---------------------------QEQ 1299
Cdd:pfam12128 522 LDELELQLFPQAgtllhflRKEAPDWEQSIGKVISPELLHRTDLDPEVWDgsvggelnlygvkldlkridvpewaasEEE 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1300 TQAEQDRVLEA------KSEEADWLATELDKWKEKFKDLETRSNQRLNtGTMDDLDVLTRKFSKLQDELQESEEKYKADR 1373
Cdd:pfam12128 602 LRERLDKAEEAlqsareKQAAAEEQLVQANGELEKASREETFARTALK-NARLDLRRLFDEKQSEKDKKNKALAERKDSA 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1374 KKWLE----EKAVLTTQAKEAENVRNREMRKYAddRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQMKA 1449
Cdd:pfam12128 681 NERLNsleaQLKQLDKKHQAWLEEQKEQKREAR--TEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKR 758
|
....
gi 1907132433 1450 LLSS 1453
Cdd:pfam12128 759 DLAS 762
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
989-1179 |
6.47e-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: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 989 QIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNR----DHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALS 1064
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRiralEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1065 ELSQ------------------DVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANLKEceakhqdhi 1126
Cdd:COG4942 115 RLGRqpplalllspedfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE--------- 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907132433 1127 RTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAA 1179
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
533-1311 |
8.17e-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: 47.53 E-value: 8.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 533 LVEDLEENEETQNmETELTDEDSDKSLEECRVSTCHKKNKELLDLIEKLNKRLINENKEKLTLELKIREEVTQEFTQYWS 612
Cdd:pfam12128 202 IVAILEDDGVVPP-KSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 613 QRE--ADFKETLLH-EREILEENAERRLAIF--KDLVGKCDSQdeptnricdIELETEEAIACLQLKFNQVKAELaeTKE 687
Cdd:pfam12128 281 RQEtsAELNQLLRTlDDQWKEKRDELNGELSaaDAAVAKDRSE---------LEALEDQHGAFLDADIETAAADQ--EQL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 688 ELIKAQEELKNRESNSLVQAL-KTSSKVDTSLTSNKSTCNETSEMPKNSRAQTHSERKRLN---EDGLQLGEPPAKKgli 763
Cdd:pfam12128 350 PSWQSELENLEERLKALTGKHqDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLavaEDDLQALESELRE--- 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 764 lvsppiteeqnkmgEMQQSVSEVVEGNRVLKEKNEELKRLL---TIGENELRNE----------KEEKAELNKQVVSLQQ 830
Cdd:pfam12128 427 --------------QLEAGKLEFNEEEYRLKSRLGELKLRLnqaTATPELLLQLenfderieraREEQEAANAEVERLQS 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 831 QLRffeeknsslradveQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSqiKQMQTKIDELRSLDS 910
Cdd:pfam12128 493 ELR--------------QARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLR--KEAPDWEQSIGKVIS 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 911 PSHISKIDLLNLQDLSSGAKGDNCLNTSQQLPGGDFsstwvkeyhtqeisreNSFHASIEAIWEECKEIVKASSKKSHQI 990
Cdd:pfam12128 557 PELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDV----------------PEWAASEEELRERLDKAEEALQSAREKQ 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 991 QGLEEQIEKLQVEVKGYREENSDLR-----AQESQGKNRDHQLKEKESLIQQLREELQ---EKSVSLRVQVQLVAEREQA 1062
Cdd:pfam12128 621 AAAEEQLVQANGELEKASREETFARtalknARLDLRRLFDEKQSEKDKKNKALAERKDsanERLNSLEAQLKQLDKKHQA 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1063 LSELSQD--VTCYKAKIKDLEVIVETQKDECKRLVEleqsilEKESAILKLEANLKECE--------AKHQDHIRTNDLS 1132
Cdd:pfam12128 701 WLEEQKEqkREARTEKQAYWQVVEGALDAQLALLKA------AIAARRSGAKAELKALEtwykrdlaSLGVDPDVIAKLK 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1133 AKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQeteKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQI 1212
Cdd:pfam12128 775 REIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRP---RLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKAS 851
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1213 EQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYekVCKDLSVKEKLvedMRL 1292
Cdd:pfam12128 852 EKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKY--VEHFKNVIADH---SGS 926
|
810
....*....|....*....
gi 1907132433 1293 TLVEQEQTQAEQDRVLEAK 1311
Cdd:pfam12128 927 GLAETWESLREEDHYQNDK 945
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
989-1170 |
8.25e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 989 QIQGLEEQIEKLQVEVKGYREENSDLRAQEsQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQ 1068
Cdd:COG3206 183 QLPELRKELEEAEAALEEFRQKNGLVDLSE-EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1069 D--VTCYKAKIKDLE-----------------VIVETQKDECKRLV--ELEQSILEKESAILKLEANLKECEAKHQDH-I 1126
Cdd:COG3206 262 SpvIQQLRAQLAELEaelaelsarytpnhpdvIALRAQIAALRAQLqqEAQRILASLEAELEALQAREASLQAQLAQLeA 341
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907132433 1127 RTNDLSAKEVKFReEVTRLANNLHDTKQLLQSKEEENEISRQET 1170
Cdd:COG3206 342 RLAELPELEAELR-RLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1190-1446 |
1.22e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1190 DLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQkmeeA 1269
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER----A 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1270 VQQYEkvckdlsvkeklvEDMRLTLVEQeqtqaeqdrVLEAKSeeadwlateldkwkekFKDLETRsnqrlntgtMDDLD 1349
Cdd:COG3883 93 RALYR-------------SGGSVSYLDV---------LLGSES----------------FSDFLDR---------LSALS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1350 VLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEKNSEL 1429
Cdd:COG3883 126 KIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
250
....*....|....*..
gi 1907132433 1430 QKWREERDQLVTAVETQ 1446
Cdd:COG3883 206 AAAEAAAAAAAAAAAAA 222
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
792-1368 |
1.36e-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: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 792 VLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEK----NSSLRADVEQIQASYNSAVAELQTQKAVN 867
Cdd:pfam15921 261 LLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQarnqNSMYMRQLSDLESTVSQLRSELREAKRMY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 868 Q---EQRDRILKLSQEMETAARSIESNVSQikQMQTKIDELRSLDSPSHISKIDLlnlqdlsSGAKGDNclntsQQLPGG 944
Cdd:pfam15921 341 EdkiEELEKQLVLANSELTEARTERDQFSQ--ESGNLDDQLQKLLADLHKREKEL-------SLEKEQN-----KRLWDR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 945 DFSSTWVKEYHTQEISRENSFHASIEAIWEECK-EIVKASSKKSHQIQGLEEQIEKLqvevkgyreenSDLRAQesqgkn 1023
Cdd:pfam15921 407 DTGNSITIDHLRRELDDRNMEVQRLEALLKAMKsECQGQMERQMAAIQGKNESLEKV-----------SSLTAQ------ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1024 rdhqLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVE------- 1096
Cdd:pfam15921 470 ----LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNegdhlrn 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1097 -------LEQSILEKESAILKLEANLKECEAKHQDHIRT-NDLSAKEVKFREEVTRLANNLHDTKQLLQSK-----EEEN 1163
Cdd:pfam15921 546 vqteceaLKLQMAEKDKVIEILRQQIENMTQLVGQHGRTaGAMQVEKAQLEKEINDRRLELQEFKILKDKKdakirELEA 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1164 EISRQETEKLKeELAANSILTQNLKADLQKKEEDCAELKekfiDAKKQIEQVQREVSVMRdeeKLLRIKINELEKKKNQY 1243
Cdd:pfam15921 626 RVSDLELEKVK-LVNAGSERLRAVKDIKQERDQLLNEVK----TSRNELNSLSEDYEVLK---RNFRNKSEEMETTTNKL 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1244 SQDLDMKQRTIQQLKEQLsnQKMEEAVQQYEKVC----KDLSVKEKLVEDM--RLTLVEQEQTQAEQDR--VLEAK---S 1312
Cdd:pfam15921 698 KMQLKSAQSELEQTRNTL--KSMEGSDGHAMKVAmgmqKQITAKRGQIDALqsKIQFLEEAMTNANKEKhfLKEEKnklS 775
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907132433 1313 EEADWLATELDKWKEKFKDLETRSnQRLNTGTMD---DLDVLTRKFSKLQDELQESEEK 1368
Cdd:pfam15921 776 QELSTVATEKNKMAGELEVLRSQE-RRLKEKVANmevALDKASLQFAECQDIIQRQEQE 833
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1206-1466 |
1.45e-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: 46.66 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1206 IDAKKQIEQVQREVSVMRDEeklLRIKINELEKKKNQYSQDL---DMKQRTIQQLKEQLSNQKMEEAV--QQYEKVCKDL 1280
Cdd:pfam17380 236 MERRKESFNLAEDVTTMTPE---YTVRYNGQTMTENEFLNQLlhiVQHQKAVSERQQQEKFEKMEQERlrQEKEEKAREV 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1281 SVKEKLVEDMRLTLVE---QEQTQAEQDRVLEAKSEEADWLATEldkwkEKFKDLETRSNQRL--NTGTMDDLDVLT--- 1352
Cdd:pfam17380 313 ERRRKLEEAEKARQAEmdrQAAIYAEQERMAMERERELERIRQE-----ERKRELERIRQEEIamEISRMRELERLQmer 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1353 -RKFSKLQDELqESEEKYK---ADRKKWLEEKAVLTTQA-KEAENVRNREMRKYADDRERCL--------KLQNEVETLT 1419
Cdd:pfam17380 388 qQKNERVRQEL-EAARKVKileEERQRKIQQQKVEMEQIrAEQEEARQREVRRLEEERAREMervrleeqERQQQVERLR 466
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1907132433 1420 AQLAE-KNSELQKWREERDQLVTAVETQMKALLSSCKHKDEEIQELRK 1466
Cdd:pfam17380 467 QQEEErKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERK 514
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
521-1362 |
1.55e-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: 46.58 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 521 ENSLEDVLENEDLVEDLEeNEETQNMETELTDEDSDKSLEECRVSTCHKKNKELLDLIEKLNKRLINENKEKLTLELKI- 599
Cdd:TIGR00606 251 KNRLKEIEHNLSKIMKLD-NEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELe 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 600 -----REEVTQEFTQYWSQREADFKETLLHEREILEENAERrlaifkdLVGKCDSQDEPTNRICDIELETEEAIaclqlk 674
Cdd:TIGR00606 330 klnkeRRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLI-------QSLATRLELDGFERGPFSERQIKNFH------ 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 675 fnqvkaelaETKEELIKAQEELKNRESNSLVQALKTSSKVDTSLTSNKSTCNETSEMPKNSRAQTHSERKRLNEDGLQLg 754
Cdd:TIGR00606 397 ---------TLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQL- 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 755 ePPAKKGLILVSPPITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTigeneLRNEKEEKAELNKQVVSLQQQLRF 834
Cdd:TIGR00606 467 -EGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRK-----LRKLDQEMEQLNHHTTTRTQMEML 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 835 FEEKNSSLRaDVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQE---METAARSIESNVSQIKQMQTKI-DELRSLDS 910
Cdd:TIGR00606 541 TKDKMDKDE-QIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEinqTRDRLAKLNKELASLEQNKNHInNELESKEE 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 911 P--SHISKI-DLLNLQDLSS--GAKGDNCLNTSQQLPGGDFSSTWVKEYHTQEISRENSFHASIEAIWEECKEIVKASSK 985
Cdd:TIGR00606 620 QlsSYEDKLfDVCGSQDEESdlERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISD 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 986 KSHQIQGLEEQIEKLQVEVKGyREENSDLRAQESQGKNRDHQLKEKEslIQQLREELQEKSVSLRVQVQLVAEREQALSE 1065
Cdd:TIGR00606 700 LQSKLRLAPDKLKSTESELKK-KEKRRDEMLGLAPGRQSIIDLKEKE--IPELRNKLQKVNRDIQRLKNDIEEQETLLGT 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1066 LSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEV--KFREEVT 1143
Cdd:TIGR00606 777 IMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELnrKLIQDQQ 856
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1144 RLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADL-QKKEEDC--AELKEKFIDAKKQIeqvqreVS 1220
Cdd:TIGR00606 857 EQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIkDAKEQDSplETFLEKDQQEKEEL------IS 930
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1221 VMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRlTLVEQEQT 1300
Cdd:TIGR00606 931 SKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMR-LMRQDIDT 1009
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907132433 1301 QAEQDRVLEAKseeadwlaTELDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDEL 1362
Cdd:TIGR00606 1010 QKIQERWLQDN--------LTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENI 1063
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
100-190 |
1.88e-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: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 100 HLSEKSSGQVAQKFSFSKVFGPETSQKEFF--LGCIMQPVkdlLEGHSRLIFTYGLTNSGktytfqgteENIGILPRTLN 177
Cdd:pfam16796 44 TSSDGKIGSKNKSFSFDRVFPPESEQEDVFqeISQLVQSC---LDGYNVCIFAYGQTGSG---------SNDGMIPRARE 111
|
90
....*....|...
