|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
6-327 |
0e+00 |
|
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: 655.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 6 ECSIKVMCRFRPLNEAEILRGDKFIPKFKGEETVVIG---QGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTI 82
Cdd:cd01369 1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIAtseTGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 83 FAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNR 162
Cdd:cd01369 81 FAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLDVSKTNLSVHEDKNR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 163 VPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEKVSKT 242
Cdd:cd01369 161 GPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEKVSKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 243 GAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQ 322
Cdd:cd01369 241 GAEGAVLDEAKKINKSLSALGNVINALTDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQ 320
|
....*
gi 45433560 323 RAKTI 327
Cdd:cd01369 321 RAKTI 325
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
8-334 |
1.04e-154 |
|
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: 458.96 E-value: 1.04e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 8 SIKVMCRFRPLNEAEILRGDKFIPKF--KGEETVVIGQGKP------YVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYN 79
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFpdKVGKTLTVRSPKNrqgekkFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 80 GTIFAYGQTSSGKTHTMEGklhDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHED 159
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIG---TPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSKKLEIRED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 160 KNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQE--NVETEKKLSGKLYLVDLAGSE 237
Cdd:smart00129 158 EKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKikNSSSGSGKASKLNLVDLAGSE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 238 KVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTK-THVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKS 316
Cdd:smart00129 238 RAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKsRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLS 317
|
330
....*....|....*...
gi 45433560 317 TLMFGQRAKTIKNTVSVN 334
Cdd:smart00129 318 TLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
14-327 |
2.54e-154 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 457.81 E-value: 2.54e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 14 RFRPLNEAEILRGDKFI-----PKFKGEETVVIGQGKP---YVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAY 85
Cdd:pfam00225 1 RVRPLNEREKERGSSVIvsvesVDSETVESSHLTNKNRtktFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 86 GQTSSGKTHTMEGKLHDPqlmGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTN---LAVHEDKNR 162
Cdd:pfam00225 81 GQTGSGKTYTMEGSDEQP---GIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNkrkLRIREDPKK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 163 VPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKK---LSGKLYLVDLAGSEKV 239
Cdd:pfam00225 158 GVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEesvKTGKLNLVDLAGSERA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 240 SKTG-AEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTL 318
Cdd:pfam00225 238 SKTGaAGGQRLKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTL 317
|
....*....
gi 45433560 319 MFGQRAKTI 327
Cdd:pfam00225 318 RFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
8-325 |
1.38e-153 |
|
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: 455.95 E-value: 1.38e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 8 SIKVMCRFRPLNEAEILRGDKFIpKFKGEETVVIG-------QGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNG 80
Cdd:cd00106 1 NVRVAVRVRPLNGREARSAKSVI-SVDGGKSVVLDppknrvaPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 81 TIFAYGQTSSGKTHTMEGKlhDPQLMGIIPRIAHDIFDHIYSMDE-NLEFHIKVSYFEIYLDKIRDLLD-VSKTNLAVHE 158
Cdd:cd00106 80 TIFAYGQTGSGKTYTMLGP--DPEQRGIIPRALEDIFERIDKRKEtKSSFSVSASYLEIYNEKIYDLLSpVPKKPLSLRE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 159 DKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVET--EKKLSGKLYLVDLAGS 236
Cdd:cd00106 158 DPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKsgESVTSSKLNLVDLAGS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 237 EKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKS 316
Cdd:cd00106 238 ERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLS 317
|
....*....
gi 45433560 317 TLMFGQRAK 325
Cdd:cd00106 318 TLRFASRAK 326
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
8-327 |
2.40e-119 |
|
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: 367.04 E-value: 2.40e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 8 SIKVMCRFRPLNEAEILRGDKFIPKFkGEETVVIGQ--GKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAY 85
Cdd:cd01374 1 KITVTVRVRPLNSREIGINEQVAWEI-DNDTIYLVEppSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 86 GQTSSGKTHTMEGKLHDPqlmGIIPRIAHDIFDHIYsMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNRVPY 165
Cdd:cd01374 80 GQTSSGKTFTMSGDEDEP---GIIPLAIRDIFSKIQ-DTPDREFLLRVSYLEIYNEKINDLLSPTSQNLKIRDDVEKGVY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 166 VKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIK---QENVETEKKLSGKLYLVDLAGSEKVSKT 242
Cdd:cd01374 156 VAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIEsseRGELEEGTVRVSTLNLIDLAGSERAAQT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 243 GAEGAVLDEAKNINKSLSALGNVISALAEGTK-THVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFG 321
Cdd:cd01374 236 GAAGVRRKEGSHINKSLLTLGTVISKLSEGKVgGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFA 315
|
....*.
gi 45433560 322 QRAKTI 327
Cdd:cd01374 316 SRAKKI 321
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
7-328 |
5.75e-119 |
|
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: 366.66 E-value: 5.75e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 7 CSIKVMCRFRPLNEAEILRGDK----FIPkfkGEETVVIGQGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTI 82
Cdd:cd01372 1 SSVRVAVRVRPLLPKEIIEGCRicvsFVP---GEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 83 FAYGQTSSGKTHTMEG----KLHDPQlMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLD---VSKTNLA 155
Cdd:cd01372 78 LAYGQTGSGKTYTMGTaytaEEDEEQ-VGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDpetDKKPTIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 156 VHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSG--------- 226
Cdd:cd01372 157 IREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSaddknstft 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 227 -KLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTK--THVPYRDSKMTRILQDSLGGNCRTTIVIC 303
Cdd:cd01372 237 sKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKkgAHVPYRDSKLTRLLQDSLGGNSHTLMIAC 316
|
330 340
....*....|....*....|....*
gi 45433560 304 CSPSVFNEAETKSTLMFGQRAKTIK 328
Cdd:cd01372 317 VSPADSNFEETLNTLKYANRARNIK 341
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
8-327 |
9.58e-113 |
|
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: 350.22 E-value: 9.58e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 8 SIKVMCRFRPLNEAEILRGDK---FIPKFKGEETVVIGQG------KPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGY 78
Cdd:cd01371 2 NVKVVVRCRPLNGKEKAAGALqivDVDEKRGQVSVRNPKAtaneppKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 79 NGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLL--DVSKtNLAV 156
Cdd:cd01371 82 NGTIFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLgkDQTK-RLEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 157 HEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLS---GKLYLVDL 233
Cdd:cd01371 161 KERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENHirvGKLNLVDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 234 AGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAE 313
Cdd:cd01371 241 AGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDE 320
|
330
....*....|....
gi 45433560 314 TKSTLMFGQRAKTI 327
Cdd:cd01371 321 TLSTLRYANRAKNI 334
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
9-329 |
2.81e-108 |
|
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: 338.03 E-value: 2.81e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 9 IKVMCRFRPLNEAEILRGDKFI--PKFKGEETVVIGQG---KPYVFDRVLPPNTTQEQVYNAcAKQIVKDVLEGYNGTIF 83
Cdd:cd01366 4 IRVFCRVRPLLPSEENEDTSHItfPDEDGQTIELTSIGakqKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCIF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 84 AYGQTSSGKTHTMEGklhDPQLMGIIPRIAHDIFDHIYSMDEN-LEFHIKVSYFEIYLDKIRDLL---DVSKTNLAVHED 159
Cdd:cd01366 83 AYGQTGSGKTYTMEG---PPESPGIIPRALQELFNTIKELKEKgWSYTIKASMLEIYNETIRDLLapgNAPQKKLEIRHD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 160 K-NRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEK 238
Cdd:cd01366 160 SeKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGSER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 239 VSKTGAEGAVLDEAKNINKSLSALGNVISALAEGtKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTL 318
Cdd:cd01366 240 LNKSGATGDRLKETQAINKSLSALGDVISALRQK-QSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSL 318
|
330
....*....|.
gi 45433560 319 MFGQRAKTIKN 329
Cdd:cd01366 319 RFASKVNSCEL 329
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
8-334 |
9.45e-102 |
|
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: 322.38 E-value: 9.45e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 8 SIKVMCRFRPLNEAEILRGDKFIPKFKGEETVVI-------------GQGKPYVFDRVL-------PPNTTQEQVYNACA 67
Cdd:cd01365 2 NVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKnpkqadknnkatrEVPKSFSFDYSYwshdsedPNYASQEQVYEDLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 68 KQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGklhDPQLMGIIPRIAHDIFDHIYSM-DENLEFHIKVSYFEIYLDKIRDL 146
Cdd:cd01365 82 EELLQHAFEGYNVCLFAYGQTGSGKSYTMMG---TQEQPGIIPRLCEDLFSRIADTtNQNMSYSVEVSYMEIYNEKVRDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 147 LDVS----KTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEK 222
Cdd:cd01365 159 LNPKpkknKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAET 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 223 KLSG----KLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE-------GTKTHVPYRDSKMTRILQDS 291
Cdd:cd01365 239 NLTTekvsKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADmssgkskKKSSFIPYRDSVLTWLLKEN 318
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 45433560 292 LGGNCRTTIVICCSPSVFNEAETKSTLMFGQRAKTIKNTVSVN 334
Cdd:cd01365 319 LGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
8-327 |
1.44e-99 |
|
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: 315.82 E-value: 1.44e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 8 SIKVMCRFRPLNEAEILRGDK------------FIPKFKGEETVVIGQG-----------KPYVFDRVLPPNTTQEQVYN 64
Cdd:cd01370 1 SLTVAVRVRPFSEKEKNEGFRrivkvmdnhmlvFDPKDEEDGFFHGGSNnrdrrkrrnkeLKYVFDRVFDETSTQEEVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 65 ACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPqlmGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIR 144
Cdd:cd01370 81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEP---GLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 145 DLLDVSKTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQEN---VETE 221
Cdd:cd01370 158 DLLNPSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDktaSINQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 222 KKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTK--THVPYRDSKMTRILQDSLGGNCRTT 299
Cdd:cd01370 238 QVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKknKHIPYRDSKLTRLLKDSLGGNCRTV 317
|
330 340
....*....|....*....|....*...
gi 45433560 300 IVICCSPSVFNEAETKSTLMFGQRAKTI 327
Cdd:cd01370 318 MIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
6-334 |
1.13e-95 |
|
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: 305.79 E-value: 1.13e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 6 ECSIKVMCRFRPLNEAEILRGDKFIPKFKG-EETVVIGQG--------KPYVFDRVLPPNTTQEQVYNACAKQIVKDVLE 76
Cdd:cd01364 1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPvRKEVSVRTGgladksstKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 77 GYNGTIFAYGQTSSGKTHTMEGK--------LHDPQLMGIIPRIAHDIFDHIYSMDEnlEFHIKVSYFEIYLDKIRDLLD 148
Cdd:cd01364 81 GYNCTIFAYGQTGTGKTYTMEGDrspneeytWELDPLAGIIPRTLHQLFEKLEDNGT--EYSVKVSYLEIYNEELFDLLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 149 VS---KTNLAVHEDKNRVP--YVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLI--NIKQENVETE 221
Cdd:cd01364 159 PSsdvSERLRMFDDPRNKRgvIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSItiHIKETTIDGE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 222 KKLS-GKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKtHVPYRDSKMTRILQDSLGGNCRTTI 300
Cdd:cd01364 239 ELVKiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAP-HVPYRESKLTRLLQDSLGGRTKTSI 317
|
330 340 350
....*....|....*....|....*....|....
gi 45433560 301 VICCSPSVFNEAETKSTLMFGQRAKTIKNTVSVN 334
Cdd:cd01364 318 IATISPASVNLEETLSTLEYAHRAKNIKNKPEVN 351
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
9-334 |
5.40e-88 |
|
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: 285.17 E-value: 5.40e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 9 IKVMCRFRPLNEAEILRGDKFIPKFKGEETVVIGQGKP--YVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAYG 86
Cdd:cd01373 3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKPPktFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 87 QTSSGKTHTMEGKLHDP-----QLMGIIPRIAHDIFDHI----YSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVH 157
Cdd:cd01373 83 QTGSGKTYTMWGPSESDnesphGLRGVIPRIFEYLFSLIqrekEKAGEGKSFLCKCSFLEIYNEQIYDLLDPASRNLKLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 158 EDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIkqENVETEKKLS----GKLYLVDL 233
Cdd:cd01373 163 EDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTI--ESWEKKACFVnirtSRLNLVDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 234 AGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE---GTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFN 310
Cdd:cd01373 241 AGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvahGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSKC 320
|
330 340
....*....|....*....|....