gi 1907132433 178 VLFDSLQERLYTK 190
Cdd:pfam16796 112 QIFRFISSLKKGW 124
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1140-1425 |
2.24e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1140 EEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREV 1219
Cdd:COG4372 38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1220 SVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQ 1299
Cdd:COG4372 118 EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1300 TQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEE 1379
Cdd:COG4372 198 KEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEE 277
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1907132433 1380 KAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEK 1425
Cdd:COG4372 278 LEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1029-1265 |
2.31e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1029 KEKESLIQQLRE-------ELQEKSVSLRVQ--VQLVAEREQALSELSQDV--------TCYKAKIKDLEVIVETQKDEc 1091
Cdd:PRK05771 16 SYKDEVLEALHElgvvhieDLKEELSNERLRklRSLLTKLSEALDKLRSYLpklnplreEKKKVSVKSLEELIKDVEEE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1092 krLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVKFREE--VTRLANNLHDTKQLLQSKEEENEISrQE 1169
Cdd:PRK05771 95 --LEKIEKEIKELEEEISELENEIKELEQEIERLEPWGNFDLDLSLLLGFkyVSVFVGTVPEDKLEELKLESDVENV-EY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1170 TEKLKEEL---------AANSILTQNLKADLQKKE-EDCAELKEKFIDAKKQIEQVQREvsvmrdEEKLlrikINELEKK 1239
Cdd:PRK05771 172 ISTDKGYVyvvvvvlkeLSDEVEEELKKLGFERLElEEEGTPSELIREIKEELEEIEKE------RESL----LEELKEL 241
|
250 260
....*....|....*....|....*.
gi 1907132433 1240 KNQYSQDldmkqrtIQQLKEQLSNQK 1265
Cdd:PRK05771 242 AKKYLEE-------LLALYEYLEIEL 260
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1021-1272 |
2.33e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1021 GKNRDHQLKEKESLIQQLREEL---QEKSVSLRVQVQLVAEREQALSELSQdvtcYKAKIKDLEVIVEtqkdeckRLVEL 1097
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELaeaEERLEALEAELDALQERREALQRLAE----YSWDEIDVASAER-------EIAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1098 EQSI--LEKESAILK-LEANLKECEAKHQDHIRT-NDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQET--E 1171
Cdd:COG4913 674 EAELerLDASSDDLAaLEEQLEELEAELEELEEElDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALleE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1172 KLKEELAANSI--LTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRD---------EEKLLRIKINELEKKK 1240
Cdd:COG4913 754 RFAAALGDAVEreLRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDadleslpeyLALLDRLEEDGLPEYE 833
|
250 260 270
....*....|....*....|....*....|..
gi 1907132433 1241 NQYsqdLDMKQRTIQQLKEQLsNQKMEEAVQQ 1272
Cdd:COG4913 834 ERF---KELLNENSIEFVADL-LSKLRRAIRE 861
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
771-1179 |
2.33e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 771 EEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGE--NELRNEKEEKAELNKQVVSLQQQLRFFEE---KNSSLRAD 845
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELREleeELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 846 VEQIQASYNSAVAELQTQKAVN-QEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQD 924
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 925 LSSGA-------KGDNCLNTSQQLPGGDFSSTWVKEYHTQEISRENSFHAsieaiwEECKEIVKASSKKSHQIQGLEEQI 997
Cdd:COG4717 252 LLIAAallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG------KEAEELQALPALEELEEEELEELL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 998 EKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELsqdvtcykaki 1077
Cdd:COG4717 326 AALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA----------- 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1078 kdlevivETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEvkfrEEVTRLANNLHDTKQLLQ 1157
Cdd:COG4717 395 -------EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELE----EELEELREELAELEAELE 463
|
410 420
....*....|....*....|....
gi 1907132433 1158 SKEEENEIS--RQETEKLKEELAA 1179
Cdd:COG4717 464 QLEEDGELAelLQELEELKAELRE 487
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1264-1480 |
2.61e-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: 45.82 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1264 QKMEEAVQQYEKVCKDLSVKEKLVEDMR--LTLVEQEQTQAEQDRVLEAKSEEADWLA-----TELDKWKEKFKDLETRS 1336
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELErqLKSLERQAEKAERYKELKAELRELELALlvlrlEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1337 NQRLNTGTmDDLDVLTRKFSKLQDELQESEEKYKADRKKWLE---EKAVLTTQ---AKEAENVRNREMRKYADDRERCLK 1410
Cdd:TIGR02168 252 EEELEELT-AELQELEEKLEELRLEVSELEEEIEELQKELYAlanEISRLEQQkqiLRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1411 LQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQMKALLSSCKHKDEEIQELRKAAAKSTGTENQTMN 1480
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1011-1335 |
2.62e-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: 45.89 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1011 NSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALselsqdvtcyKAKIKDLEVIVETQKDE 1090
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQEL----------QKRIRLLEKREAEAEEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1091 CKRLVELEQSILEKESAILKLeanLKECEAKHQDhirtndlsAKEVK--FREEVTRLANNLHDTKQLLQSKEEENEISRQ 1168
Cdd:pfam05557 71 LREQAELNRLKKKYLEALNKK---LNEKESQLAD--------AREVIscLKNELSELRRQIQRAELELQSTNSELEELQE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1169 ETEKLKEELAANSILTQNLKA-----------------DLQKKEEDCAELKekfiDAKKQIEQV---QREVSVMRDEEKL 1228
Cdd:pfam05557 140 RLDLLKAKASEAEQLRQNLEKqqsslaeaeqrikelefEIQSQEQDSEIVK----NSKSELARIpelEKELERLREHNKH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1229 LRIKINE---LEKKKNQYSQDLDMKQRTIQQL-KEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMR----------LTL 1294
Cdd:pfam05557 216 LNENIENkllLKEEVEDLKRKLEREEKYREEAaTLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSrrieqlqqreIVL 295
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1907132433 1295 VEQEQTQAEQDRVLEAKSEEadwLATELDKWKEKFKDLETR 1335
Cdd:pfam05557 296 KEENSSLTSSARQLEKARRE---LEQELAQYLKKIEDLNKK 333
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
812-1041 |
3.25e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 812 RNEKEEKAELNKQVVSLQQQL----RFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMEtaarS 887
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIktynKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE----D 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 888 IESNVSQIKQMQTKIDelrsldspshiSKIDLLNlQDLSSGAKGDNCLNTSQQLPGGDfsstwvkeyhtqeisrensfhA 967
Cdd:PHA02562 253 PSAALNKLNTAAAKIK-----------SKIEQFQ-KVIKMYEKGGVCPTCTQQISEGP---------------------D 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907132433 968 SIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREE 1041
Cdd:PHA02562 300 RITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAE 373
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
815-1053 |
3.41e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 815 KEEKAELNKQVVSLQQQLRFFEEKNSSLRAD-----VEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIE 889
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLVDLSeeaklLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 890 SN------VSQIKQMQTKIDELRSLDSPSHISKIDLLnlqdlssgakgdnclntsqqlpggdfsstwvkeyhtQEIsren 963
Cdd:COG3206 261 QSpviqqlRAQLAELEAELAELSARYTPNHPDVIALR------------------------------------AQI---- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 964 sfhASIEAIWEEckEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGK--NRDHQLKEK--ESLIQQLR 1039
Cdd:COG3206 301 ---AALRAQLQQ--EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRrlEREVEVARElyESLLQRLE 375
|
250
....*....|....*
gi 1907132433 1040 E-ELQEKSVSLRVQV 1053
Cdd:COG3206 376 EaRLAEALTVGNVRV 390
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
494-1460 |
3.69e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.81 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 494 NKSLQDV-SLDSNLDNKI---------LNVKRKTVSwenSLEDVLENEDLVEDLEENEETQNMET--ELTDEDSDKSLEE 561
Cdd:TIGR01612 754 NKILEDFkNKEKELSNKIndyakekdeLNKYKSKIS---EIKNHYNDQINIDNIKDEDAKQNYDKskEYIKTISIKEDEI 830
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 562 CRVSTCHKKNKEllDLIEKLNK--RLINENKEKLT--------LELKIREEVTQEFTQYWSQREADFKeTLLHEREILEE 631
Cdd:TIGR01612 831 FKIINEMKFMKD--DFLNKVDKfiNFENNCKEKIDseheqfaeLTNKIKAEISDDKLNDYEKKFNDSK-SLINEINKSIE 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 632 NAERRLAIFKDLVGKCdsqdeptnRICDIELETEEAIACLQLKFNQVKAELAETKEELIKAQEELKNRESNSLVQALKTS 711