gi 45433560 311 EAETKSTLMFGQRAKTIKNTVSVN 334
Cdd:cd01373 321 FGETLSTLRFAQRAKLIKNKAVVN 344
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
47-334 |
7.83e-85 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 283.94 E-value: 7.83e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 47 YVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPqlmGIIPRIAHDIFDHIYSMDEN 126
Cdd:COG5059 58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEP---GIIPLSLKELFSKLEDLSMT 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 127 LEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSH 206
Cdd:COG5059 135 KDFAVSISYLEIYNEKIYDLLSPNEESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSH 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 207 SIFLINIKQENVETEKKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKT-HVPYRDSKMT 285
Cdd:COG5059 215 SIFQIELASKNKVSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSgHIPYRESKLT 294
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 45433560 286 RILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQRAKTIKNTVSVN 334
Cdd:COG5059 295 RLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVN 343
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
9-325 |
5.91e-77 |
|
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: 255.40 E-value: 5.91e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 9 IKVMCRFRPLNEAEILRGDKFIPKFKGEETVVI-------------GQGKP---YVFDRVLPPNTTQEQVYNACAKQIVK 72
Cdd:cd01368 3 VKVYLRVRPLSKDELESEDEGCIEVINSTTVVLhppkgsaankserNGGQKetkFSFSKVFGPNTTQKEFFQGTALPLVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 73 DVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPqlmGIIPRIAHDIFDHIYsmdenlEFHIKVSYFEIYLDKIRDLLDVS-- 150
Cdd:cd01368 83 DLLHGKNGLLFTYGVTNSGKTYTMQGSPGDG---GILPRSLDVIFNSIG------GYSVFVSYIEIYNEYIYDLLEPSps 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 151 -----KTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLS 225
Cdd:cd01368 154 sptkkRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDGDVD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 226 --------GKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE----GTKTHVPYRDSKMTRILQDSLG 293
Cdd:cd01368 234 qdkdqitvSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLREnqlqGTNKMVPFRDSKLTHLFQNYFD 313
|
330 340 350
....*....|....*....|....*....|..
gi 45433560 294 GNCRTTIVICCSPSVFNEAETKSTLMFGQRAK 325
Cdd:cd01368 314 GEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
49-325 |
2.18e-74 |
|
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: 247.88 E-value: 2.18e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 49 FDRVLPpNTTQEQVYNACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIySMDENLE 128
Cdd:cd01375 52 FDGVLH-NASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENYKHRGIIPRALQQVFRMI-EERPTKA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 129 FHIKVSYFEIYLDKIRDLLDV------SKTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHS 202
Cdd:cd01375 130 YTVHVSYLEIYNEQLYDLLSTlpyvgpSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 203 SRSHSIFLINIKQENVE--TEKKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYR 280
Cdd:cd01375 210 SRSHCIFTIHLEAHSRTlsSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDRTHVPFR 289
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 45433560 281 DSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQRAK 325
Cdd:cd01375 290 QSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
9-325 |
2.41e-71 |
|
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: 238.94 E-value: 2.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 9 IKVMCRFRPLNEAEILRGDKFIPKFKGEETVVI------GQGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTI 82
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVELadprnhGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNATV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 83 FAYGQTSSGKTHTMEGklhDPQLMGIIPRIAHDIFDHIYSMDENLEFhiKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNR 162
Cdd:cd01376 82 FAYGSTGAGKTFTMLG---SPEQPGLMPLTVMDLLQMTRKEAWALSF--TMSYLEIYQEKILDLLEPASKELVIREDKDG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 163 VPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLIN-IKQENVETEKKLSGKLYLVDLAGSEKVSK 241
Cdd:cd01376 157 NILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKvDQRERLAPFRQRTGKLNLIDLAGSEDNRR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 242 TGAEGAVLDEAKNINKSLSALGNVISALAEGTKtHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFG 321
Cdd:cd01376 237 TGNEGIRLKESGAINSSLFVLSKVVNALNKNLP-RIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFA 315
|
....
gi 45433560 322 QRAK 325
Cdd:cd01376 316 ARSR 319
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
9-325 |
4.10e-70 |
|
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: 236.04 E-value: 4.10e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 9 IKVMCRFRPLNEAEILRGDKFIPKFKGEETVVIGQGK------------PYVFDRVLPPNTTQEQVYNACAKQIVKDVLE 76
Cdd:cd01367 2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHEPKlkvdltkyienhTFRFDYVFDESSSNETVYRSTVKPLVPHIFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 77 GYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIA-HDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDvSKTNLA 155
Cdd:cd01367 82 GGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALAaRDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLLN-RKKRVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 156 VHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENvetEKKLSGKLYLVDLAG 235
Cdd:cd01367 161 LREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRG---TNKLHGKLSFVDLAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 236 SEKVSKTGAEGA-VLDEAKNINKSLSALGNVISALAEGtKTHVPYRDSKMTRILQDSL-GGNCRTTIVICCSPSVFNEAE 313
Cdd:cd01367 238 SERGADTSSADRqTRMEGAEINKSLLALKECIRALGQN-KAHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEH 316
|
330
....*....|..
gi 45433560 314 TKSTLMFGQRAK 325
Cdd:cd01367 317 TLNTLRYADRVK 328
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
5-337 |
6.37e-62 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 229.82 E-value: 6.37e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 5 AECSIKVMCRFRPLNEAEilRGDKFIPKFKGEETVVIGQgkPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFA 84
Cdd:PLN03188 96 SDSGVKVIVRMKPLNKGE--EGEMIVQKMSNDSLTINGQ--TFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 85 YGQTSSGKTHTMEGK---LHDPQL----MGIIPRIAHDIFDHIYS-----MDENLEFHIKVSYFEIYLDKIRDLLDVSKT 152
Cdd:PLN03188 172 YGQTGSGKTYTMWGPangLLEEHLsgdqQGLTPRVFERLFARINEeqikhADRQLKYQCRCSFLEIYNEQITDLLDPSQK 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 153 NLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSG----KL 228
Cdd:PLN03188 252 NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVADGLSSfktsRI 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 229 YLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE----GTKTHVPYRDSKMTRILQDSLGGNCRTTIVICC 304
Cdd:PLN03188 332 NLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAI 411
|
330 340 350
....*....|....*....|....*....|...
gi 45433560 305 SPSVFNEAETKSTLMFGQRAKTIKNTVSVNLEL 337
Cdd:PLN03188 412 SPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVM 444
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
11-306 |
1.98e-45 |
|
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: 160.97 E-value: 1.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 11 VMCRFRPLNEAEILRGDKFIpkfkgeetvvigqgkpyVFDRVLPPNTTQEQVYNACAKqIVKDVLEGYNG-TIFAYGQTS 89
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKII-----------------VFYRGFRRSESQPHVFAIADP-AYQSMLDGYNNqSIFAYGESG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 90 SGKTHTMegklhdpqlMGIIPRIAHDIFDHIYSMDENLEFHikvsyfeiyldkirdlldvsktnlavhedknrvpyvkgC 169
Cdd:cd01363 63 AGKTETM---------KGVIPYLASVAFNGINKGETEGWVY--------------------------------------L 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 170 TERFVSSPEEVMDVIDEGKANRhVAVTNMNEHSSRSHSIFLInikqenvetekklsgklyLVDLAGSEkvsktgaegavl 249
Cdd:cd01363 96 TEITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------------LLDIAGFE------------ 144
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 45433560 250 deakNINKSLSALGNVISAlaegtkthvpyrdskmtrilqdslggnCRTTIVICCSP 306
Cdd:cd01363 145 ----IINESLNTLMNVLRA---------------------------TRPHFVRCISP 170
|
|
| Khc_CBD_cc |
cd23649 |
cargo binding coiled-coil domain found in kinesin heavy chains; The family includes Drosophila ... |
835-904 |
1.16e-22 |
|
cargo binding coiled-coil domain found in kinesin heavy chains; The family includes Drosophila kinesin-1, also called kinesin heavy chain (Khc), and Homo sapiens kinesin-1 heavy chain, also called conventional kinesin heavy chain/ubiquitous kinesin heavy chain (UKHC). Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Milt and Miro form an essential protein complex that links Khc to mitochondria for light chain-independent, anterograde transport of mitochondria. The family also includes kinesin heavy chain isoform 5A (KIF5A), also called kinesin heavy chain neuron-specific 1/neuronal kinesin heavy chain (NKHC1), and kinesin heavy chain isoform 5C (KIF5C), also called kinesin heavy chain neuron-specific 2 (NKHC2). KIF5A is a microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH, NFM and NFL). It can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner. KIF5C is involved in synaptic transmission and mediates dendritic trafficking of mRNAs. Khc comprises an N-terminal motor-domain, followed by a long coiled-coil stalk that mediates homodimerization, and an unstructured tail with regulatory function. The stalk includes the kinesin light chain (Klc) binding region and an alternative cargo binding region. The model corresponds to the cargo binding region, which is responsible for binding of the atypical tropomyosin, aTm1, a cargo adaptor that plays a stabilizing role in the interaction of Khc with RNA.
Pssm-ID: 467880 [Multi-domain] Cd Length: 70 Bit Score: 92.26 E-value: 1.16e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 835 FLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIK 904
Cdd:cd23649 1 FLERNLEQLTLVQKQLVRQNSTLKKELALAEKKLAARNERIKSLEALLKEAQEKLEKQNQKFEEQLQRLR 70
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
7-147 |
7.72e-22 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 92.67 E-value: 7.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 7 CSIKVMCRFRP--LNEAEILRGDKFIpkfkgEETVVIGQGKPYVFDRVLPPNTTQEQVYNACaKQIVKDVLEGYNGTIFA 84
Cdd:pfam16796 20 GNIRVFARVRPelLSEAQIDYPDETS-----SDGKIGSKNKSFSFDRVFPPESEQEDVFQEI-SQLVQSCLDGYNVCIFA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45433560 85 YGQTSSGKTHTMegklhdpqlmgiIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLL 147
Cdd:pfam16796 94 YGQTGSGSNDGM------------IPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQDLL 144
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
616-923 |
2.36e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.67 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 616 RKMNASERELAACQLLISQHEAKIKSLtdymqnmEQKRRQLEESQDsLSEELAKLRAQEKMHEVSFQDKEKEHLT----R 691
Cdd:COG1196 179 RKLEATEENLERLEDILGELERQLEPL-------ERQAEKAERYRE-LKEELKELEAELLLLKLRELEAELEELEaeleE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 692 LQDAEEVKKALEQQMESHREAHQKQLSRLRDEIEEKQ----RIIDEIRDLNQKLQLEQERLSSDYNKLKIEDQEREVKLE 767
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQaeeyELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 768 KLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDSDDGGGSAAQKQKISfLENNLEQLTKVH 847
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE-LAAQLEELEEAE 409
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45433560 848 KQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIAK 923
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
399-906 |
3.05e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 399 IDNITPVVDGISAEKEKYDEEitslYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQ----- 473
Cdd:PRK03918 209 INEISSELPELREELEKLEKE----VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvke 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 474 -----------IENEAAKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQElsnhq 542
Cdd:PRK03918 285 lkelkekaeeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE----- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 543 KKRATEILNLLLKDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMdsnrKMNASE 622
Cdd:PRK03918 360 RHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE----ELKKAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 623 RELAACQLLISQHE---------AKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQ 693
Cdd:PRK03918 436 GKCPVCGRELTEEHrkelleeytAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKY 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 694 DAEEVKKALEQQMESHREAH--QKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLSSDYNKLkiedqerevkleklll 771
Cdd:PRK03918 516 NLEELEKKAEEYEKLKEKLIklKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL---------------- 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 772 lndkREQAREDLKGLEETVsRELQTLHN--LRKLFVQDLTTRVKKSVELDSDDgggSAAQKQKISFLENNLEQLTKVHKQ 849
Cdd:PRK03918 580 ----EELGFESVEELEERL-KELEPFYNeyLELKDAEKELEREEKELKKLEEE---LDKAFEELAETEKRLEELRKELEE 651
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45433560 850 LVR-----DNADLRCELPKLEKRLRATAERVKALESALKEAKENA------MRDRKRYQQEVDRIKEA 906
Cdd:PRK03918 652 LEKkyseeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLeklkeeLEEREKAKKELEKLEKA 719
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
407-906 |
8.76e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 8.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 407 DGISAEKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEV 486
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 487 LQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIgT 566
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL-R 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 567 NDVKTLADVNGVIEEEFTMARLyISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYM 646
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLER-LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 647 QNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEVKKALEQQMESHREAHQK---QLSRLRDE 723
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEaalAAALQNIV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 724 IEEKQRIIDEIRDLNQKLQLEQERLSSDynklKIEDQEREVKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHnLRKL 803
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLD----KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL-GRTL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 804 FVQDLTTRVKKSVELD------SDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADlrcELPKLEKRLRATAERVKA 877
Cdd:COG1196 628 VAARLEAALRRAVTLAgrlrevTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE---RLAEEELELEEALLAEEE 704
|
490 500
....*....|....*....|....*....
gi 45433560 878 LESALKEAKENAMRDRKRYQQEVDRIKEA 906
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAE 733
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
596-886 |
2.34e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 596 EVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEakiksltDYMQNMEQKRRQLEESQDSLSEELAKLRAQEK 675
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR-------LEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 676 MHEVSFQdkekehltRLQDAEEVKKALEQQMESHREAHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLssdynKL 755
Cdd:TIGR02168 306 ILRERLA--------NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL-----ES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 756 KIEDQErevklekllllnDKREQAREDLKGLEETVSRELQTLHNLRKLfVQDLTTRVKKSVELDSDDggGSAAQKQKISF 835
Cdd:TIGR02168 373 RLEELE------------EQLETLRSKVAQLELQIASLNNEIERLEAR-LERLEDRRERLQQEIEEL--LKKLEEAELKE 437
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 45433560 836 LENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAK 886
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
592-906 |
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: 65.47 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 592 KMKSEVKSLVNRSKQLEsaqmdsnRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAkLR 671
Cdd:TIGR02169 220 KREYEGYELLKEKEALE-------RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-LR 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 672 AQEKMHEV-----SFQDKEKEHLTRLQDAEEVKKALEQQMESHREAHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQE 746
Cdd:TIGR02169 292 VKEKIGELeaeiaSLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 747 RLSSDYNKLKIEDQEREVKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRklfvQDLTTRVKKSVELDSDdgggS 826
Cdd:TIGR02169 372 ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKINELEEE----K 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 827 AAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRAtaervKALESALKEAKENAMRDRKRYQQEVDRIKEA 906
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK-----LQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
409-797 |
2.02e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 409 ISAEKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQ 488
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 489 ALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTT-TQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTN 567
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEaAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 568 -----------DVKTLADVNGVIEEEFTMARLYISKMKSEVKSLV-----NRSKQLESAQMDSNRKMNASERELAACQL- 630
Cdd:COG1196 530 igveaayeaalEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtflplDKIRARAALAAALARGAIGAAVDLVASDLr 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 631 -------LISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMhevsFQDKEKEHLTRLQDAEEVKKALE 703
Cdd:COG1196 610 eadaryyVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSL----TGGSRRELLAALLEAEAELEELA 685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 704 QQMESHREAHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLSSDYNKLKIEDQEREVKLEKLLLLNDKREQAREDL 783
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL 765
|
410
....*....|....
gi 45433560 784 KGLEETVSRELQTL 797
Cdd:COG1196 766 ERELERLEREIEAL 779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
590-906 |
3.89e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 3.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 590 ISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAK 669
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 670 L-----RAQEKMHEVSFQDKE-KEHLTRLQDAEEVKKALEQQMESHREAHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQL 743
Cdd:TIGR02168 328 LeskldELAEELAELEEKLEElKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 744 EQERLSSDYNKLK--IEDQEREVKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDSd 821
Cdd:TIGR02168 408 RLERLEDRRERLQqeIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ- 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 822 dgggSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKEN-AMRDRKRYQQEV 900
Cdd:TIGR02168 487 ----LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAvVVENLNAAKKAI 562
|
....*.
gi 45433560 901 DRIKEA 906
Cdd:TIGR02168 563 AFLKQN 568
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
407-751 |
4.44e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 407 DGISAEKEKYDEEITSLYRQLDDKDDEINQQSQLAE--KLKQQMLDQDELLASTRRDYEKIQEeltrLQIENEAAKDEVK 484
Cdd:COG4717 98 EELEEELEELEAELEELREELEKLEKLLQLLPLYQEleALEAELAELPERLEELEERLEELRE----LEEELEELEAELA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 485 EVLQALEELAVNYD-QKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQE--------LSNHQKKRATEILNLLLK 555
Cdd:COG4717 174 ELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEeleqleneLEAAALEERLKEARLLLL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 556 DLGEIGGIIGTNDV--KTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLIS 633
Cdd:COG4717 254 IAAALLALLGLGGSllSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 634 QHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEK-----EHLTRLQDAEEVKKALEQQMES 708
Cdd:COG4717 334 LSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEElraalEQAEEYQELKEELEELEEQLEE 413
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 45433560 709 H------------REAHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLSSD 751
Cdd:COG4717 414 LlgeleellealdEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
647-923 |
6.03e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.55 E-value: 6.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 647 QNMEQKRRQLEESQDSLSEELAKLRAQekmhevsFQDKEKEHLTRLQDAEEVKKALEQQMESHREAHQKQLSRLRDEIEE 726
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEE-------ISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 727 KQRIIDEIRDLNQKLQLEQERLSSDYNKLKIEDQEREVKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQ 806
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 807 DLTTRVKKSVELdsddgggsaaqKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAK 886
Cdd:TIGR02169 386 ELKDYREKLEKL-----------KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE 454
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 45433560 887 ENAMR---DRKRYQQEVDRIKEAVRAKNMARRAHSAQIAK 923
Cdd:TIGR02169 455 WKLEQlaaDLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
590-903 |
6.05e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.54 E-value: 6.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 590 ISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAK 669
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 670 LRAQEKmhevSFQDKEKEHLTRLQDAEEVKKALEQQMEshreAHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLS 749
Cdd:TIGR02168 759 LEAEIE----ELEERLEEAEEELAEAEAEIEELEAQIE----QLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 750 SDYNKLKIEDQEREVKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDSDDGGGSaaq 829
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE--- 907
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45433560 830 kQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRA----TAERVKALESALKEAKENAMRDRKRYQQEVDRI 903
Cdd:TIGR02168 908 -SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeyslTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
398-802 |
7.09e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.16 E-value: 7.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 398 IIDNITPVVDgISAEKEKYDEEItslyrqlddkdDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQiene 477
Cdd:TIGR02169 158 IIDEIAGVAE-FDRKKEKALEEL-----------EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKR---- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 478 aaKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQlqelsnhqkkrateiLNLLLKDL 557
Cdd:TIGR02169 222 --EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE---------------LNKKIKDL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 558 GEiggiigtndvktladvngviEEeftmarlyISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEA 637
Cdd:TIGR02169 285 GE--------------------EE--------QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 638 KIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQekmhevsFQDKEKEHLTRLQDAEEVKKALEqQMESHREAHQKQL 717
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE-------LEEVDKEFAETRDELKDYREKLE-KLKREINELKREL 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 718 SRLrdeIEEKQRIIDEIRDLNQKLqleqERLSSDYNKLkieDQEREVKLEKLLLLNDKREQAREDLKGLEETVSRELQTL 797
Cdd:TIGR02169 409 DRL---QEELQRLSEELADLNAAI----AGIEAKINEL---EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
....*
gi 45433560 798 HNLRK 802
Cdd:TIGR02169 479 DRVEK 483
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
592-916 |
9.91e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 9.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 592 KMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLL---ISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELA 668
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELlaeLARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 669 KLRAQEKMHEVSFQDKEKEHLTRLQDAEEVKKALEQQMESHREAHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERL 748
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 749 ssdyNKLKIEDQEREVKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDSDDgggsaA 828
Cdd:COG1196 414 ----ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL-----E 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 829 QKQKISFLENNLEQLTKVHKQLVRD--NADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEA 906
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEGFLEGvkAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIE 564
|
330
....*....|
gi 45433560 907 VRAKNMARRA 916
Cdd:COG1196 565 YLKAAKAGRA 574
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
411-801 |
1.06e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 411 AEKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQ--QMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQ 488
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 489 ALEELAVNYDQ------------------KSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQE--------LSNHQ 542
Cdd:COG4717 161 LEEELEELEAElaelqeeleelleqlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEeleqleneLEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 543 KKRATEILNLLLKDLGEIGGIIGTNDV--KTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNA 620
Cdd:COG4717 241 LEERLKEARLLLLIAAALLALLGLGGSllSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 621 SERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEK-----EHLTRLQDA 695
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEElraalEQAEEYQEL 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 696 EEVKKALEQQMESH-----REAHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLSSDYNKLKIEDQEREVKLEKLL 770
Cdd:COG4717 401 KEELEELEEQLEELlgeleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEE 480
|
410 420 430
....*....|....*....|....*....|...
gi 45433560 771 LLNDKREQARED--LKGLEETVSRELQTLHNLR 801
Cdd:COG4717 481 LKAELRELAEEWaaLKLALELLEEAREEYREER 513
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
594-806 |
7.43e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 59.75 E-value: 7.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 594 KSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQ 673
Cdd:pfam17380 367 QEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 674 EkMHEVSFQDKEKEH---LTRLQDAEEVKKALEQQMESHREAHQKQLSR--LRDEIEE-KQRIIDEIRD---LNQKLQLE 744
Cdd:pfam17380 447 E-MERVRLEEQERQQqveRLRQQEEERKRKKLELEKEKRDRKRAEEQRRkiLEKELEErKQAMIEEERKrklLEKEMEER 525
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45433560 745 QERLSSDYNKLKIEDQEREVKLEkllllnDKREQAREDLKGLEETVSReLQTLHNLRKLFVQ 806
Cdd:pfam17380 526 QKAIYEEERRREAEEERRKQQEM------EERRRIQEQMRKATEERSR-LEAMEREREMMRQ 580
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
410-756 |
8.75e-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: 59.70 E-value: 8.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 410 SAEKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDqdellasTRRDYEKIQEELTRLQIENEAAKDEvkevlqa 489
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSD-------ASRKIGEIEKEIEQLEQEEEKLKER------- 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 490 LEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQL-QELSNHQKKRATEILNLLLKDLGEIGGIIGTND 568
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeARLSHSRIPEIQAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 569 VKTladvnGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQN 648
Cdd:TIGR02169 819 QKL-----NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 649 MEQKRRQLEESQDSLSEELAKLRA-----QEKMHEVSFQDKEKEHLTR-----------LQDAEEVKKALEQQMESHREA 712
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKKRKrlselKAKLEALEEELSEIEDPKGedeeipeeelsLEDVQAELQRVEEEIRALEPV 973
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 45433560 713 HQKQLsrlrDEIEEKQRIIDEIRDLNQKLQLEQERL---SSDYNKLK 756
Cdd:TIGR02169 974 NMLAI----QEYEEVLKRLDELKEKRAKLEEERKAIlerIEEYEKKK 1016
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
418-756 |
1.03e-08 |
|
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: 59.26 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 418 EEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNY 497
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 498 DQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEI------LNLLLKDLGEIGGIIGTNdVKT 571
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLtnqdsvKELIIKNLDNTRESLETQ-LKV 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 572 LADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQ 651
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 652 --KRRQLEESQDSLSEELAKLraqekmhevsfqdkeKEHLTRLQDAEEVKKALEQQMESHREAHQKQLSRLRDEIEEKQR 729
Cdd:TIGR04523 553 elKKENLEKEIDEKNKEIEEL---------------KQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
|
330 340
....*....|....*....|....*..