Cdd:TIGR01612 908 EEYQNINTLKKVDEYI--------KICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLIDKINEL 979
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 712 SKV--DTSLTSNKSTCNETSEMPKNSRA-----------QTHSERKRLNEDGLQLGEPPAKKGLILVSPPITEEQNKMGE 778
Cdd:TIGR01612 980 DKAfkDASLNDYEAKNNELIKYFNDLKAnlgknkenmlyHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDE 1059
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 779 MQQSVSEVVE--GNRVLKEKNEELKRLLTIGEN-ELRN----EKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQA 851
Cdd:TIGR01612 1060 IEKEIGKNIEllNKEILEEAEINITNFNEIKEKlKHYNfddfGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKK 1139
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 852 SYNSAVAELQTQKAVNQEQRDRILKlSQEMETAARSIESNVSQIKQMQTKIDELRSLdsPSHISKIDllnlQDLSSGAKG 931
Cdd:TIGR01612 1140 KSENYIDEIKAQINDLEDVADKAIS-NDDPEEIEKKIENIVTKIDKKKNIYDEIKKL--LNEIAEIE----KDKTSLEEV 1212
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 932 DNcLNTSQqlpGGDFSSTWVKEYHTQEISRENSFHaSIEAIWEECKEIvKASSKKSHQIQGLEEQIEKlqvEVKGYREEN 1011
Cdd:TIGR01612 1213 KG-INLSY---GKNLGKLFLEKIDEEKKKSEHMIK-AMEAYIEDLDEI-KEKSPEIENEMGIEMDIKA---EMETFNISH 1283
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1012 SDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQL---VAEREQALSE----LSQDVTCYKA-KIKDLEVI 1083
Cdd:TIGR01612 1284 DDDKDHHIISKKHDENISDIREKSLKIIEDFSEESDINDIKKELqknLLDAQKHNSDinlyLNEIANIYNIlKLNKIKKI 1363
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1084 VETQKDECKRLVELEQSI---LEKESAILKL---EANLKECEAKHQDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQ 1157
Cdd:TIGR01612 1364 IDEVKEYTKEIEENNKNIkdeLDKSEKLIKKikdDINLEECKSKIESTLDDKDIDECIKKIKELKNHILSEESNIDTYFK 1443
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1158 SKEEEN----------EISRQETE---KLKEELAANSI------LTQNLkaDLQKKEEDCAELKEKFIDAKKQI-EQVQR 1217
Cdd:TIGR01612 1444 NADENNenvlllfkniEMADNKSQhilKIKKDNATNDHdfnineLKEHI--DKSKGCKDEADKNAKAIEKNKELfEQYKK 1521
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1218 EVSVMRDEEKLLRIKiNELEKKKNQYSQdldmkqrTIQQLKEqLSNQKMEEAVQQYEKVCKdlsvkeklvedmrltlVEQ 1297
Cdd:TIGR01612 1522 DVTELLNKYSALAIK-NKFAKTKKDSEI-------IIKEIKD-AHKKFILEAEKSEQKIKE----------------IKK 1576
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1298 EQTQAEQDRVLEAKSEEADW-LATELDKWKEKF---KDLETRSNQRLNtgtmdDLDVLTRKFSKLQDELQESEEKYKADR 1373
Cdd:TIGR01612 1577 EKFRIEDDAAKNDKSNKAAIdIQLSLENFENKFlkiSDIKKKINDCLK-----ETESIEKKISSFSIDSQDTELKENGDN 1651
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1374 KKWLEE--------KAVLTTQAKEAENVrNREMRKYADDRERCLKlqneveTLTAQLAEKNSELQKW-REERDQLVTAVE 1444
Cdd:TIGR01612 1652 LNSLQEfleslkdqKKNIEDKKKELDEL-DSEIEKIEIDVDQHKK------NYEIGIIEKIKEIAIAnKEEIESIKELIE 1724
|
1050
....*....|....*.
gi 1907132433 1445 TQMKALLSSCKHKDEE 1460
Cdd:TIGR01612 1725 PTIENLISSFNTNDLE 1740
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
769-1255 |
4.23e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 769 ITEEQNKMGEMQQSVSEVvEGNRVLKEKNEELKRLLTIGENELRNE--KEEKAELN------KQVVSLQQQLRFFEEKNS 840
Cdd:PRK01156 268 ELEKNNYYKELEERHMKI-INDPVYKNRNYINDYFKYKNDIENKKQilSNIDAEINkyhaiiKKLSVLQKDYNDYIKKKS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 841 ------SLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDelRSLDSPShi 914
Cdd:PRK01156 347 ryddlnNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEIN--VKLQDIS-- 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 915 SKIDLLNLQDLSSGAKGDNCLNTSQQLPG-----------GDFSSTWVKEYHTQEISRENsfhasiEAIWEECKEIVKAS 983
Cdd:PRK01156 423 SKVSSLNQRIRALRENLDELSRNMEMLNGqsvcpvcgttlGEEKSNHIINHYNEKKSRLE------EKIREIEIEVKDID 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 984 SKKSHQIQgLEEQIEKLQV-EVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELqeKSVSLRVqvqLVAEREQA 1062
Cdd:PRK01156 497 EKIVDLKK-RKEYLESEEInKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRY--KSLKLED---LDSKRTSW 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1063 LSELSQdvtcykAKIKDLEVIvETQKDEckrlveleqsileKESAILKLEANLKECEAKHQDHIRTNDLSAKEVKfrEEV 1142
Cdd:PRK01156 571 LNALAV------ISLIDIETN-RSRSNE-------------IKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIE--NEA 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1143 trlaNNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsilTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVM 1222
Cdd:PRK01156 629 ----NNLNNKYNEIQENKILIEKLRGKIDNYKKQIAE----IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARL 700
|
490 500 510
....*....|....*....|....*....|...
gi 1907132433 1223 RDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQ 1255
Cdd:PRK01156 701 ESTIEILRTRINELSDRINDINETLESMKKIKK 733
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1139-1407 |
4.65e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1139 REEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQRE 1218
Cdd:COG4372 51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1219 VSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQE 1298
Cdd:COG4372 131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1299 QTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLE 1378
Cdd:COG4372 211 SLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
250 260
....*....|....*....|....*....
gi 1907132433 1379 EKAVLTTQAKEAENVRNREMRKYADDRER 1407
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 ... |
524-1439 |
5.50e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 524 LEDVLEneDLVEDLEENEE---------------TQNMETELTDEDSDKSLEECRVSTCHKKNKELLDLIeklnkRLINE 588
Cdd:pfam01576 73 LEEILH--ELESRLEEEEErsqqlqnekkkmqqhIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDI-----LLLED 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 589 NKEKLTLELKIREEVTQEFTQYWSQREADFK--ETLLHEREILEENAERRLAIFKdlvgKCDSQDEPTNRICDIEL-ETE 665
Cdd:pfam01576 146 QNSKLSKERKLLEERISEFTSNLAEEEEKAKslSKLKNKHEAMISDLEERLKKEE----KGRQELEKAKRKLEGEStDLQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 666 EAIACLQLKFNQVKAELAETKEELIKAQEELKNrESNSLVQALKTSSKvdtsLTSNKSTCNETSEMPKNSRAQTHSERKR 745
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLEE-ETAQKNNALKKIRE----LEAQISELQEDLESERAARNKAEKQRRD 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 746 LNEDGLQLG--------------EPPAKKG--LILVSPPITEE----QNKMGEMQQSVSEVVEGnrvLKEKNEELKRLLT 805
Cdd:pfam01576 297 LGEELEALKteledtldttaaqqELRSKREqeVTELKKALEEEtrshEAQLQEMRQKHTQALEE---LTEQLEQAKRNKA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 806 IGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAvaelqtqKAVNQEQRDRILKLSQEMETAA 885
Cdd:pfam01576 374 NLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSES-------ERQRAELAEKLSKLQSELESVS 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 886 RSIESNVSQIKQMQTkidELRSLDSPSHiskiDLLNLQDLSSGAKgdncLNTSQQLPGGDFSSTWVKEYHTQEISRENSF 965
Cdd:pfam01576 447 SLLNEAEGKNIKLSK---DVSSLESQLQ----DTQELLQEETRQK----LNLSTRLRQLEDERNSLQEQLEEEEEAKRNV 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 966 HASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQvevkgyreenSDLRAQESQGKNRDHQLKEKESLIQQLREELQEK 1045
Cdd:pfam01576 516 ERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQ----------RELEALTQQLEEKAAAYDKLEKTKNRLQQELDDL 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1046 SVSLRVQVQLVAERE-------QALSElSQDVTCYKAKIKDLEVIVETQKDecKRLVELEQSILEKESAILKLEANLKEC 1118
Cdd:pfam01576 586 LVDLDHQRQLVSNLEkkqkkfdQMLAE-EKAISARYAEERDRAEAEAREKE--TRALSLARALEEALEAKEELERTNKQL 662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1119 EAKHQDHIRTNDLSAKEVkfrEEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANsilTQNLKA----DLQKK 1194
Cdd:pfam01576 663 RAEMEDLVSSKDDVGKNV---HELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVN---MQALKAqferDLQAR 736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1195 EEDCAElkekfidAKKQIEQVQREVSVMRDEEKLLRIKINELEKKknqysqdLDMKqrtIQQLKEQL--SNQKMEEAVQQ 1272
Cdd:pfam01576 737 DEQGEE-------KRRQLVKQVRELEAELEDERKQRAQAVAAKKK-------LELD---LKELEAQIdaANKGREEAVKQ 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1273 YEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRvlEAKSEEADWLATEldkwkekfKDLETRSNQRlntgtmddldvlt 1352
Cdd:pfam01576 800 LKKLQAQMKDLQRELEEARASRDEILAQSKESEK--KLKNLEAELLQLQ--------EDLAASERAR------------- 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1353 RKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEKNSELQKW 1432
Cdd:pfam01576 857 RQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKS 936
|
....*..