gi 45433560 730 IIDEIRDLNQKLQLEQERLSSDYNKLK 756
Cdd:TIGR04523 618 ELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
425-921 |
3.09e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 425 RQLDDKDDEINQ-QSQLAEKLKQqmlDQDELLASTRRDYEKIQEELTRLQIENEAA---KDEVKEVLQAleelavnYDQK 500
Cdd:PRK02224 180 RVLSDQRGSLDQlKAQIEEKEEK---DLHERLNGLESELAELDEEIERYEEQREQAretRDEADEVLEE-------HEER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 501 SQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTNDvkTLADVNGVIE 580
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE--ELEDRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 581 EEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQK-------R 653
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 654 RQLEESQDSLSEELAKLRAQEKMHEVSFQD------------------------KEKEHLTRLQDAEEVKKALEQQMESH 709
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRTarerveeaealleagkcpecgqpvEGSPHVETIEEDRERVEELEAELEDL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 710 REAHQKQLSRLrDEIEEKQRIIDEIRDLNQKLQLEQERLSSDYNKLKiEDQEREVKLEKLLLLND-KREQAREDLKGLEE 788
Cdd:PRK02224 488 EEEVEEVEERL-ERAEDLVEAEDRIERLEERREDLEELIAERRETIE-EKRERAEELRERAAELEaEAEEKREAAAEAEE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 789 TVSRELQTLHNL--RKLFVQDLTTRVKKSVELDSDdgggsaaqkqkISFLENNLEQLTKVHKQLVRDNaDLRCElpklek 866
Cdd:PRK02224 566 EAEEAREEVAELnsKLAELKERIESLERIRTLLAA-----------IADAEDEIERLREKREALAELN-DERRE------ 627
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 45433560 867 RLRATAERVKALESALKEAK-ENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQI 921
Cdd:PRK02224 628 RLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEI 683
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
439-739 |
5.63e-08 |
|
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: 57.27 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 439 QLAEKLKQQMLDQDEL---LASTRRDYEKIQEELTRLQIENEAAKDEVKE-------VLQALEEL---AVNYDQKSQEVE 505
Cdd:COG3096 344 RQQEKIERYQEDLEELterLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSlksqladYQQALDVQqtrAIQYQQAVQALE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 506 DKTR-------ANEQLTDELAQ---KTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEI----GGIIGTNDVKT 571
Cdd:COG3096 424 KARAlcglpdlTPENAEDYLAAfraKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVersqAWQTARELLRR 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 572 LADVNGVIEEEFTMARLYiskmkSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQ 651
Cdd:COG3096 504 YRSQQALAQRLQQLRAQL-----AELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVE 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 652 KRRQLEESQDSLSEELAKLRAQE----KMHEVSFQDKEKEHLTrLQDAEEVKKALEQQMESHREAhqkqlSRLRDEIEE- 726
Cdd:COG3096 579 QRSELRQQLEQLRARIKELAARApawlAAQDALERLREQSGEA-LADSQEVTAAMQQLLEREREA-----TVERDELAAr 652
|
330
....*....|...
gi 45433560 727 KQRIIDEIRDLNQ 739
Cdd:COG3096 653 KQALESQIERLSQ 665
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
361-903 |
7.39e-08 |
|
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: 56.52 E-value: 7.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 361 QHLEMELNRWRNGEAVPEDEQISAKDQKSLEPCDNTPIIDnitpvvdgISAEKEKYDEEITSLYRQLDDKDDEinQQSQL 440
Cdd:TIGR00618 344 RRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHT--------LQQQKTTLTQKLQSLCKELDILQRE--QATID 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 441 AEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVlqALEELAVNYDQKSQEVEDKTRANEQLTDELAQ 520
Cdd:TIGR00618 414 TRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKI--HLQESAQSLKEREQQLQTKEQIHLQETRKKAV 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 521 KTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTNDVKT-LADVNGVIEEEFTMARLYISKMKSEVKS 599
Cdd:TIGR00618 492 VLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETsEEDVYHQLTSERKQRASLKEQMQEIQQS 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 600 LVNRSKQLESAQMDSNR------------KMNASERELAAC----QLLISQHEAKIKSLTDYMQNMEQK---------RR 654
Cdd:TIGR00618 572 FSILTQCDNRSKEDIPNlqnitvrlqdltEKLSEAEDMLACeqhaLLRKLQPEQDLQDVRLHLQQCSQElalkltalhAL 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 655 QLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEVKKALEQQMESHREAHQKQLSRLRDEIEEKQRIIDEI 734
Cdd:TIGR00618 652 QLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLG 731
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 735 RDLNQKLQLEQERLssdyNKLKIEDQEREVKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDL-TTRVK 813
Cdd:TIGR00618 732 SDLAAREDALNQSL----KELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLkTLEAE 807
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 814 KSVELDSDDGGGSAAQKQKISFLENNLEQLTKVHKQLVrdnaDLRCELPKLEKRLRATAERVKALESALKEAKENAMRDR 893
Cdd:TIGR00618 808 IGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLG----EITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQ 883
|
570
....*....|
gi 45433560 894 KRYQQEVDRI 903
Cdd:TIGR00618 884 IKIQFDGDAL 893
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
402-761 |
1.33e-07 |
|
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: 55.89 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 402 ITPVVDGISAEKEKYDEEITSLYRQLDDKDDeinqqsQLAEKLKQQMLDQDELLASTRRDYEKIQeelTRLQIENEAAKD 481
Cdd:pfam15921 240 IFPVEDQLEALKSESQNKIELLLQQHQDRIE------QLISEHEVEITGLTEKASSARSQANSIQ---SQLEIIQEQARN 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 482 E--------------VKEVLQALEELAVNYDQKSQEVEDK-TRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRA 546
Cdd:pfam15921 311 QnsmymrqlsdlestVSQLRSELREAKRMYEDKIEELEKQlVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKRE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 547 TEI-----LNLLLKDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYIS----KMKSEVKSLVNRSKQLE-----SAQM 612
Cdd:pfam15921 391 KELslekeQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSecqgQMERQMAAIQGKNESLEkvsslTAQL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 613 DSNRKM-NASERELAACQLLISQHEAKIKSLTDYMQnmeQKRRQLEESqdslSEELAKLRAQE--KMHEVSFQDKEKEHL 689
Cdd:pfam15921 471 ESTKEMlRKVVEELTAKKMTLESSERTVSDLTASLQ---EKERAIEAT----NAEITKLRSRVdlKLQELQHLKNEGDHL 543
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45433560 690 TRLQDAEEvkkALEQQMESHreahQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLSSDYNKLKIEDQE 761
Cdd:pfam15921 544 RNVQTECE---ALKLQMAEK----DKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQE 608
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
399-923 |
1.40e-07 |
|
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: 55.83 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 399 IDNITPVVDGISAEKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEA 478
Cdd:TIGR02168 283 IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 479 AKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQL-QELSNHQKKRATEILNLLLKDL 557
Cdd:TIGR02168 363 LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqQEIEELLKKLEEAELKELQAEL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 558 GEIGGIIgTNDVKTLADVNG---VIEEEFTMARLYISKMKSEVKSLVNRSKQLESaQMDSNRKMNASERELAACQLLISQ 634
Cdd:TIGR02168 443 EELEEEL-EELQEELERLEEaleELREELEEAEQALDAAERELAQLQARLDSLER-LQENLEGFSEGVKALLKNQSGLSG 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 635 HEAKIKSL----TDYMQNME---QKRRQ--LEESQDSLSEELAKLrAQEKMHEVSF--------QDKEKEHLTRLQDAEE 697
Cdd:TIGR02168 521 ILGVLSELisvdEGYEAAIEaalGGRLQavVVENLNAAKKAIAFL-KQNELGRVTFlpldsikgTEIQGNDREILKNIEG 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 698 VK---KALEQQMESHREAHQKQLSRLR--DEIEEKQRIIDEIRDLNQKLQLEQERLSSDYnklkIEDQEREVKLEKLLLL 772
Cdd:TIGR02168 600 FLgvaKDLVKFDPKLRKALSYLLGGVLvvDDLDNALELAKKLRPGYRIVTLDGDLVRPGG----VITGGSAKTNSSILER 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 773 NDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDSddgggsaaQKQKISFLENNLEQLTKVHKQLVR 852
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE--------LSRQISALRKDLARLEAEVEQLEE 747
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45433560 853 DNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQ---EVDRIKEAVRAKNMARRAHSAQIAK 923
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTLLNEEAAN 821
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
621-905 |
1.50e-07 |
|
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: 55.51 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 621 SERELAACQLLISQHEAKI--KSLTDYMQNMEQ---------------KRRQLEESQDSLSEELAKLRAQEKMHEVSFQD 683
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVseRQQQEKFEKMEQerlrqekeekareveRRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 684 KEKEhLTRLQdAEEVKKALEQ--------QMESHREAHQKQLSR------LRDEIE----------EKQRIIDEIRDLNQ 739
Cdd:pfam17380 346 RERE-LERIR-QEERKRELERirqeeiamEISRMRELERLQMERqqknerVRQELEaarkvkileeERQRKIQQQKVEME 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 740 KLQLEQErlSSDYNKLKIEDQEREVKLEKLLLLNDKREQAREDLKgleetvsrelqtlhnlrklfvQDLTTRVKKSVELD 819
Cdd:pfam17380 424 QIRAEQE--EARQREVRRLEEERAREMERVRLEEQERQQQVERLR---------------------QQEEERKRKKLELE 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 820 SDDGGGSAAQKQKISFLENNLEQltkvHKQLVRDNADLRCELPK-LEKRLRATAERVKALESALKEAKENAMRDRKRYQQ 898
Cdd:pfam17380 481 KEKRDRKRAEEQRRKILEKELEE----RKQAMIEEERKRKLLEKeMEERQKAIYEEERRREAEEERRKQQEMEERRRIQE 556
|
....*..
gi 45433560 899 EVDRIKE 905
Cdd:pfam17380 557 QMRKATE 563
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
430-914 |
2.54e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 430 KDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKiQEELTRLQIEN---EAAKDEVKEVLQAlEELAVNYDQKSQEVED 506
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK-ADELKKAAAAKkkaDEAKKKAEEKKKA-DEAKKKAEEAKKADEA 1449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 507 KTRANEQLTDELAQKTTTLTTTQRELSQLQElsnhQKKRATEilnllLKDLGEiggiigtnDVKTLADVNGVIEEEFTMA 586
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKADEAKKKAE----EAKKADE-----AKKKAE--------EAKKKADEAKKAAEAKKKA 1512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 587 ---RLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKR----RQLEES 659
Cdd:PTZ00121 1513 deaKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaeeaKKAEEA 1592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 660 QDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEVKKALEqQMESHREAHQKQLSRLRDEIEEkqriiDEIRDLNQ 739
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE-QLKKKEAEEKKKAEELKKAEEE-----NKIKAAEE 1666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 740 KLQLEQERLSSDynKLKIEDQEREVKLEKLLLLNDKREQAREDLKGLEETVSR--ELQTLHNLRKLFVQDLTTRV----K 813
Cdd:PTZ00121 1667 AKKAEEDKKKAE--EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKaeELKKAEEENKIKAEEAKKEAeedkK 1744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 814 KSVELDSDDGGGSAAQKQKISfLENNLEQLTKVHKQLVRDNADLRCELPKLEKRlRATAERVKALESALKEAKENAMRDR 893
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKIAHLKKE-EEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD-KKIKDIFDNFANIIEGGKEGNLVIN 1822
|
490 500
....*....|....*....|.
gi 45433560 894 KRYQQEVDRIKEAVRAKNMAR 914
Cdd:PTZ00121 1823 DSKEMEDSAIKEVADSKNMQL 1843
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
451-675 |
2.87e-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: 54.00 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 451 QDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELavnydqkSQEVEDKTRANEQLTDELAQKTTTLTTTQR 530
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-------ERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 531 ELSQLQELSNHQKKRATEILNLLLK--DLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLE 608
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45433560 609 SAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEK 675
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
411-893 |
3.33e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 411 AEKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDellastRRDYEKIQEELTRLQIENEAAKDEVKEVLQAL 490
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG------GDRLEQLEREIERLERELEERERRRARLEALL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 491 -----------EELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRAT-------EILNL 552
Cdd:COG4913 369 aalglplpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSniparllALRDA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 553 LLKDLGE------------------------IGGIIGTN------DVKTLADVNGVIEEEFTMARLYISKMKSEVK---- 598
Cdd:COG4913 449 LAEALGLdeaelpfvgelievrpeeerwrgaIERVLGGFaltllvPPEHYAAALRWVNRLHLRGRLVYERVRTGLPdper 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 599 ------SLVNR-----SKQLESAQMDSNRKMN----ASEREL--------AACQL--------------LISQH------ 635
Cdd:COG4913 529 prldpdSLAGKldfkpHPFRAWLEAELGRRFDyvcvDSPEELrrhpraitRAGQVkgngtrhekddrrrIRSRYvlgfdn 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 636 EAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQ----EKMHEVSFQDKE-KEHLTRLQDAEEVKKALE------Q 704
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERrealQRLAEYSWDEIDvASAEREIAELEAELERLDassddlA 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 705 QMESHREAHQKQLSRLRDEIEEKQRII----DEIRDLNQKLQLEQERLSSDYNKLKIED----QEREVKLEKLLLLNDKR 776
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIgrleKELEQAEEELDELQDRLEAAEDLARLELrallEERFAAALGDAVERELR 768
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 777 EQAREDLKGLEETVSRELQTLHNLRKLFVQDLTtrvkksveLDSDDGGGSAAqkqkisflenNLEQLTKVHKQLVRDNad 856
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAMRAFNREWP--------AETADLDADLE----------SLPEYLALLDRLEEDG-- 828
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 45433560 857 lrceLPKLEKRLR-----ATAERVKALESALKEAKENAmRDR 893
Cdd:COG4913 829 ----LPEYEERFKellneNSIEFVADLLSKLRRAIREI-KER 865
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
597-793 |
5.25e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 597 VKSLVNRSKQLESAQmDSNRKMNASERELAACQL-LISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEK 675
Cdd:COG4717 48 LERLEKEADELFKPQ-GRKPELNLKELKELEEELkEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 676 MHEVSFQDKEKEHltRLQDAEEVKKALEQQMESHREAhQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQ-ERLSSDYNK 754
Cdd:COG4717 127 LLPLYQELEALEA--ELAELPERLEELEERLEELREL-EEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEE 203
|
170 180 190
....*....|....*....|....*....|....*....
gi 45433560 755 LKiedQEREVKLEKLLLLNDKREQAREDLKGLEETVSRE 793
Cdd:COG4717 204 LQ---QRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
412-905 |
6.98e-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: 53.53 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 412 EKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMldqdellastrrdyEKIQEELTRLQIENEAAKDEVKEVLQALE 491
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEELADLNAAI--------------AGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 492 ELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHqKKRATEILNlllkdlGEIGGIIGTndVKT 571
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG-GRAVEEVLK------ASIQGVHGT--VAQ 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 572 LADV-----------------NGVIEEEFTMAR---------------LYISKMKSEVK---------------SLVNRS 604
Cdd:TIGR02169 530 LGSVgeryataievaagnrlnNVVVEDDAVAKEaiellkrrkagratfLPLNKMRDERRdlsilsedgvigfavDLVEFD 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 605 KQLESA------------QMDSNRK--------------------MNASERELAACQLLISQHEAKIKSLTDYMQNMEQK 652
Cdd:TIGR02169 610 PKYEPAfkyvfgdtlvveDIEAARRlmgkyrmvtlegelfeksgaMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRE 689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 653 RRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEVKKALEQQMEshreahqkQLSRLRDEIEEKqriID 732
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE--------DLSSLEQEIENV---KS 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 733 EIRDLNQKLQLEQERLSSDynKLKIEDQEREVKLEKLLLLNDKREQAREDLKGLEETVS---RELQTLHNLRKLFVQDLT 809
Cdd:TIGR02169 759 ELKELEARIEELEEDLHKL--EEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLReieQKLNRLTLEKEYLEKEIQ 836
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 810 TRVKKSVELDS----------DDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKR---LRATAERVK 876
Cdd:TIGR02169 837 ELQEQRIDLKEqiksiekeieNLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKieeLEAQIEKKR 916
|
570 580
....*....|....*....|....*....
gi 45433560 877 ALESALKEAKENAMRDRKRYQQEVDRIKE 905
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
412-868 |
1.00e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.72 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 412 EKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTrlQIENEAAKDEVKevLQALE 491
Cdd:TIGR04523 132 QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID--KIKNKLLKLELL--LSNLK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 492 ELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTNDVKT 571
Cdd:TIGR04523 208 KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 572 LAdvngvieeeftmarlyISKMKSEVKSLVNRSKQLESAQMDSNRKMNasERELAACQLLISQHEAKIKSLTDYMQNMEQ 651
Cdd:TIGR04523 288 KQ----------------LNQLKSEISDLNNQKEQDWNKELKSELKNQ--EKKLEEIQNQISQNNKIISQLNEQISQLKK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 652 KRRQLEESQDSLSEELaklraQEKMHEVSFQDKEKE-HLTRLQDAEEVKKALEQQMESHREAHQK---QLSRLRDEIEEK 727
Cdd:TIGR04523 350 ELTNSESENSEKQREL-----EEKQNEIEKLKKENQsYKQEIKNLESQINDLESKIQNQEKLNQQkdeQIKKLQQEKELL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 728 QRIIDEIRDLNQKLQLEQERLSSDYNKLKIEDQErevkleklllLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQD 807
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN----------LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK 494
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45433560 808 lTTRVKKSVELDSDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRL 868
Cdd:TIGR04523 495 -EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL 554
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
451-748 |
1.19e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.65 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 451 QDELLASTRRDYEK------IQEELTRLQIENEAAKDEVKE-------VLQALEEL---AVNYDQKSQEVEdktRAN--- 511
Cdd:PRK04863 354 QADLEELEERLEEQnevveeADEQQEENEARAEAAEEEVDElksqladYQQALDVQqtrAIQYQQAVQALE---RAKqlc 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 512 -------EQLTDELAQKTTTLTTTQRELSQL-QELSNHQ--KKRATEILNLLLKdlgeIGGIIGTNDVKTLA-DVNGVIE 580
Cdd:PRK04863 431 glpdltaDNAEDWLEEFQAKEQEATEELLSLeQKLSVAQaaHSQFEQAYQLVRK----IAGEVSRSEAWDVArELLRRLR 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 581 EEFTMA-RLYISKMK-SEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEE 658
Cdd:PRK04863 507 EQRHLAeQLQQLRMRlSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQ 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 659 SQDSLSEELAKLRAQE-KMHEvsFQDKekehLTRLQ----DAEEVKKALEQQMESHREaHQKQLSRLRDEIEE-KQRIID 732
Cdd:PRK04863 587 QLEQLQARIQRLAARApAWLA--AQDA----LARLReqsgEEFEDSQDVTEYMQQLLE-RERELTVERDELAArKQALDE 659
|
330
....*....|....*.
gi 45433560 733 EIRDLNQKLQLEQERL 748
Cdd:PRK04863 660 EIERLSQPGGSEDPRL 675
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
414-893 |
1.56e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 414 EKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEel 493
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ-- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 494 avnydqksqeVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEIlnlllkdlgeiggiigtndvktlA 573
Cdd:COG4717 127 ----------LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL-----------------------A 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 574 DVNGVIEEEFTMARLyisKMKSEVKSLVNRSKQLEsaqmdsnRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKR 653
Cdd:COG4717 174 ELQEELEELLEQLSL---ATEEELQDLAEELEELQ-------QRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 654 RQLEESQ-------------------DSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEVKkALEQQMESHREAHQ 714
Cdd:COG4717 244 RLKEARLllliaaallallglggsllSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ-ALPALEELEEEELE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 715 KQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLSSDYNKLKIEDQEREVKLEKLLLLNDKREQAREDLKgleetVSREL 794
Cdd:COG4717 323 ELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALE-----QAEEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 795 QTLHNLRKLFVQDLTTRVKKSVELDsdDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEK--RLRATA 872
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELL--EALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELL 475
|
490 500
....*....|....*....|.
gi 45433560 873 ERVKALESALKEAKENAMRDR 893
Cdd:COG4717 476 QELEELKAELRELAEEWAALK 496
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
406-887 |
1.90e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 406 VDGISAEKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQqmlDQDELLAST---RRDYEKIQEELTRLQIENEAAKDE 482
Cdd:PRK02224 253 LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEE---ERDDLLAEAgldDADAEAVEARREELEDRDEELRDR 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 483 VKEVLQAL-------EELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKR---------- 545
Cdd:PRK02224 330 LEECRVAAqahneeaESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdlgn 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 546 ATEILNLLLKDLGEIGGIIGTNDVkTLADVNGVIEEEftmARLY--------------------ISKMKSEVKSLVNRSK 605
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEA-TLRTARERVEEA---EALLeagkcpecgqpvegsphvetIEEDRERVEELEAELE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 606 QLESAQMDSNRKMNASERELAAcqllisqhEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKE 685
Cdd:PRK02224 486 DLEEEVEEVEERLERAEDLVEA--------EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKR 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 686 KEHLTRLQDAEEVK---KALEQQMESHREAHQkQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERlssdynklkiEDQER 762
Cdd:PRK02224 558 EAAAEAEEEAEEAReevAELNSKLAELKERIE-SLERIRTLLAAIADAEDEIERLREKREALAEL----------NDERR 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 763 EVKLekllllnDKREQAREdlkgLEETVSRE-LQTLHNLRKLFVQDLTTRVKKSVELDSDdgggSAAQKQKISFLENNLE 841
Cdd:PRK02224 627 ERLA-------EKRERKRE----LEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREE----RDDLQAEIGAVENELE 691
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 45433560 842 qltkvhkqlvrdnadlrcELPKLEKRLRATAERVKALESALKEAKE 887
Cdd:PRK02224 692 ------------------ELEELRERREALENRVEALEALYDEAEE 719
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
412-910 |
1.92e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 412 EKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALE 491
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 492 --ELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQElsnhQKKRATEilnllLKDLGEiggiigtnDV 569
Cdd:PTZ00121 1368 aaEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA----AKKKADE-----AKKKAE--------EK 1430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 570 KTLADVNGVIEEEFTMARLyiSKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAAcQLLISQHEAKIKSltDYMQNM 649
Cdd:PTZ00121 1431 KKADEAKKKAEEAKKADEA--KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD-EAKKKAEEAKKKA--DEAKKA 1505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 650 EQKRRQLEESQDS----LSEELAKLRAQEKMHEV--SFQDKEKEHLTR---LQDAEEVKKALEQQMESHREAHQKQLSRL 720
Cdd:PTZ00121 1506 AEAKKKADEAKKAeeakKADEAKKAEEAKKADEAkkAEEKKKADELKKaeeLKKAEEKKKAEEAKKAEEDKNMALRKAEE 1585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 721 RDEIEEKQriideirdlnqklQLEQERLSSDYNKLKIEDQEREVKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNL 800
Cdd:PTZ00121 1586 AKKAEEAR-------------IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL 1652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 801 RKlfvQDLTTRVKKSVELDSDDgggsaAQKQKISFLENNLEQLTKVHKQLVRDNADLRcelpKLEKRLRATAERVKALES 880
Cdd:PTZ00121 1653 KK---AEEENKIKAAEEAKKAE-----EDKKKAEEAKKAEEDEKKAAEALKKEAEEAK----KAEELKKKEAEEKKKAEE 1720
|
490 500 510
....*....|....*....|....*....|
gi 45433560 881 ALKEAKENAMRDRKRYQQEVDRIKEAVRAK 910
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
412-862 |
1.93e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 412 EKEKYDEeitsLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALE 491
Cdd:PTZ00121 1442 EAKKADE----AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK 1517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 492 ELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQrELSQLQELSN-HQKKRATEILNLLLKDLGEIGGIigtnDVK 570
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKaEEAKKAEEDKNMALRKAEEAKKA----EEA 1592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 571 TLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNME 650
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE 1672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 651 QKRRQLE----ESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTR---LQDAEEVKKALEQQMESHREAHQKQLSRLRDE 723
Cdd:PTZ00121 1673 DKKKAEEakkaEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 724 IEEKQRIIDEIRDLNQKL-QLEQERLSSDYNKLKIEDQEREVKLEKLLLL-----------NDKREQAREDLKGLEETVS 791
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAeEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDifdnfaniiegGKEGNLVINDSKEMEDSAI 1832
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45433560 792 RELQTLHNLRKLFVQDLTTRVKKSVELDSDDGGGSAAQKQKISFLENNLEQL--TKVHKQLvrDNADLRCELP 862
Cdd:PTZ00121 1833 KEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIeeADEIEKI--DKDDIEREIP 1903
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
686-922 |
2.21e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 686 KEHLTRLQDA-EEVKKALEQQMeshreaHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLSSDYNKLKIEDQEREV 764
Cdd:COG4913 231 VEHFDDLERAhEALEDAREQIE------LLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 765 klekllllnDKREQAREDLKGLEETVSRELQTLHNlrklfvqdlttrvkksvELDSDDGggsaaqkQKISFLENNLEQLT 844
Cdd:COG4913 305 ---------ARLEAELERLEARLDALREELDELEA-----------------QIRGNGG-------DRLEQLEREIERLE 351
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45433560 845 KVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIA 922
Cdd:COG4913 352 RELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
515-747 |
2.47e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 515 TDELAQKTTTLTTTQRELSQLQELSNHQKKRATEilnlLLKDLGEIggiigTNDVKTLADVNGVIEEEFTMARLYISKMK 594
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAAL-----ERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 595 SEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQe 674
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE- 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45433560 675 kmhevsFQDKEKEHLTRLQDAEEVKKALEQQMESHREA---HQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQER 747
Cdd:COG4942 169 ------LEAERAELEALLAELEEERAALEALKAERQKLlarLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
590-756 |
3.30e-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: 50.53 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 590 ISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTdymQNMEQKRRQLEESQDSLSEELAK 669
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE---KEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 670 L----------------------RAQEKMHEVSFQDKE-----KEHLTRLQDAEEVKKALEQQMESHREAHQKQLSRLRD 722
Cdd:COG4942 113 LyrlgrqpplalllspedfldavRRLQYLKYLAPARREqaeelRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190
....*....|....*....|....*....|....