gi 1907132433 1433 REERDQL 1439
Cdd:pfam01576 937 ESARQQL 943
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1033-1259 |
5.56e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1033 SLIQQLREELQEKSVSLRVQVQLVAEREQALSEL----SQDVTCYKAKIKDLeviVETQKDECKRLVELEQSILEKESAI 1108
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQrkknGENIARKQNKYDEL---VEEAKTIKAEIEELTDELLNLVMDI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1109 LKLEANLKECEAKHQDHIRTNDLSAKEVKFREE-----------------VTRLANNLHDtkqlLQSKEEENEISRQETE 1171
Cdd:PHA02562 251 EDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqqisegpdrITKIKDKLKE----LQHSLEKLDTAIDELE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1172 KLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQ 1251
Cdd:PHA02562 327 EIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRG 406
|
....*...
gi 1907132433 1252 RTIQQLKE 1259
Cdd:PHA02562 407 IVTDLLKD 414
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1209-1470 |
5.80e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1209 KKQIEQVQREVsvmRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQyekvcKDLSVKEKLVE 1288
Cdd:COG1196 199 ERQLEPLERQA---EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELE-----AELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1289 DMRLTLVEQEQT-QAEQDRVLEAKSEEADwLATELDKWKEKFKDLETRsnqrlntgtmddldvltrkfsklQDELQESEE 1367
Cdd:COG1196 271 ELRLELEELELElEEAQAEEYELLAELAR-LEQDIARLEERRRELEER-----------------------LEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1368 KYKADRKKWLEEKAVLTTQAKEAEnvrnremrkyADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLVTAvETQM 1447
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAE----------EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-LRAA 395
|
250 260
....*....|....*....|...
gi 1907132433 1448 KALLSSCKHKDEEIQELRKAAAK 1470
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLER 418
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1139-1462 |
5.99e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 44.29 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1139 REEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAAnsiltqnlkadLQKKEEDCAELKEKFIDAKKQIEQVQRE 1218
Cdd:pfam05622 6 QEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQ-----------LESGDDSGTPGGKKYLLLQKQLEQLQEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1219 VSVMRDEEKLLRIKINELEKK---KNQYSQDLDMKQRTIQQLKEQL-----SNQK---MEEAVQQYEKVCKDLSVKEKLV 1287
Cdd:pfam05622 75 NFRLETARDDYRIKCEELEKEvleLQHRNEELTSLAEEAQALKDEMdilreSSDKvkkLEATVETYKKKLEDLGDLRRQV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1288 EdmrlTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRsnqrlntgtmddLDVLTRKFSKLQDELQESEE 1367
Cdd:pfam05622 155 K----LLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGK------------LSEESKKADKLEFEYKKLEE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1368 KYKA---DRKKWLEEKAVL--------TTQAKEAENVRNREMRKYADD--------------RERCLKLQNEVETL---- 1418
Cdd:pfam05622 219 KLEAlqkEKERLIIERDTLretneelrCAQLQQAELSQADALLSPSSDpgdnlaaeimpaeiREKLIRLQHENKMLrlgq 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1907132433 1419 TAQLAEKNSELQKWREERDQLVTAVETQMKAL---LSSCKHKDEEIQ 1462
Cdd:pfam05622 299 EGSYRERLTELQQLLEDANRRKNELETQNRLAnqrILELQQQVEELQ 345
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
809-1107 |
6.17e-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: 43.98 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 809 NELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSI 888
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 889 ESNVSQIKQMqtkideLRSLDSPSHISKIDLLnlqdLSSgakgdnclntsqqlpggdfsstwvkeyhtqeisrensfhas 968
Cdd:COG4942 100 EAQKEELAEL------LRALYRLGRQPPLALL----LSP----------------------------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 969 ieaiwEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQesqgknrdhqLKEKESLIQQLREELQEKSvs 1048
Cdd:COG4942 129 -----EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE----------RAELEALLAELEEERAALE-- 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907132433 1049 lrvqvQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESA 1107
Cdd:COG4942 192 -----ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
991-1467 |
6.35e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 991 QGLEEQIEKLQVEVKGYREENSDLRAQESQGKNrdhQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDV 1070
Cdd:pfam01576 204 QELEKAKRKLEGESTDLQEQIAELQAQIAELRA---QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDL 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1071 TCYKA-------KIKDLEVIVETQKDECKRLVELEQSILEKESailKLEANLKECEAKHQDHIRTNDLSAKEVKFR--EE 1141
Cdd:pfam01576 281 ESERAarnkaekQRRDLGEELEALKTELEDTLDTTAAQQELRS---KREQEVTELKKALEEETRSHEAQLQEMRQKhtQA 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1142 VTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSV 1221
Cdd:pfam01576 358 LEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSK 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1222 MRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSnqkmEEAVQQYekvckDLSVKEKLVEDMRLTLVEQEQTQ 1301
Cdd:pfam01576 438 LQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ----EETRQKL-----NLSTRLRQLEDERNSLQEQLEEE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1302 AEQDRVLEaksEEADWLATELDKWKEKFKDletrsnqrlNTGTMDDLDVLTRKFSK-LQDELQESEEKY-------KADR 1373
Cdd:pfam01576 509 EEAKRNVE---RQLSTLQAQLSDMKKKLEE---------DAGTLEALEEGKKRLQReLEALTQQLEEKAaaydkleKTKN 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1374 KKWLEEKAVLTTQAKEAENVRNREMR----------------KYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERD 1437
Cdd:pfam01576 577 RLQQELDDLLVDLDHQRQLVSNLEKKqkkfdqmlaeekaisaRYAEERDRAEAEAREKETRALSLARALEEALEAKEELE 656
|
490 500 510
....*....|....*....|....*....|
gi 1907132433 1438 QLVTAVETQMKALLSSCKHKDEEIQELRKA 1467
Cdd:pfam01576 657 RTNKQLRAEMEDLVSSKDDVGKNVHELERS 686
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
891-1297 |
6.66e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.44 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 891 NVSQIKQMQTKIDELRSLDSPSHISKIDLLNLqdlssgaKGDnclntSQQLpggdFSStWVKEYhtQEISrENSFhASIE 970
Cdd:PRK04778 27 NYKRIDELEERKQELENLPVNDELEKVKKLNL-------TGQ-----SEEK----FEE-WRQKW--DEIV-TNSL-PDIE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 971 AIWEECKEIVKAS--SKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKeslIQQLREELQEKSVS 1048
Cdd:PRK04778 86 EQLFEAEELNDKFrfRKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDL---YRELRKSLLANRFS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1049 -------LRVQV-QLVAEREQA---------------LSELSQDVTCYKAKIKDLEVIVETQKDE-----------CKRL 1094
Cdd:PRK04778 163 fgpaldeLEKQLeNLEEEFSQFveltesgdyveareiLDQLEEELAALEQIMEEIPELLKELQTElpdqlqelkagYREL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1095 VE---------LEQSILEKESAILKLEANLKECEAKH----QDHIRTN-----DLSAKEVKFREEVTRLANNLhdTKQLL 1156
Cdd:PRK04778 243 VEegyhldhldIEKEIQDLKEQIDENLALLEELDLDEaeekNEEIQERidqlyDILEREVKARKYVEKNSDTL--PDFLE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1157 QSKEEENEIsRQETEKLKE--ELAANSILTQ--------NLKADLQKKEEDCA-------ELKEKFIDAKKQIEQVQRE- 1218
Cdd:PRK04778 321 HAKEQNKEL-KEEIDRVKQsyTLNESELESVrqlekqleSLEKQYDEITERIAeqeiaysELQEELEEILKQLEEIEKEq 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1219 ------VSVMRDEEKLLRIKINELEKKK----------------NQYSQDLDMKQRTIQQLKEQLSNQK--MEEAVQQYE 1274
Cdd:PRK04778 400 eklsemLQGLRKDELEAREKLERYRNKLheikryleksnlpglpEDYLEMFFEVSDEIEALAEELEEKPinMEAVNRLLE 479
|
490 500
....*....|....*....|....*
gi 1907132433 1275 KVCKDLSVKEKLVEDMR--LTLVEQ 1297
Cdd:PRK04778 480 EATEDVETLEEETEELVenATLTEQ 504
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1415-1667 |
6.70e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 44.65 E-value: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1415 VETLTAQLAEKNSELQK---------WREERDQLVTAVETQMKALLssckhkdEEIQELRKAAAKSTGTENQTMNPKPEY 1485
Cdd:PTZ00108 1104 VEKLNAELEKKEKELEKlknttpkdmWLEDLDKFEEALEEQEEVEE-------KEIAKEQRLKSKTKGKASKLRKPKLKK 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1486 NDSVDLGGVETEPQSTSLEISRNTAEDGSVVLDSCEVSTENVQSTRFPKPELEIQFT----------PLQPNKMAVKHPG 1555
Cdd:PTZ00108 1177 KEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTkpkkssvkrlKSKKNNSSKSSED 1256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1556 CPTPVTIKIPKARKRKSgEVEEVSVGPSSKKTYslrSQASTVSANIASKKREGTLQKFGDFLQHSPTILQSKAKKIIETM 1635
Cdd:PTZ00108 1257 NDEFSSDDLSKEGKPKN-APKRVSAVQYSPPPP---SKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTA 1332
|
250 260 270
....*....|....*....|....*....|....
gi 1907132433 1636 SSPKLST--VEVSKENVSQPKKAKRKLYRNEISS 1667
Cdd:PTZ00108 1333 RKKKSKTrvKQASASQSSRLLRRPRKKKSDSSSE 1366
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
818-1290 |
7.25e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.65 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 818 KAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQ 897
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 898 MQTKIDELRSLDSPSHISKIDLLNLQDLSSGAKGdnclntsqqlpggdfsstwVKEYHTQEISRENSFHASIEAiweecK 977
Cdd:TIGR00606 770 QETLLGTIMPEEESAKVCLTDVTIMERFQMELKD-------------------VERKIAQQAAKLQGSDLDRTV-----Q 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 978 EIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRvqvQLVA 1057
Cdd:TIGR00606 826 QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQ---SLIR 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1058 EREQALSELSQDVTCYKAKIKDLEVIVeTQKDECKRLVELEQSILEKEsaILKLEANLKECEAKHQDhirtndlsAKEVK 1137
Cdd:TIGR00606 903 EIKDAKEQDSPLETFLEKDQQEKEELI-SSKETSNKKAQDKVNDIKEK--VKNIHGYMKDIENKIQD--------GKDDY 971
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1138 FREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKadLQKKEEDCAELKEKFIDAKKQIEQVQr 1217
Cdd:TIGR00606 972 LKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLT--LRKRENELKEVEEELKQHLKEMGQMQ- 1048
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907132433 1218 eVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDM 1290
Cdd:TIGR00606 1049 -VLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDL 1120
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
654-891 |
8.10e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 654 TNRICDIELETEEAIACLQLKFNQVKAELAETKEELIKAQEELKN--RESNSLVQALKTSSKVDTSLTSNKSTCNETSEM 731
Cdd:PHA02562 201 NKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNlvMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKM 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 732 pknsraqthserkrlNEDGlqlGEPPAkkglilVSPPITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLltigENEL 811
Cdd:PHA02562 281 ---------------YEKG---GVCPT------CTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEI----MDEF 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 812 RNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELqtqKAVNQEQRDRILKLSQ-EMETAARSIES 890
Cdd:PHA02562 333 NEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEEL---AKLQDELDKIVKTKSElVKEKYHRGIVT 409
|
.
gi 1907132433 891 N 891
Cdd:PHA02562 410 D 410
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
991-1537 |
8.90e-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: 44.04 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 991 QGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQeksvslrvqvqlvAEREQALSELSqdv 1070
Cdd:pfam10174 70 QHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQ-------------SEHERQAKELF--- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1071 tCYKAKIKDLEVIVETQK-------DECKRLVELEQSI-LEKESAILKLEANLKECEAKHQDHIRTNDLSAKE---VKFR 1139
Cdd:pfam10174 134 -LLRKTLEEMELRIETQKqtlgardESIKKLLEMLQSKgLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEkenIHLR 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1140 EEVTR---LANNLHDTKQLLQSKE-EENEISRQETEKLKEELAANSILTQNLKADLQKKEE----DCAELKEKFIdaKKQ 1211
Cdd:pfam10174 213 EELHRrnqLQPDPAKTKALQTVIEmKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEikqmEVYKSHSKFM--KNK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1212 IEQVQREVSVMRDEEKLLRIKineLEKKKNQYSqdlDMKQRtIQQLKEQLSNQKMEEAVQQYEkvckdlsvkeklVEDMR 1291
Cdd:pfam10174 291 IDQLKQELSKKESELLALQTK---LETLTNQNS---DCKQH-IEVLKESLTAKEQRAAILQTE------------VDALR 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1292 LTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKekfkdletrsnqrlntgtmDDLDVLTRKFSKLQDELQESEEKYKa 1371
Cdd:pfam10174 352 LRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLK-------------------DMLDVKERKINVLQKKIENLQEQLR- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1372 DRKKWLEEKavlttqakeaenvrnremrkyaddRERCLKLQNE-------VETLTAQLAEKNSELQKWREERDQLvtavE 1444
Cdd:pfam10174 412 DKDKQLAGL------------------------KERVKSLQTDssntdtaLTTLEEALSEKERIIERLKEQRERE----D 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1445 TQMKALLSSCKHKDEEIQELRKAAAKSTGTENQTMNPKPEYNDSVDLGGVETEPQSTSLEISRNTAEDGSVVLDSCEVST 1524
Cdd:pfam10174 464 RERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKA 543
|
570
....*....|...
gi 1907132433 1525 ENVQSTRFPKPEL 1537
Cdd:pfam10174 544 HNAEEAVRTNPEI 556
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
989-1308 |
9.89e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 989 QIQGLEEQIEKLQVEVKGYREENSDLRAQESqgknrdhQLKEKESLIQQLrEELQEKSVSLRVQVQLVAEREQALSEL-- 1066
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELD-------ALQERREALQRL-AEYSWDEIDVASAEREIAELEAELERLda 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1067 -SQDVTCYKAKIKDLEVIVETQKDECKRLVE----LEQSILEKESAILKLEANLKECEAKHQDHIRTN-DLSAKEVKFRE 1140
Cdd:COG4913 683 sSDDLAALEEQLEELEAELEELEEELDELKGeigrLEKELEQAEEELDELQDRLEAAEDLARLELRALlEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1141 EVTRLANNLHDtkQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADL-----------QKKEEDCAELKEKFIDAK 1209
Cdd:COG4913 763 VERELRENLEE--RIDALRARLNRAEEELERAMRAFNREWPAETADLDADLeslpeylalldRLEEDGLPEYEERFKELL 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1210 KQ--IEQVQREVSVMRDEEKLLRIKINELEK--KKNQYSQD----LDMKQRTIQQLKE------QLSNQKMEEAVQQYEK 1275
Cdd:COG4913 841 NEnsIEFVADLLSKLRRAIREIKERIDPLNDslKRIPFGPGrylrLEARPRPDPEVREfrqelrAVTSGASLFDEELSEA 920
|
330 340 350
....*....|....*....|....*....|...
gi 1907132433 1276 VCKDLsvkEKLVEdmRLTLVEQEQTQAEQDRVL 1308
Cdd:COG4913 921 RFAAL---KRLIE--RLRSEEEESDRRWRARVL 948
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
663-890 |
1.10e-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: 43.21 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 663 ETEEAIACLQLKFNQVKAELAETKEELIKAQEELKNREsNSLVQALKTSSKVDTSLTSNKSTCNETSEMPKNSRAQTHSE 742
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE-RRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 743 RKRLNE--DGLQ-LGEPPAKKglILVSPPITEEQNKMGEMQQSVsevvegNRVLKEKNEELKRLLTIGENELRNEKEEKA 819
Cdd:COG4942 103 KEELAEllRALYrLGRQPPLA--LLLSPEDFLDAVRRLQYLKYL------APARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907132433 820 ELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIES 890
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
680-1470 |
1.15e-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: 44.01 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 680 AELAETKEELIKAQEELKNRESNSlVQALKTSSKVDTSLTSNKSTCNETSEMPKNSRAQTHSERKRLNEDGLQLGEPPAK 759
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKH-QQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 760 kglilvSPPITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELK------------RLLTIGENELRNEKEEKAeLNKQVVS 827
Cdd:pfam01576 91 ------SQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKvtteakikkleeDILLLEDQNSKLSKERKL-LEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 828 LQQQLRFFEEKNSSLradvEQIQASYNSAVAELqtqkavnQEQRDRILKLSQEMETAARSIESNVS----QIKQMQTKID 903
Cdd:pfam01576 164 FTSNLAEEEEKAKSL----SKLKNKHEAMISDL-------EERLKKEEKGRQELEKAKRKLEGESTdlqeQIAELQAQIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 904 ELRSLDSPSHISKIDLLNLQDLSSGAKgdnclntsqqlpggdfsstwvkeyhTQEISRENSFHASIEAIWEECKEIVKAS 983
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLEEETAQK-------------------------NNALKKIRELEAQISELQEDLESERAAR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 984 SKKSHQIQGLEEQIEKLQVEVkgyrEENSDLRAQESQGKNRdhqlkeKESLIQQLREELQEKSVSLRVQVQLVAERE-QA 1062
Cdd:pfam01576 288 NKAEKQRRDLGEELEALKTEL----EDTLDTTAAQQELRSK------REQEVTELKKALEEETRSHEAQLQEMRQKHtQA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1063 LSELSQDVTCYKAKIKDLEVIVETQKDECKRLVE----LEQSILEKESAILKLEANLKECEAKHQDHIRT---------- 1128
Cdd:pfam01576 358 LEELTEQLEQAKRNKANLEKAKQALESENAELQAelrtLQQAKQDSEHKRKKLEGQLQELQARLSESERQraelaeklsk 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1129 ------------NDLSAKEVKFREEVTRLANNLHDTKQLLQS---------------KEEENEISRQ--ETEKLKEELAA 1179
Cdd:pfam01576 438 lqselesvssllNEAEGKNIKLSKDVSSLESQLQDTQELLQEetrqklnlstrlrqlEDERNSLQEQleEEEEAKRNVER 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1180 NSILTQNLKADLQKKEEDCAELKEKFIDAKKqieQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKE 1259
Cdd:pfam01576 518 QLSTLQAQLSDMKKKLEEDAGTLEALEEGKK---RLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQ 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1260 QLSNqkMEEAVQQYEKVCKDlsvkEKLVedmrltlveQEQTQAEQDRVlEAKSEEADW----LATELDKWKEKFKDLEtR 1335
Cdd:pfam01576 595 LVSN--LEKKQKKFDQMLAE----EKAI---------SARYAEERDRA-EAEAREKETralsLARALEEALEAKEELE-R 657
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1336 SNQRLNtGTMDDL-----DV--------------------LTRKFSKLQDELQESEekykaDRKKWLEekavLTTQAKEA 1390
Cdd:pfam01576 658 TNKQLR-AEMEDLvsskdDVgknvhelerskraleqqveeMKTQLEELEDELQATE-----DAKLRLE----VNMQALKA 727
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1391 ENVRNREMRKYADDRERclklqnevETLTAQLAEKNSELQKWREERDQLVTA---VETQMKALLS----SCKHKDEEIQE 1463
Cdd:pfam01576 728 QFERDLQARDEQGEEKR--------RQLVKQVRELEAELEDERKQRAQAVAAkkkLELDLKELEAqidaANKGREEAVKQ 799
|
....*..