gi 45433560 723 EIEEKQRIIDEIRDLNQKLQLEQERLSSDYNKLK 756
Cdd:COG4942 193 LKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
590-887 |
3.49e-06 |
|
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: 50.99 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 590 ISKMKSEVKSLVNRSKQLESAQMdsnrKMNASERELAACQLLIS-QHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELA 668
Cdd:pfam12128 236 IMKIRPEFTKLQQEFNTLESAEL----RLSHLHFGYKSDETLIAsRQEERQETSAELNQLLRTLDDQWKEKRDELNGELS 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 669 KLRAQEKmhevsfqdKEKEHLTRLqdaEEVKKALEQQMESHREAHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERL 748
Cdd:pfam12128 312 AADAAVA--------KDRSELEAL---EDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 749 SS---DYNKLKIEDQEREVKLEKLLLLNdKREQAREDLKGLEETVSREL-QTLHNLR------KLFVQDLTTRVkKSVEL 818
Cdd:pfam12128 381 RSkikEQNNRDIAGIKDKLAKIREARDR-QLAVAEDDLQALESELREQLeAGKLEFNeeeyrlKSRLGELKLRL-NQATA 458
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45433560 819 DSDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKE 887
Cdd:pfam12128 459 TPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELEL 527
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
6-269 |
3.64e-06 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 50.89 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 6 ECSIKVMCRFRPLNEA--EILRGDKFIPKFKGEETVVI---GQGKP-----YVFDRVLPPNTTQEQVYNaCAKQIVKDVL 75
Cdd:COG5059 304 NCNTRVICTISPSSNSfeETINTLKFASRAKSIKNKIQvnsSSDSSreieeIKFDLSEDRSEIEILVFR-EQSQLSQSSL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 76 EGyngtIFAYGQTSSGKTHTMEGKLHDPQ---LMGIIPRIAHDIFDHIYSMDENLEFHIKVSYfeiyldKIRDLLDVSKT 152
Cdd:COG5059 383 SG----IFAYMQSLKKETETLKSRIDLIMksiISGTFERKKLLKEEGWKYKSTLQFLRIEIDR------LLLLREEELSK 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 153 NLAVHEDKNRVpyvKGCTERFVS-SPEEVMDVIDEGKA--NRHVAVTNMNEHSSRSHSIFlINIKQENVETEKKLSgkLY 229
Cdd:COG5059 453 KKTKIHKLNKL---RHDLSSLLSsIPEETSDRVESEKAskLRSSASTKLNLRSSRSHSKF-RDHLNGSNSSTKELS--LN 526
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 45433560 230 LVDLAGSEKVSKTgAEGAVLDEAKNINKSLSALGNVISAL 269
Cdd:COG5059 527 QVDLAGSERKVSQ-SVGELLRETQSLNKSLSSLGDVIHAL 565
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
695-937 |
5.57e-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: 49.76 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 695 AEEVKKALEQQMESHREAHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLSsdynklKIEdQEREVKLEKLLLLND 774
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR------ALE-QELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 775 KREQAREDLKGLEETVSRelqtlhNLRKLFVQDLTTRVKksVELDSDDGGGSAAQ----KQKISFLENNLEQLTKVHKQL 850
Cdd:COG4942 91 EIAELRAELEAQKEELAE------LLRALYRLGRQPPLA--LLLSPEDFLDAVRRlqylKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 851 VRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIAKPIRPGHY 930
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
....*..
gi 45433560 931 PASSPTA 937
Cdd:COG4942 243 TPAAGFA 249
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
622-742 |
5.99e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 50.03 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 622 ERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEES---QDSLSEELAK-LRAQEKMHEVSFQDKEK-EHLTRL-QDA 695
Cdd:pfam05667 334 EEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEEleeLKEQNEELEKqYKVKKKTLDLLPDAEENiAKLQALvDAS 413
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 45433560 696 EEVKKALEQQMESHREAHQKQLSRLRDEIEEK----QRIIDEIRDLNQKLQ 742
Cdd:pfam05667 414 AQRLVELAGQWEKHRVPLIEEYRALKEAKSNKedesQRKLEEIKELREKIK 464
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
413-799 |
6.78e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.83 E-value: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 413 KEKYDEEITslyRQLDDKDDEINQQSQLAEKL-----KQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVL 487
Cdd:PRK04778 70 RQKWDEIVT---NSLPDIEEQLFEAEELNDKFrfrkaKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 488 QALEELAVNYDQKSQEVEDktrANEQLTDELAQktttlttTQRELSQLQELS---NHQKkrATEILNLLLKDLGEIGGII 564
Cdd:PRK04778 147 DLYRELRKSLLANRFSFGP---ALDELEKQLEN-------LEEEFSQFVELTesgDYVE--AREILDQLEEELAALEQIM 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 565 gtNDVKTL-ADVNGVIEEEFTMARLYISKMKSE-----VKSLVNRSKQLEsAQMDSNRKMnASERELAACQLLISQHEAK 638
Cdd:PRK04778 215 --EEIPELlKELQTELPDQLQELKAGYRELVEEgyhldHLDIEKEIQDLK-EQIDENLAL-LEELDLDEAEEKNEEIQER 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 639 IKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEK--MHEVSF-----------QDKEKEHLTRLQDAEEVKKALEQQ 705
Cdd:PRK04778 291 IDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKelKEEIDRvkqsytlneseLESVRQLEKQLESLEKQYDEITER 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 706 MESHREAHqkqlSRLRDEIEEKQRIIDEIrdlnqklQLEQERLSSDYNKLKIEDQE--REVKLEKLLLLNDKREQAREDL 783
Cdd:PRK04778 371 IAEQEIAY----SELQEELEEILKQLEEI-------EKEQEKLSEMLQGLRKDELEarEKLERYRNKLHEIKRYLEKSNL 439
|
410 420
....*....|....*....|...
gi 45433560 784 KGLEE-------TVSRELQTLHN 799
Cdd:PRK04778 440 PGLPEdylemffEVSDEIEALAE 462
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
411-742 |
7.43e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 7.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 411 AEKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQ-QMLDQDEL-LASTRRDYEKIQEELTRLqienEAAKDEVKEVLQ 488
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRlAEYSWDEIdVASAEREIAELEAELERL----DASSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 489 ALEELAVNYDQKSQEVEDKTRANEQLTDELAQktttlttTQRELSQLQELSNHQKKRATEILNLLLKDLgeIGGIIGTND 568
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQ-------AEEELDELQDRLEAAEDLARLELRALLEER--FAAALGDAV 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 569 VKTLAdvngvieeeftmarlyiskmksevkslvnrsKQLESAQMDSNRKMNASERELAACqllisqheakiksltdymqn 648
Cdd:COG4913 764 ERELR-------------------------------ENLEERIDALRARLNRAEEELERA-------------------- 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 649 MEQKRRQLEESQDSLSEELAKLRAQEKMHEvsfqDKEKEHLTRLQdaEEVKKALEQQMESHREAHQkqlSRLRDEIEEkq 728
Cdd:COG4913 793 MRAFNREWPAETADLDADLESLPEYLALLD----RLEEDGLPEYE--ERFKELLNENSIEFVADLL---SKLRRAIRE-- 861
|
330
....*....|....
gi 45433560 729 rIIDEIRDLNQKLQ 742
Cdd:COG4913 862 -IKERIDPLNDSLK 874
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
406-534 |
1.15e-05 |
|
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: 47.61 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 406 VDGISAEKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDqdellASTRRDYEKIQEELTRLQIENEAAKDEVKE 485
Cdd:COG1579 40 LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-----VRNNKEYEALQKEIESLKRRISDLEDEILE 114
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 45433560 486 VLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQ 534
Cdd:COG1579 115 LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
420-758 |
1.64e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.96 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 420 ITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNYDQ 499
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLES 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 500 KSQEVED-------KTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKdlgeiggiigtndvktL 572
Cdd:pfam15921 494 SERTVSDltaslqeKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQ----------------M 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 573 ADVNGVIEeeftMARLYISKMKSEV--KSLVNRSKQLESAQMDsnRKMNASERELAACQLLISQHEAKIKSLTDYMQNME 650
Cdd:pfam15921 558 AEKDKVIE----ILRQQIENMTQLVgqHGRTAGAMQVEKAQLE--KEINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 651 ---------------------QKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEVKKALEQQMESH 709
Cdd:pfam15921 632 lekvklvnagserlravkdikQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQT 711
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45433560 710 R---------EAH--------QKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLSSDYNKLKIE 758
Cdd:pfam15921 712 RntlksmegsDGHamkvamgmQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQE 777
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
380-707 |
2.47e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 380 EQISAKdQKSLEPCDNTpiIDNITPVVDGISAEKEKYDEEITSLYRQLDDKDDEI----NQQSQL------AEKLKQQML 449
Cdd:pfam15921 482 EELTAK-KMTLESSERT--VSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELqhlkNEGDHLrnvqteCEALKLQMA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 450 DQDELLASTRRDYEKIQEELTR-------LQIENEAAKDEVKEVLQALEELAVNYDQKSQEVEDktrANEQLTDELAQKT 522
Cdd:pfam15921 559 EKDKVIEILRQQIENMTQLVGQhgrtagaMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRE---LEARVSDLELEKV 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 523 TTLTTTQRELSQLQELsnhqKKRATEILNLLLKDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARL--YISKMKSEVKSL 600
Cdd:pfam15921 636 KLVNAGSERLRAVKDI----KQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLkmQLKSAQSELEQT 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 601 VNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAK----------- 669
Cdd:pfam15921 712 RNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTvateknkmage 791
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 45433560 670 ---LRAQEK------------MHEVSFQDKEKEHLTRLQDAEEVKKALEQQME 707
Cdd:pfam15921 792 levLRSQERrlkekvanmevaLDKASLQFAECQDIIQRQEQESVRLKLQHTLD 844
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
600-918 |
2.61e-05 |
|
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: 48.50 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 600 LVNRSKQLESAQMDSNRKMNASErELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEelaklraqeKMHEV 679
Cdd:TIGR00606 226 ITSKEAQLESSREIVKSYENELD-PLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELEL---------KMEKV 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 680 SFQDKEKehltrLQDAEEVKKALEQQMESHREAHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLSSDYNKLKIED 759
Cdd:TIGR00606 296 FQGTDEQ-----LNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 760 QEREVKLEKLLLLNDK--REQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDSDDGGGSAAQKQKISFLE 837
Cdd:TIGR00606 371 QSLATRLELDGFERGPfsERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 838 NNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAH 917
Cdd:TIGR00606 451 KKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHH 530
|
.
gi 45433560 918 S 918
Cdd:TIGR00606 531 T 531
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
413-675 |
2.61e-05 |
|
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: 48.14 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 413 KEKYDEEITSLYRQLDDKDDEINQ-QSQLAEKlKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALE 491
Cdd:TIGR02169 282 KDLGEEEQLRVKEKIGELEAEIASlERSIAEK-ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 492 ELAVNYDQKSQEVEDKTRANEQLTDELAQktttlttTQRELSQLQElsnhqkkrateilnlllkdlgEIGGIIGTNDVKt 571
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDKEFAETRDELKD-------YREKLEKLKR---------------------EINELKRELDRL- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 572 ladvngviEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELaacqlliSQHEAKIKSLTDYMQNMEQ 651
Cdd:TIGR02169 412 --------QEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL-------EQLAADLSKYEQELYDLKE 476
|
250 260
....*....|....*....|....