gi 1907132433 1464 LRKAAAK 1470
Cdd:pfam01576 800 LKKLQAQ 806
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1210-1438 |
1.17e-03 |
|
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: 42.32 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1210 KQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQL--SNQKMEEAVQQYEkvckDLSVKEKLV 1287
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELerTEERLAEALEKLE----EAEKAADES 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1288 EDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELD--------KWKEKFKDLE-TRSNQRLNTGTMDDLDVLTRKFSKL 1358
Cdd:pfam00261 77 ERGRKVLENRALKDEEKMEILEAQLKEAKEIAEEADrkyeevarKLVVVEGDLErAEERAELAESKIVELEEELKVVGNN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1359 QDELQESEEKYKADRKKWLEEKAVLTTQAKEAENvrnremrKYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQ 1438
Cdd:pfam00261 157 LKSLEASEEKASEREDKYEEQIRFLTEKLKEAET-------RAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQ 229
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
993-1305 |
1.20e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 43.69 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 993 LEEQIEKLQVEVkgyreensdLRAQESQGKNRDHQLKEK-ESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVT 1071
Cdd:PLN03229 434 LEGEVEKLKEQI---------LKAKESSSKPSELALNEMiEKLKKEIDLEYTEAVIAMGLQERLENLREEFSKANSQDQL 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1072 CYKAKIKDLEVIVE---------------TQKDECKRLVELEQSILEKESAILKLEAnlkECEAKHQDHIRTNDLSAKEV 1136
Cdd:PLN03229 505 MHPVLMEKIEKLKDefnkrlsrapnylslKYKLDMLNEFSRAKALSEKKSKAEKLKA---EINKKFKEVMDRPEIKEKME 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1137 KFREEVtrlannlhdTKQLLQSKEEENEISRQETEKLKEELA---ANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIE 1213
Cdd:PLN03229 582 ALKAEV---------ASSGASSGDELDDDLKEKVEKMKKEIElelAGVLKSMGLEVIGVTKKNKDTAEQTPPPNLQEKIE 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1214 QVQREVS-----VMRDEEKLLRIKINELEKKKNQYSQDLDMKQrTIQQLKEQLsNQKMEEAVQQYEkvckdlsVKEKLvE 1288
Cdd:PLN03229 653 SLNEEINkkierVIRSSDLKSKIELLKLEVAKASKTPDVTEKE-KIEALEQQI-KQKIAEALNSSE-------LKEKF-E 722
|
330
....*....|....*..
gi 1907132433 1289 DMRLTLVEQEQTQAEQD 1305
Cdd:PLN03229 723 ELEAELAAARETAAESN 739
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1190-1335 |
1.29e-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: 42.22 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1190 DLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEA 1269
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907132433 1270 VQQYEKVCKDLSVKEKLVEDMRLTLVEQ-EQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETR 1335
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERiEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
974-1314 |
1.31e-03 |
|
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: 43.56 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 974 EECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYRE---ENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLR 1050
Cdd:pfam05483 377 DQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKilaEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLE 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1051 VQVQLVAEREQALSELSQDVTCY--KAKIKDLEVIVETQKdeckrlVELEQSILEKESAILKLEANlkeceaKHQDHIRT 1128
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTEleKEKLKNIELTAHCDK------LLLENKELTQEASDMTLELK------KHQEDIIN 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1129 NDlsakevKFREEVTRLANNLHDTK-QLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFID 1207
Cdd:pfam05483 525 CK------KQEERMLKQIENLEEKEmNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1208 AKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKeqlsnQKMEEAVQQYEKVCKDLSVKEK-- 1285
Cdd:pfam05483 599 LKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAK-----QKFEEIIDNYQKEIEDKKISEEkl 673
|
330 340 350
....*....|....*....|....*....|.
gi 1907132433 1286 --LVEDMRLTLVEQEQTQAEQDRVLEAKSEE 1314
Cdd:pfam05483 674 leEVEKAKAIADEAVKLQKEIDKRCQHKIAE 704
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1032-1175 |
1.36e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1032 ESLIQQLREELQEKSVSLRVQVQLVAEREQALSElsqdvtcykAKIKDLEVIVETQKDEckrLVELEQSILEKESAILKL 1111
Cdd:COG2433 379 EEALEELIEKELPEEEPEAEREKEHEERELTEEE---------EEIRRLEEQVERLEAE---VEELEAELEEKDERIERL 446
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907132433 1112 EANLKEceakhqdhIRTNdlSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKE 1175
Cdd:COG2433 447 ERELSE--------ARSE--ERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
978-1440 |
1.39e-03 |
|
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: 43.42 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 978 EIVKASSKKSHQIQGLEEQIEKLQVEVKGYREenSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVA 1057
Cdd:pfam02463 261 EKEEEKLAQVLKENKEEEKEKKLQEEELKLLA--KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1058 EREQALSELsqdvtcYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQdhirtndLSAKEVK 1137
Cdd:pfam02463 339 ELEKELKEL------EIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE-------LKSEEEK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1138 FREEVTRLANNLHDTKQLLQSKEEENEI---SRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFID-AKKQIE 1213
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEEKKEELEILEeeeESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQlVKLQEQ 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1214 QVQREVSVMRDEEKLLRIKINELEKKKNQYSQDL--------DMKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEK 1285
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGvggriisaHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQK 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1286 LVEDMRLTLVEQEQTQAE-QDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQE 1364
Cdd:pfam02463 566 LVRALTELPLGARKLRLLiPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKE 645
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907132433 1365 SEEKYKADRKKWLEEKAVLTTQAKEAENvRNREMRKYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLV 1440
Cdd:pfam02463 646 SGLRKGVSLEEGLAEKSEVKASLSELTK-ELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAE 720
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1036-1319 |
1.82e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.12 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1036 QQLREELQE-KSVSLRVQVQLVAEREQALSELS------QDVTCYKAKIKDLEVI-------VETQKDECKRL------V 1095
Cdd:PRK10929 26 KQITQELEQaKAAKTPAQAEIVEALQSALNWLEerkgslERAKQYQQVIDNFPKLsaelrqqLNNERDEPRSVppnmstD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1096 ELEQSILEKESAILKLEANLKEceakHQDHIRtndlsakevkfreEVTRLANNLhdTKQLLQSKEEENEISRQetekLKE 1175
Cdd:PRK10929 106 ALEQEILQVSSQLLEKSRQAQQ----EQDRAR-------------EISDSLSQL--PQQQTEARRQLNEIERR----LQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1176 ELAANSILTQNLKADLQkkeedcAELKEKfidaKKQIEQVQREVSVMRDEEKLLRIKInELEKKKnqySQDLDMKqrtIQ 1255
Cdd:PRK10929 163 LGTPNTPLAQAQLTALQ------AESAAL----KALVDELELAQLSANNRQELARLRS-ELAKKR---SQQLDAY---LQ 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907132433 1256 QLKEQLSNQKMEEAVQQYEKVckdlsvkEKLVE---DMRLTLVEQEQTQAEQDRVLEAKSEEADWLA 1319
Cdd:PRK10929 226 ALRNQLNSQRQREAERALEST-------ELLAEqsgDLPKSIVAQFKINRELSQALNQQAQRMDLIA 285
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1023-1466 |
2.10e-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: 42.70 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1023 NRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVElEQSIL 1102
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNS-DLSKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1103 EKESAILKLEANLKECE-AKHQDHIRTNDlsAKEVKFREEVTRLANNLhdtkqllqsKEEENEISRQETEKlkeelaans 1181
Cdd:TIGR04523 109 NSEIKNDKEQKNKLEVElNKLEKQKKENK--KNIDKFLTEIKKKEKEL---------EKLNNKYNDLKKQK--------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1182 iltQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMR---DEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLK 1258
Cdd:TIGR04523 169 ---EELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1259 EQLSN--QKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQE-QTQAEQDRVLEAKSE-EADW---LATELDKWKEKFKD 1331
Cdd:TIGR04523 246 TEISNtqTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEkQLNQLKSEISDLNNQkEQDWnkeLKSELKNQEKKLEE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1332 LETRSNQRLNTgtmddLDVLTRKFSKLQDELQESEEKyKADRKKWLEEKavlttqakeaenvrNREMRKYADDRErclKL 1411
Cdd:TIGR04523 326 IQNQISQNNKI-----ISQLNEQISQLKKELTNSESE-NSEKQRELEEK--------------QNEIEKLKKENQ---SY 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1907132433 1412 QNEVETLTAQLAEKNSELQKWREERDQLvtavETQMKALLSSCKHKDEEIQELRK 1466
Cdd:TIGR04523 383 KQEIKNLESQINDLESKIQNQEKLNQQK----DEQIKKLQQEKELLEKEIERLKE 433
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1005-1397 |
2.31e-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: 42.64 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1005 KGYREENSDLRAQESQGKNRDHQL--KEKESLIQQLREELQEKSvslrvQVQLVAEREQALSELSQDVTCYKAKIKDLEV 1082
Cdd:COG5185 128 SEIVALKDELIKVEKLDEIADIEAsyGEVETGIIKDIFGKLTQE-----LNQNLKKLEIFGLTLGLLKGISELKKAEPSG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1083 IVETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVKFREEVTRL-ANNLHDTKQLLQSKEE 1161
Cdd:COG5185 203 TVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLrLEKLGENAESSKRLNE 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1162 ENEISRQETEKLKEELAANSILTQNLKADLQKKEED-CAELKEKFIDAKKQIEQ-VQREVSVMRDEEKLLRIKINELEKK 1239
Cdd:COG5185 283 NANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLaAAEAEQELEESKRETETgIQNLTAEIEQGQESLTENLEAIKEE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1240 KNQ--YSQDLDMKQRTIQQLKEQLSNQK--MEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQ-DRVLEAKSEE 1314
Cdd:COG5185 363 IENivGEVELSKSSEELDSFKDTIESTKesLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQaTSSNEEVSKL 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1315 ADWLATELDKWKEKFKDLETR----SNQRLNTGTMDDLDVLTRKFSKLQD---ELQESEEKYKADRKKWLEEKAVLTTQA 1387
Cdd:COG5185 443 LNELISELNKVMREADEESQSrleeAYDEINRSVRSKKEDLNEELTQIESrvsTLKATLEKLRAKLERQLEGVRSKLDQV 522
|
410
....*....|
gi 1907132433 1388 KEAENVRNRE 1397
Cdd:COG5185 523 AESLKDFMRA 532
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
986-1275 |
2.31e-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: 42.71 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 986 KSHQIQGLE------EQIEKLQVEVKGYREENSDLRAQESQ------GKNR---------------DHQLKEKESLIQQL 1038
Cdd:pfam05701 27 KAHRIQTVErrklveLELEKVQEEIPEYKKQSEAAEAAKAQvleeleSTKRlieelklnleraqteEAQAKQDSELAKLR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1039 REELQ-----EKSVSLRVQVQLVAER-EQALSELSQdvtcYKAKIKDLE---VIVETQKDECKRLVE---LEQSILEK-- 1104
Cdd:pfam05701 107 VEEMEqgiadEASVAAKAQLEVAKARhAAAVAELKS----VKEELESLRkeyASLVSERDIAIKRAEeavSASKEIEKtv 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1105 ESAILKLEANLKECEAKHQDHirtndLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQ--ETEKLKEELAANSI 1182
Cdd:pfam05701 183 EELTIELIATKESLESAHAAH-----LEAEEHRIGAALAREQDKLNWEKELKQAEEELQRLNQQllSAKDLKSKLETASA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1183 LTQNLKADL---------------QKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKI----NELEKKKnqy 1243
Cdd:pfam05701 258 LLLDLKAELaaymesklkeeadgeGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAaslrSELEKEK--- 334
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1907132433 1244 sQDLD-MKQR------TIQQLKEQLSNQKME-EAVQQYEK 1275
Cdd:pfam05701 335 -AELAsLRQRegmasiAVSSLEAELNRTKSEiALVQAKEK 373
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
994-1465 |
2.34e-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: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 994 EEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQalselsQDVTCY 1073
Cdd:TIGR00606 244 ENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQ------RTVREK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1074 KAKIKDLEVIVETQKDEcKRLVELEQSILEKESAILKLEANlkeceaKHQDHIRTNDLSAKEVKFREEVTRLA------- 1146
Cdd:TIGR00606 318 ERELVDCQRELEKLNKE-RRLLNQEKTELLVEQGRLQLQAD------RHQEHIRARDSLIQSLATRLELDGFErgpfser 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1147 --NNLHDTKQLLQSKE-----------EENEISRQET-EKLKEELAANSILTQNLKADLQKKEEDC----AELKEKFIDA 1208
Cdd:TIGR00606 391 qiKNFHTLVIERQEDEaktaaqlcadlQSKERLKQEQaDEIRDEKKGLGRTIELKKEILEKKQEELkfviKELQQLEGSS 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1209 KKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQ----DLDMKQRTIQQLKEQLSNQKmeEAVQQYEKVCKDLSVKE 1284
Cdd:TIGR00606 471 DRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQnekaDLDRKLRKLDQEMEQLNHHT--TTRTQMEMLTKDKMDKD 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1285 KLVEDMRLTLVEQEQTQA-------EQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNtgtmdDLDVLTRKFSK 1357
Cdd:TIGR00606 549 EQIRKIKSRHSDELTSLLgyfpnkkQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINN-----ELESKEEQLSS 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1358 LQDE----------------LQESEEKYKADRKKWLEEKAV-------LTTQAKEAENVRNREMRKYADDRERCLKLQNE 1414
Cdd:TIGR00606 624 YEDKlfdvcgsqdeesdlerLKEEIEKSSKQRAMLAGATAVysqfitqLTDENQSCCPVCQRVFQTEAELQEFISDLQSK 703
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1907132433 1415 VETLTAQLAEKNSELQKWREERDQLVTAVETQMKALlsscKHKDEEIQELR 1465
Cdd:TIGR00606 704 LRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSII----DLKEKEIPELR 750
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
665-882 |
2.55e-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: 42.63 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 665 EEAIACLQLKFNQVKAELAETKEELIKAQEELKN-RESNSLVQALKTSSKV--DTSLTSNKSTCNETSEMPKNSRA--QT 739
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQlKEQLQLLNKLLPQANLlaDETLADRLEELREELDAAQEAQAfiQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 740 HSERKRLNEDGLQlgeppakkglILVSPPITEEQnkmgeMQQSVSEVVEGNRVLKEKNEELK----RLLTIGENELRNEK 815
Cdd:COG3096 915 HGKALAQLEPLVA----------VLQSDPEQFEQ-----LQADYLQAKEQQRRLKQQIFALSevvqRRPHFSYEDAVGLL 979
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907132433 816 EEKAELNKQvvsLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEME 882
Cdd:COG3096 980 GENSDLNEK---LRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELE 1043
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
586-905 |
2.74e-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: 42.75 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 586 INENKEKLTLELKI----REEVTQEFTQYWSQREADFKET--LLHEREILEENAERRLAIFKDLVGKCDSqdeptnricd 659
Cdd:TIGR02169 679 LRERLEGLKRELSSlqseLRRIENRLDELSQELSDASRKIgeIEKEIEQLEQEEEKLKERLEELEEDLSS---------- 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 660 IELETEEAIACLQlKFNQVKAELAETKEELIKAQEELKNRESNSLVQAL-KTSSKVDTSLTSNKSTCNETsempkNSRAQ 738
Cdd:TIGR02169 749 LEQEIENVKSELK-ELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIqAELSKLEEEVSRIEARLREI-----EQKLN 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 739 THSERKRLNEDGLQlgeppakkglilvsppitEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEK 818
Cdd:TIGR02169 823 RLTLEKEYLEKEIQ------------------ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 819 AELNKQVVSLQQQLRFFEEKNSSLRADVEQIqasyNSAVAELQTQKAVNQEQRDRILKLSQEMEtaarSIESNVSQIKQM 898
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKK----RKRLSELKAKLEALEEELSEIEDPKGEDE----EIPEEELSLEDV 956
|
....*..
gi 1907132433 899 QTKIDEL 905
Cdd:TIGR02169 957 QAELQRV 963
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1157-1316 |
2.82e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1157 QSKEEENEISRQETEKLKEELaansiltQNLKADLQKkeedcaELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINEL 1236
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEI-------HKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLELLEKREEEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1237 EKKKNQYSQ---DLDMKQRTIQQLK-------EQLSNQKMEEAVQQYEKvckdlSVKEKLVEDMRLTLVEQEQtqaeqdr 1306
Cdd:PRK12704 113 EKKEKELEQkqqELEKKEEELEELIeeqlqelERISGLTAEEAKEILLE-----KVEEEARHEAAVLIKEIEE------- 180
|
170
....*....|
gi 1907132433 1307 vlEAKsEEAD 1316
Cdd:PRK12704 181 --EAK-EEAD 187
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
805-1184 |
2.90e-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: 42.42 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 805 TIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQiQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETA 884
Cdd:pfam17380 264 TMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEE-KAREVERRRKLEEAEKARQAEMDRQAAIYAEQERM 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 885 ARSIESNVSQIKQMQTK--IDELRSLDSPSHISKIDLLNLQDLSSGAKGDnclNTSQQLPGGdfsstwvKEYHTQEISRE 962
Cdd:pfam17380 343 AMERERELERIRQEERKreLERIRQEEIAMEISRMRELERLQMERQQKNE---RVRQELEAA-------RKVKILEEERQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 963 NSFHASIEAIWEECKEIVKAsskKSHQIQGLEE----QIEKLQVEVKGYREENSDLRAQESQGKnRDHQLKEKESLIQQL 1038
Cdd:pfam17380 413 RKIQQQKVEMEQIRAEQEEA---RQREVRRLEEerarEMERVRLEEQERQQQVERLRQQEEERK-RKKLELEKEKRDRKR 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1039 REELQEKSVslrvqvqlvaerEQALSELSQDVTCYKAKIKDLEvivetqkdecKRLVELEQSILEKESAILKLEANLKEC 1118
Cdd:pfam17380 489 AEEQRRKIL------------EKELEERKQAMIEEERKRKLLE----------KEMEERQKAIYEEERRREAEEERRKQQ 546
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907132433 1119 EAKHQDHIRTNDLSAKEVKFReevtrlannlhdtkqlLQSKEEENEISRQ--ETEKLKEELAANSILT 1184
Cdd:pfam17380 547 EMEERRRIQEQMRKATEERSR----------------LEAMEREREMMRQivESEKARAEYEATTPIT 598
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1157-1435 |
3.28e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1157 QSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINEL 1236
Cdd:pfam07888 55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1237 EKKKNQYSQDLDMKQRTIQQLKE---QLSNQKMEE---------AVQQYEKVCKDLSvkeKLVEDMRLTLVEQE-QTQAE 1303
Cdd:pfam07888 135 EEDIKTLTQRVLERETELERMKErakKAGAQRKEEeaerkqlqaKLQQTEEELRSLS---KEFQELRNSLAQRDtQVLQL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1304 QDRV--LEAKSEEADWLATELDKWKEKFKDLETR--SNQRLNTGTMDDLDVLTRKFSKLQDELQESE-------EKYKAD 1372
Cdd:pfam07888 212 QDTIttLTQKLTTAHRKEAENEALLEELRSLQERlnASERKVEGLGEELSSMAAQRDRTQAELHQARlqaaqltLQLADA 291
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907132433 1373 RKKWLEEKAvltTQAKEAENV-RNREMrkyadDRERCLKLQNEVETLTAQLAEKNSELQKWREE 1435
Cdd:pfam07888 292 SLALREGRA---RWAQERETLqQSAEA-----DKDRIEKLSAELQRLEERLQEERMEREKLEVE 347
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
115-183 |
3.80e-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: 3.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907132433 115 FSKVFGPETSQKEFFLGC--IMQPVKDLLEGHSrlIFTYGLTNSGKTYTFQgteeniGILPRTLNVLFDSL 183
Cdd:cd01363 22 FYRGFRRSESQPHVFAIAdpAYQSMLDGYNNQS--IFAYGESGAGKTETMK------GVIPYLASVAFNGI 84
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1177-1347 |
3.81e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1177 LAANSILTQNLKADLQKKEEDCAELKEKFIDAKKqiEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQ 1256
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAK--ELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1257 LKEQLSnqKMEEAVQQYEkvcKDLSVKEKLVED--MRLTLVEQEQTQAEQDRVLEAKSEEAdwLATELDKWKEKFKDLET 1334
Cdd:PRK12705 103 LENQLE--EREKALSARE---LELEELEKQLDNelYRVAGLTPEQARKLLLKLLDAELEEE--KAQRVKKIEEEADLEAE 175
|
170
....*....|...
gi 1907132433 1335 RSNQRLNTGTMDD 1347
Cdd:PRK12705 176 RKAQNILAQAMQR 188
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1260-1430 |
4.86e-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: 41.58 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1260 QLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSnqr 1339
Cdd:pfam05911 684 KRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQLKCMAESYEDLETRL--- 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1340 lnTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLttqakeaENVRNREMRKYADDRERcLKLQNEVETLT 1419
Cdd:pfam05911 761 --TELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQL-------ERNEKKESSNCDADQED-KKLQQEKEITA 830
|
170
....*....|.