gi 45433560 652 KRRQLEESQDSLSEELAKLRAQEK 675
Cdd:TIGR02169 477 EYDRVEKELSKLQRELAEAEAQAR 500
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
408-802 |
2.79e-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: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 408 GISAEKEKYDEEITSLYRQLDDKDDEIN-QQSQLAEKLKQQMLDQDELLAS--TRRDYEKIQEELTRLQIENEAAKDEVK 484
Cdd:pfam12128 409 QLAVAEDDLQALESELREQLEAGKLEFNeEEYRLKSRLGELKLRLNQATATpeLLLQLENFDERIERAREEQEAANAEVE 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 485 EVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQREL-----SQLQELSNHQKKRAT-----------E 548
Cdd:pfam12128 489 RLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLlhflrKEAPDWEQSIGKVISpellhrtdldpE 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 549 ILNLLLKDLGEIGGIigTNDVKTLaDVNGVIEEEFTMaRLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAAC 628
Cdd:pfam12128 569 VWDGSVGGELNLYGV--KLDLKRI-DVPEWAASEEEL-RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFA 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 629 QLLISQHEAKIKSLTDYMQNME-QKRRQLEESQDSLSEELAKLRAQEKMHEV-------SFQDKEKEHLTRLQDA----E 696
Cdd:pfam12128 645 RTALKNARLDLRRLFDEKQSEKdKKNKALAERKDSANERLNSLEAQLKQLDKkhqawleEQKEQKREARTEKQAYwqvvE 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 697 EVKKA----LEQQMESHREAHQKQLSRLRDEIE--------EKQRIID---EIRDLNQKL----QLEQERLSSDYNKLKI 757
Cdd:pfam12128 725 GALDAqlalLKAAIAARRSGAKAELKALETWYKrdlaslgvDPDVIAKlkrEIRTLERKIeriaVRRQEVLRYFDWYQET 804
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 45433560 758 EDQEREVKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRK 802
Cdd:pfam12128 805 WLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERK 849
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
407-757 |
4.31e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 47.44 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 407 DGISAEKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRdyEKIQEELTRLQIENEAAKDEVKEV 486
Cdd:pfam07111 259 ADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWR--EKVFALMVQLKAQDLEHRDSVKQL 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 487 LQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKR---ATEILNLLLKDLGEIGGI 563
Cdd:pfam07111 337 RGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQtasAEEQLKFVVNAMSSTQIW 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 564 IGTN--------------------DVKTLADVNGVIEEEFTMARLYI-SKMKSEVKSLVNRSKQLESAQMDSNRKMNASE 622
Cdd:pfam07111 417 LETTmtrveqavaripslsnrlsyAVRKVHTIKGLMARKVALAQLRQeSCPPPPPAPPVDADLSLELEQLREERNRLDAE 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 623 RELAAcqLLISQH--------EAKIKSLTDYMQNMEQKRRQLEES--------------QDSLSEELAKLR----AQEKM 676
Cdd:pfam07111 497 LQLSA--HLIQQEvgrareqgEAERQQLSEVAQQLEQELQRAQESlasvgqqlevarqgQQESTEEAASLRqeltQQQEI 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 677 HEVSFQDKEKEHLTRLQDA-------------EEVKKALEQQMESHREAHQK----QLSRLRDEI--EEKQRIIDEIRDL 737
Cdd:pfam07111 575 YGQALQEKVAEVETRLREQlsdtkrrlnearrEQAKAVVSLRQIQHRATQEKernqELRRLQDEArkEEGQRLARRVQEL 654
|
410 420
....*....|....*....|....*
gi 45433560 738 NQK-----LQLEQERLSSDYNKLKI 757
Cdd:pfam07111 655 ERDknlmlATLQQEGLLSRYKQQRL 679
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
478-735 |
4.52e-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: 46.68 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 478 AAKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRateiLNLLLKDL 557
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----LAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 558 GEIGgiigtndvKTLADVNGVIEEefTMARLYISKMKSEVKSLVnrskqlesaqmdSNRKMNASERELAACQLLISQHEA 637
Cdd:COG4942 93 AELR--------AELEAQKEELAE--LLRALYRLGRQPPLALLL------------SPEDFLDAVRRLQYLKYLAPARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 638 KIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKmhevsfqdkekehltRLQDAEEVKKALEQQMESHREAHQKQL 717
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERAELEALLAELEEERA---------------ALEALKAERQKLLARLEKELAELAAEL 215
|
250
....*....|....*...
gi 45433560 718 SRLRDEIEEKQRIIDEIR 735
Cdd:COG4942 216 AELQQEAEELEALIARLE 233
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
413-910 |
5.08e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 413 KEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMldqdellastRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEE 492
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYL----------RQSVIDLQTKLQEMQMERDAMADIRRRESQSQED 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 493 LAVNYDQKSQEVEDKTRANEQLTDElaqktttlttTQRELSQLQELSNHQKKRATEILNLLLkDLGEIGGiigtndvKTL 572
Cdd:pfam15921 143 LRNQLQNTVHELEAAKCLKEDMLED----------SNTQIEQLRKMMLSHEGVLQEIRSILV-DFEEASG-------KKI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 573 ADVNGVIEEEFTMARLYISKMKSEVKSLVNRSK--------QLESAQMDSNRKMNAS-ERELAACQLLISQHEAKIKSLT 643
Cdd:pfam15921 205 YEHDSMSTMHFRSLGSAISKILRELDTEISYLKgrifpvedQLEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLT 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 644 dymQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEVKKALEQQMEShreaHQKQLSRLRDE 723
Cdd:pfam15921 285 ---EKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEE----LEKQLVLANSE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 724 IEEKQRIIDEIRDLNQKLQLEQERLSSDYNKLKIEdqerevklEKLLLLNDKREQAREDLKGLE-ETVSRELQTlhnlRK 802
Cdd:pfam15921 358 LTEARTERDQFSQESGNLDDQLQKLLADLHKREKE--------LSLEKEQNKRLWDRDTGNSITiDHLRRELDD----RN 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 803 LFVQDLTTRVKKsveLDSDDGGgsaAQKQKISFLENNLEQLTKVhkqlvrdnADLRCELPKLEKRLRATAERVKALESAL 882
Cdd:pfam15921 426 MEVQRLEALLKA---MKSECQG---QMERQMAAIQGKNESLEKV--------SSLTAQLESTKEMLRKVVEELTAKKMTL 491
|
490 500
....*....|....*....|....*...
gi 45433560 883 kEAKENAMRDRKRYQQEVDRIKEAVRAK 910
Cdd:pfam15921 492 -ESSERTVSDLTASLQEKERAIEATNAE 518
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
411-915 |
6.08e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 411 AEKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLAST---RRDYEKIQEELTRLQIENEAAKDEVK--- 484
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdeaKKAEEKKKADEAKKKAEEAKKADEAKkka 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 485 -EVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEilnlllkdlgeiggi 563
Cdd:PTZ00121 1325 eEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE--------------- 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 564 igtndVKTLADVNGVIEEEftmarlyiSKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQlliSQHEAKIKSLT 643
Cdd:PTZ00121 1390 -----KKKADEAKKKAEED--------KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE---AKKADEAKKKA 1453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 644 DYMQNMEQKRRQLEESQDSlseELAKLRAQEKMHEVSFQDKEKEHLTRlqdAEEVKKALEQQMESHrEAHQKQLSRLRDE 723
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEAKKA---DEAKKKAEEAKKADEAKKKAEEAKKK---ADEAKKAAEAKKKAD-EAKKAEEAKKADE 1526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 724 IE--EKQRIIDEIRDLNQKLQLEQERLSSDYNKlkIEDQEREVKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLR 801
Cdd:PTZ00121 1527 AKkaEEAKKADEAKKAEEKKKADELKKAEELKK--AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 802 KlfvqdlttRVKKSVELDSDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCElpKLEKRLRATAERVKALESA 881
Cdd:PTZ00121 1605 K--------KMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA--EEENKIKAAEEAKKAEEDK 1674
|
490 500 510
....*....|....*....|....*....|....*.
gi 45433560 882 LK--EAKENAMRDRKRYQQEVDRIKEAVRAKNMARR 915
Cdd:PTZ00121 1675 KKaeEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
411-923 |
7.33e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 411 AEKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQAL 490
Cdd:PTZ00121 1145 ARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAK 1224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 491 EELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLK----DLGEIGGIIGT 566
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKkkadEAKKAEEKKKA 1304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 567 NDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNR---KMNASERELAACQLLISQHEAK---IK 640
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAaadEAEAAEEKAEAAEKKKEEAKKKadaAK 1384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 641 SLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQD-AEEVKKALEQQMESHReahQKQLSR 719
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKkAEEAKKADEAKKKAEE---AKKAEE 1461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 720 LRDEIEEKQRIIDEIRDLNQKLQLEQERLSSDYNKLKIEDQEREVKLEKLLLLNDKREQARedlKGLEETVSRELQTLHN 799
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK---KADEAKKAEEAKKADE 1538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 800 LRKLFVQDLTTRVKKSVELDSDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATA------E 873
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakkaeeA 1618
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 45433560 874 RVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIAK 923
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
454-891 |
1.05e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.20 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 454 LLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQAleelAVNYDQKSQEVEDKTRANEQ-------LTDELAQKTTTLT 526
Cdd:PRK10929 17 AYAATAPDEKQITQELEQAKAAKTPAQAEIVEALQS----ALNWLEERKGSLERAKQYQQvidnfpkLSAELRQQLNNER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 527 TTQREL-----------------SQLQELS---NHQKKRATEILNLLLKdlgeiggiigtndvktladvngvIEEEFTMA 586
Cdd:PRK10929 93 DEPRSVppnmstdaleqeilqvsSQLLEKSrqaQQEQDRAREISDSLSQ-----------------------LPQQQTEA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 587 RLYISKMKSEVKSLVNRSKQLESAQMDSnRKMNASERELAACQLLISQHEAKIKSLTDYMQ-NMEQKRR-QLEESQDSLS 664
Cdd:PRK10929 150 RRQLNEIERRLQTLGTPNTPLAQAQLTA-LQAESAALKALVDELELAQLSANNRQELARLRsELAKKRSqQLDAYLQALR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 665 EELAKLRAQEKmhevsfqDKEKEHLTRL-QDAEEVKKALEQQMESHREAHQ---KQLSRLrDEIEEKQRIIDeirdlNQK 740
Cdd:PRK10929 229 NQLNSQRQREA-------ERALESTELLaEQSGDLPKSIVAQFKINRELSQalnQQAQRM-DLIASQQRQAA-----SQT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 741 LQLEQerlssdynklkiedqerevklekllLLNDKREQAR--EDLKGLEET----VSR-----ELQTLHN------LRKL 803
Cdd:PRK10929 296 LQVRQ-------------------------ALNTLREQSQwlGVSNALGEAlraqVARlpempKPQQLDTemaqlrVQRL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 804 FVQDLTTRVKKSVELDSDDGGGSAAQKQKIsflennLEQLTKVHKQLVR------DNADLrcELPKLEKrlrATAErvka 877
Cdd:PRK10929 351 RYEDLLNKQPQLRQIRQADGQPLTAEQNRI------LDAQLRTQRELLNsllsggDTLIL--ELTKLKV---ANSQ---- 415
|
490
....*....|....