gi 1907132433 1420 AqlAEKNSELQ 1430
Cdd:pfam05911 831 A--SEKLAECQ 839
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
1175-1273 |
5.00e-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: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1175 EELAANSILTQNLKADLQKKEEDC-AELKEKFIDAKKQIEQVQREVSVMRDEEKllRIKINELEKKKNQYSQDLDMKQRT 1253
Cdd:COG2825 32 QRILQESPEGKAAQKKLEKEFKKRqAELQKLEKELQALQEKLQKEAATLSEEER--QKKERELQKKQQELQRKQQEAQQD 109
|
90 100
....*....|....*....|...
gi 1907132433 1254 IQQLKEQLSNQ---KMEEAVQQY 1273
Cdd:COG2825 110 LQKRQQELLQPileKIQKAIKEV 132
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
984-1368 |
5.35e-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: 41.65 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 984 SKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQ----------LREELQEKSVSLRVQV 1053
Cdd:pfam05557 128 QSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSqeqdseivknSKSELARIPELEKELE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1054 QLVAEREQaLSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEqsiLEKEsailKLEANLKECEAKHQDHIRT----N 1129
Cdd:pfam05557 208 RLREHNKH-LNENIENKLLLKEEVEDLKRKLEREEKYREEAATLE---LEKE----KLEQELQSWVKLAQDTGLNlrspE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1130 DLSAK-------EVKFREEVTRLAN---NLHDTKQLLQ-------SKEEENEISRQETEKLKEELA-ANSILTQN---LK 1188
Cdd:pfam05557 280 DLSRRieqlqqrEIVLKEENSSLTSsarQLEKARRELEqelaqylKKIEDLNKKLKRHKALVRRLQrRVLLLTKErdgYR 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1189 ADLQKKEEDCAElKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEE 1268
Cdd:pfam05557 360 AILESYDKELTM-SNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSY 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1269 AVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQD----------RVL-----------EAKSEEADWLATELDKWKE 1327
Cdd:pfam05557 439 SKEEVDSLRRKLETLELERQRLREQKNELEMELERRClqgdydpkktKVLhlsmnpaaeayQQRKNQLEKLQAEIERLKR 518
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1907132433 1328 KFKDLETrSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEK 1368
Cdd:pfam05557 519 LLKKLED-DLEQVLRLPETTSTMNFKEVLDLRKELESAELK 558
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1133-1260 |
5.68e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1133 AKEV--KFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDcaELKEKFIDAKK 1210
Cdd:PRK00409 507 AKKLigEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK--EAQQAIKEAKK 584
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1211 QIEQVQREVSVMRDEEKlLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQ 1260
Cdd:PRK00409 585 EADEIIKELRQLQKGGY-ASVKAHELIEARKRLNKANEKKEKKKKKQKEK 633
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
993-1309 |
5.86e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 993 LEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVaEREQALSELSqDVTc 1072
Cdd:PRK04863 360 LEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQAL-ERAKQLCGLP-DLT- 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1073 ykakIKDLEVIVETQKDECKRLVEleqsilekesAILKLEANLKECEAKHQDHIRTNDLSAKEV----------KFREEV 1142
Cdd:PRK04863 437 ----ADNAEDWLEEFQAKEQEATE----------ELLSLEQKLSVAQAAHSQFEQAYQLVRKIAgevsrseawdVARELL 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1143 TRLANNLHDTKQLLQSKEEENEISR-----QETEKLKEELAANSILTQNLKADLQKKEEdcaELKEKFIDAKKQIEQVQR 1217
Cdd:PRK04863 503 RRLREQRHLAEQLQQLRMRLSELEQrlrqqQRAERLLAEFCKRLGKNLDDEDELEQLQE---ELEARLESLSESVSEARE 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1218 EVSVMRDEEKLLRIKINELEKKKNQYSQdldmKQRTIQQLKEQ-----LSNQKMEEAVQQyekvckdlsvkekLVEDMRL 1292
Cdd:PRK04863 580 RRMALRQQLEQLQARIQRLAARAPAWLA----AQDALARLREQsgeefEDSQDVTEYMQQ-------------LLERERE 642
|
330
....*....|....*..
gi 1907132433 1293 TLVEQEQTQAEQDRVLE 1309
Cdd:PRK04863 643 LTVERDELAARKQALDE 659
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1032-1262 |
5.88e-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: 41.03 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1032 ESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKL 1111
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1112 EANLKEceakhqdhiRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADL 1191
Cdd:pfam07888 110 SEELSE---------EKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1192 QKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKIN-------ELEKKKNQYS---QDLDMKQRTIQQLKEQL 1261
Cdd:pfam07888 181 QQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTtahrkeaENEALLEELRslqERLNASERKVEGLGEEL 260
|
.
gi 1907132433 1262 S 1262
Cdd:pfam07888 261 S 261
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1184-1276 |
6.48e-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: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1184 TQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQD-LDMKQRT--IQQLKEQ 1260
Cdd:pfam13851 21 TRNNLELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDkQSLKNLKarLKVLEKE 100
|
90
....*....|....*...
gi 1907132433 1261 LSNQKMEEAV--QQYEKV 1276
Cdd:pfam13851 101 LKDLKWEHEVleQRFEKV 118
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
984-1274 |
7.12e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 984 SKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNrdhQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQAL 1063
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEE---ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1064 SELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVKFREEVT 1143
Cdd:COG4372 104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1144 RLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMR 1223
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907132433 1224 DEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYE 1274
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1304-1477 |
7.39e-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: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1304 QDRVLEAKSEEA----DWLATELDKWKEKFKDLETRSNQ-RLNTGTMD---DLDVLTRKFSKLQDELQESEEKYKADRKK 1375
Cdd:COG3206 162 LEQNLELRREEArkalEFLEEQLPELRKELEEAEAALEEfRQKNGLVDlseEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1376 WLEEKAVLTTQAKEAENVRNREMrkYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQMKALLSSCK 1455
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPV--IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLE 319
|
170 180 190
....*....|....*....|....*....|...
gi 1907132433 1456 HK-----------DEEIQELRKAAAKSTGTENQ 1477
Cdd:COG3206 320 AElealqareaslQAQLAQLEARLAELPELEAE 352
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1145-1275 |
8.37e-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: 39.50 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1145 LANNLHDTKQLlqsKEEENEISRQET--EKLKEELAANSiltQNLKADLQKKEEDCAEL----------KEKFIDAKKQI 1212
Cdd:pfam13851 21 TRNNLELIKSL---KEEIAELKKKEErnEKLMSEIQQEN---KRLTEPLQKAQEEVEELrkqlenyekdKQSLKNLKARL 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907132433 1213 EQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQ---LKEQLSNQKMEEAVQQYEK 1275
Cdd:pfam13851 95 KVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQktgLKNLLLEKKLQALGETLEK 160
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
568-1267 |
9.00e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 568 HKKNKELLDLIEklnkrLINENKEKLTLELKIREEVTQEFtqywsqreaDFKETLLHEREILEENAERRLaifkdlvgkc 647
Cdd:COG5022 806 LGSRKEYRSYLA-----CIIKLQKTIKREKKLRETEEVEF---------SLKAEVLIQKFGRSLKAKKRF---------- 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 648 dsqdeptnricdiELETEEAIAClqlkfnQVKAELAETKEELIKAQEElkNRESNSLVQalkTSSKVDTSLTSNKSTCNe 727
Cdd:COG5022 862 -------------SLLKKETIYL------QSAQRVELAERQLQELKID--VKSISSLKL---VNLELESEIIELKKSLS- 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 728 TSEMPKNSRAQTHSERKRLNEDGLQLGEPPAKkglilvsppiteeqnkMGEMQQSVSEVVEGNRVLKEKNEELKRLL--- 804
Cdd:COG5022 917 SDLIENLEFKTELIARLKKLLNNIDLEEGPSI----------------EYVKLPELNKLHEVESKLKETSEEYEDLLkks 980
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 805 TIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRaDVEQIQASYNSAVAELQTQKAV----NQEQRDRILKLSQE 880
Cdd:COG5022 981 TILVREGNKANSELKNFKKELAELSKQYGALQESTKQLK-ELPVEVAELQSASKIISSESTElsilKPLQKLKGLLLLEN 1059
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 881 METAARSIESNV---------SQIKQMQT----------KIDELRSLDSPSHISKIDLLNLQDLSSGAKGD---NCLNTS 938
Cdd:COG5022 1060 NQLQARYKALKLrrensllddKQLYQLEStenllktinvKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEiskFLSQLV 1139
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 939 QQLPgGDFSSTWVKEYHTQEISRENSFHASIEAIWEecKEIVKASSKKSHqiqGLEEQIEKLQVEVKGYREENSDLRAQE 1018
Cdd:COG5022 1140 NTLE-PVFQKLSVLQLELDGLFWEANLEALPSPPPF--AALSEKRLYQSA---LYDEKSKLSSSEVNDLKNELIALFSKI 1213
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1019 SQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAER----EQALSELSQDVTCYKAKIKDLEVIVETQKDECKRL 1094
Cdd:COG5022 1214 FSGWPRGDKLKKLISEGWVPTEYSTSLKGFNNLNKKFDTPAsmsnEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYI 1293
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1095 -VELEQSILEKESAIlkleanlkecEAKHQDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKL 1173
Cdd:COG5022 1294 nVGLFNALRTKASSL----------RWKSATEVNYNSEELDDWCREFEISDVDEELEELIQAVKVLQLLKDDLNKLDELL 1363
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 1174 KEELAANSILTQNLKADLQKKEEDcAELKEKF---IDAKKQIEQVQREVSVMRDEEKLLRiKINELEKKKNQYSQDLDMK 1250
Cdd:COG5022 1364 DACYSLNPAEIQNLKSRYDPADKE-NNLPKEIlkkIEALLIKQELQLSLEGKDETEVHLS-EIFSEEKSLISLDRNSIYK 1441
|
730
....*....|....*..
gi 1907132433 1251 QRTIQQLKEQLSNQKME 1267
Cdd:COG5022 1442 EEVLSSLSALLTKEKIA 1458
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
793-906 |
9.67e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132433 793 LKEKNEELKRLltigENELRNEKEEKAELNKQVVSLQQQLR--------FFEEKN--------SSLRADVEQIQASyNSA 856
Cdd:COG4913 612 LAALEAELAEL----EEELAEAEERLEALEAELDALQERREalqrlaeySWDEIDvasaereiAELEAELERLDAS-SDD 686
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1907132433 857 VAELQTQKAVNQEQRDRilkLSQEMETAARSIESNVSQIKQMQTKIDELR 906
Cdd:COG4913 687 LAALEEQLEELEAELEE---LEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
|
| |