gi 45433560 878 LESALKEAKENAMR 891
Cdd:PRK10929 416 LEDALKEVNEATHR 429
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
413-761 |
1.36e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.87 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 413 KEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALE- 491
Cdd:pfam05483 403 KEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEk 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 492 ------ELAVNYDQKSQEVEDKTRANEQLTDELAQKTTT----LTTTQRELSQLQELSNHQKKRATEILNL---LLKDLG 558
Cdd:pfam05483 483 eklkniELTAHCDKLLLENKELTQEASDMTLELKKHQEDiincKKQEERMLKQIENLEEKEMNLRDELESVreeFIQKGD 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 559 EIGGIIGTNDVKTLADVNGVIEEEFTMARLYiSKMKSEVKSLVNRSKQLESAQMDS----------NRKMNASERELAAC 628
Cdd:pfam05483 563 EVKCKLDKSEENARSIEYEVLKKEKQMKILE-NKCNNLKKQIENKNKNIEELHQENkalkkkgsaeNKQLNAYEIKVNKL 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 629 QLLISQHEAKIKSLTD-YMQNMEQKRRQLE------ESQDSLSEELAKL------RAQEKMHE-VSFQDKEKEHLTRLQD 694
Cdd:pfam05483 642 ELELASAKQKFEEIIDnYQKEIEDKKISEEklleevEKAKAIADEAVKLqkeidkRCQHKIAEmVALMEKHKHQYDKIIE 721
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45433560 695 AEEVK----KALEQQMESHREAHQKQLSRLRDEIeekqriideirdLNQKLQLEQERlsSDYNKLKIEDQE 761
Cdd:pfam05483 722 ERDSElglyKNKEQEQSSAKAALEIELSNIKAEL------------LSLKKQLEIEK--EEKEKLKMEAKE 778
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
418-673 |
1.39e-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: 45.14 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 418 EEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNY 497
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 498 DQKSQEVEDKTRA----NEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEIlnlllkdlgeiggiigTNDVKTLA 573
Cdd:COG4942 100 EAQKEELAELLRAlyrlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL----------------RADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 574 DVNGVIEEEftmarlyiskmksevkslvnrSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKR 653
Cdd:COG4942 164 ALRAELEAE---------------------RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
250 260
....*....|....*....|
gi 45433560 654 RQLEESQDSLSEELAKLRAQ 673
Cdd:COG4942 223 EELEALIARLEAEAAAAAER 242
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
413-761 |
1.47e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 45.62 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 413 KEKYDEEITslyRQLDDKDDEINQQSQLAEKL-----KQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVL 487
Cdd:pfam06160 51 RKKWDDIVT---KSLPDIEELLFEAEELNDKYrfkkaKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 488 QALEELAVNYDQKSQEVEDktrANEQLTDELAQktttlttTQRELSQLQEL-SNHQKKRATEILNLLLKDLGEIGGIIgt 566
Cdd:pfam06160 128 DKYRELRKTLLANRFSYGP---AIDELEKQLAE-------IEEEFSQFEELtESGDYLEAREVLEKLEEETDALEELM-- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 567 NDVKTL-ADVNGVIEEEFTMARLYISKMKSEVKSL--VNRSKQLESAQMDSNRKMNASER-ELAACQLLISQHEAKIKSL 642
Cdd:pfam06160 196 EDIPPLyEELKTELPDQLEELKEGYREMEEEGYALehLNVDKEIQQLEEQLEENLALLENlELDEAEEALEEIEERIDQL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 643 TDYMQNMEQKRRQLEESQDSLSEELAKLRAQ-----EKMHEVS----FQDKEKEHL----TRLQDAEEVKKALEQQMESH 709
Cdd:pfam06160 276 YDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQnkelkEELERVQqsytLNENELERVrgleKQLEELEKRYDEIVERLEEK 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 45433560 710 REAHqkqlSRLRDEIEEKQRIIDEIRDlnqklqlEQERLSSDYNKLKIEDQE 761
Cdd:pfam06160 356 EVAY----SELQEELEEILEQLEEIEE-------EQEEFKESLQSLRKDELE 396
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
644-906 |
1.59e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.71 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 644 DYMQNMEQKR-----------------RQLEESQDSL---SEELAKLRAQEKMHEVSFQDKEkEHLTRLQDA-------- 695
Cdd:COG3096 272 DYMRHANERRelseralelrrelfgarRQLAEEQYRLvemARELEELSARESDLEQDYQAAS-DHLNLVQTAlrqqekie 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 696 ------EEVKKALEQQMESHREAHQkQLSRLRDEIEEKQRIIDEIR----DLNQKLQLEQERlssdynklKIEDQEREVK 765
Cdd:COG3096 351 ryqedlEELTERLEEQEEVVEEAAE-QLAEAEARLEAAEEEVDSLKsqlaDYQQALDVQQTR--------AIQYQQAVQA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 766 LEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRklfvqdLTTRVKKSVEldsddgggSAAQKQkisfLENNLEQLTK 845
Cdd:COG3096 422 LEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEV------LELEQKLSVA--------DAARRQ----FEKAYELVCK 483
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45433560 846 VHKQLVRDNADLRC-ELPKLEKRLRATAERVKALESALKEAkenamRDRKRYQQEVDRIKEA 906
Cdd:COG3096 484 IAGEVERSQAWQTArELLRRYRSQQALAQRLQQLRAQLAEL-----EQRLRQQQNAERLLEE 540
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
418-559 |
2.41e-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: 45.05 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 418 EEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELtrlqienEAAKDEVKEVLQALEELAVNY 497
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-------EALLNERASLEEALALLRSEL 896
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45433560 498 DQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGE 559
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEA 958
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
579-884 |
2.53e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 579 IEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEE 658
Cdd:pfam01576 136 LEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 659 SQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEVKKALEQQMESHREAhQKQLSRLRDEIEEKqriideiRDLN 738
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIREL-EAQISELQEDLESE-------RAAR 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 739 QKLQLEQERLSSDYNKLKIEDQEREVKLEKLLLLNDKREQAREDLK--GLEETVSRELQtlhnlrklfVQDLttRVKKSV 816
Cdd:pfam01576 288 NKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKkaLEEETRSHEAQ---------LQEM--RQKHTQ 356
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45433560 817 ELDSDDGGGSAAQKQKISflennleqLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKE 884
Cdd:pfam01576 357 ALEELTEQLEQAKRNKAN--------LEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE 416
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
445-787 |
2.79e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 445 KQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALeelavnydqKSQEVEDKTRAN-EQLTDELAQKTT 523
Cdd:PRK04863 299 RRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAL---------RQQEKIERYQADlEELEERLEEQNE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 524 TltttqRELSQLQELSNHQKKRATEILNLLLKdlgeiggiigtndvKTLADVNGVIEEEFTMARLYiskmkSEVKSLVNR 603
Cdd:PRK04863 370 V-----VEEADEQQEENEARAEAAEEEVDELK--------------SQLADYQQALDVQQTRAIQY-----QQAVQALER 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 604 SKQLesaqmdsnrkMNASERELAACQLLISQHEAKIKSLTDYMQNMEQK-------RRQLEESQD---SLSEELAKLRAQ 673
Cdd:PRK04863 426 AKQL----------CGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKlsvaqaaHSQFEQAYQlvrKIAGEVSRSEAW 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 674 EKMHEVSFQDKEKEHL-TRLQDAEEVKKALEQQMESHREAhqkqlSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLSSDY 752
Cdd:PRK04863 496 DVARELLRRLREQRHLaEQLQQLRMRLSELEQRLRQQQRA-----ERLLAEFCKRLGKNLDDEDELEQLQEELEARLESL 570
|
330 340 350
....*....|....*....|....*....|....*
gi 45433560 753 NKLKIEDQEREVKLEkllllnDKREQAREDLKGLE 787
Cdd:PRK04863 571 SESVSEARERRMALR------QQLEQLQARIQRLA 599
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
415-910 |
2.82e-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: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 415 KYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQ---ALE 491
Cdd:pfam01576 240 KKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDttaAQQ 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 492 ELAVNYDQKSQE----VEDKTRANEQLTDELAQKTTTLTTtqrELSQLQELSNHQKKRATEILNLLLKDLGEIggiigTN 567
Cdd:pfam01576 320 ELRSKREQEVTElkkaLEEETRSHEAQLQEMRQKHTQALE---ELTEQLEQAKRNKANLEKAKQALESENAEL-----QA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 568 DVKTLADVNGVIEEEFtmarlyiSKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQ 647
Cdd:pfam01576 392 ELRTLQQAKQDSEHKR-------KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVS 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 648 NMEQkrrQLEESQDSLSEEL-AKLRAQEKMHevSFQDKEKEHLTRLQDAEEVKKALEQQMESHreahQKQLSRLRDEIEE 726
Cdd:pfam01576 465 SLES---QLQDTQELLQEETrQKLNLSTRLR--QLEDERNSLQEQLEEEEEAKRNVERQLSTL----QAQLSDMKKKLEE 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 727 KQRIIDEIRDLNQKLQLEQERLSSDYnklkiedQEREVKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQ 806
Cdd:pfam01576 536 DAGTLEALEEGKKRLQRELEALTQQL-------EEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQ 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 807 DLTTRVKKSVEL--DSDDGGGSAAQKQ-KISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESAlK 883
Cdd:pfam01576 609 MLAEEKAISARYaeERDRAEAEAREKEtRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERS-K 687
|
490 500
....*....|....*....|....*...
gi 45433560 884 EAKENAMRDRKRYQQEV-DRIKEAVRAK 910
Cdd:pfam01576 688 RALEQQVEEMKTQLEELeDELQATEDAK 715
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
622-893 |
3.06e-04 |
|
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: 44.96 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 622 ERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHE--VSFQDKEKEHLTRLQDAEEVK 699
Cdd:TIGR00618 197 ELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEeqLKKQQLLKQLRARIEELRAQE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 700 KALEQQMEshREAHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLSSDYNKLKIEDQEREVKLEKLLLLN------ 773
Cdd:TIGR00618 277 AVLEETQE--RINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQtlhsqe 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 774 DKREQAREDLKGLEETVSRELQTLHNLRKLfVQDLTTrvkksveldsddgggsaaQKQKISFLENNLEQLTK-VHKQLVR 852
Cdd:TIGR00618 355 IHIRDAHEVATSIREISCQQHTLTQHIHTL-QQQKTT------------------LTQKLQSLCKELDILQReQATIDTR 415
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 45433560 853 DNA--DLRCELPKLEKRLRATAERVKALESAL-KEAKENAMRDR 893
Cdd:TIGR00618 416 TSAfrDLQGQLAHAKKQQELQQRYAELCAAAItCTAQCEKLEKI 459
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
429-687 |
3.36e-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: 44.34 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 429 DKDDEINQQSQLAEKLKQQMLDQDELLASTRRdyekiQEELTRLQIENEAAKDEVKEVLQALEElavnydQKSQEVEDKT 508
Cdd:pfam17380 345 ERERELERIRQEERKRELERIRQEEIAMEISR-----MRELERLQMERQQKNERVRQELEAARK------VKILEEERQR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 509 RANEQLTDELAQKTTTLTTTQRELSQLQElsnhqkKRATEILNLLLKDLGEiggiigTNDVKTLADVngviEEEFTMARL 588
Cdd:pfam17380 414 KIQQQKVEMEQIRAEQEEARQREVRRLEE------ERAREMERVRLEEQER------QQQVERLRQQ----EEERKRKKL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 589 YISKMKSEVKSLVNRSKQLESAQMDSN--------RKMNASERELAACQLLISQHEAKIKSLTDYMQNME-QKRRQLEES 659
Cdd:pfam17380 478 ELEKEKRDRKRAEEQRRKILEKELEERkqamieeeRKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEmEERRRIQEQ 557
|
250 260
....*....|....*....|....*...
gi 45433560 660 QDSLSEELAKLRAQEKMHEVSFQDKEKE 687
Cdd:pfam17380 558 MRKATEERSRLEAMEREREMMRQIVESE 585
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
380-916 |
5.98e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 380 EQISAKDQKSLEPCDNTPIIDNITPVVDGISAEKEKYDEEItslYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTR 459
Cdd:pfam02463 496 EERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGV---AVENYKVAISTAVIVEVSATADEVEERQKLVRALTE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 460 RDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELS 539
Cdd:pfam02463 573 LPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGV 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 540 NHQKKRATEilNLLLKDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKmn 619
Cdd:pfam02463 653 SLEEGLAEK--SEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQ-- 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 620 aSERELAACQLLISQHEAKIKSLTDymQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEVK 699
Cdd:pfam02463 729 -EAQDKINEELKLLKQKIDEEEEEE--EKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRA 805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 700 KaleQQMESHREAHQKQLSRLRDEIEEKQriIDEIRDLNQKLQLEQERlssdyNKLKIEDQEREVKLEKLLLLNDKREQA 779
Cdd:pfam02463 806 L---EEELKEEAELLEEEQLLIEQEEKIK--EEELEELALELKEEQKL-----EKLAEEELERLEEEITKEELLQELLLK 875
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 780 REDLkgLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDSDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRC 859
Cdd:pfam02463 876 EEEL--EEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEEN 953
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 45433560 860 ELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRA 916
Cdd:pfam02463 954 NKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRA 1010
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
650-745 |
6.82e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 650 EQKRRQLEESQDSLSEELAKLRAQEKmhevSFQDKEKEHLTRLQDAEEVKKALEQQMESHREAHQKQLSRLRDEIEE--- 726
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELER----ELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQaik 580
|
90 100
....*....|....*....|.
gi 45433560 727 --KQRIIDEIRDLNQKLQLEQ 745
Cdd:PRK00409 581 eaKKEADEIIKELRQLQKGGY 601
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
590-735 |
7.34e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 590 ISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDyMQNMEQKRRQLEesqdSLSEELAK 669
Cdd:COG1579 26 LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE-QLGNVRNNKEYE----ALQKEIES 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45433560 670 LRAQEKMHEvsfqDKEKEHLTRLQDAEEVKKALEQQMESHREAHQKQLSRLRDEIEEKQRIIDEIR 735
Cdd:COG1579 101 LKRRISDLE----DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
624-783 |
7.41e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 624 ELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKE------KEHLTRLQDAEE 697
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEarikkyEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 698 VKkALEQQMESHReahqKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLSSDYNKLKIE-DQEREVKLEKLLLLNDKR 776
Cdd:COG1579 91 YE-ALQKEIESLK----RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAElDEELAELEAELEELEAER 165
|
....*..
gi 45433560 777 EQAREDL 783
Cdd:COG1579 166 EELAAKI 172
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
697-915 |
8.37e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 697 EVKKALEQQMESHR------EAHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLSSDYNKLKiedqEREVKLEKLL 770
Cdd:PRK03918 169 EVIKEIKRRIERLEkfikrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 771 LLNDKREQareDLKGLEETVsRELQTLHNLRKLFVQDLTTRVKKSVELDsddggGSAAQKQKIS-FLENNLEQLTKVHKq 849
Cdd:PRK03918 245 KELESLEG---SKRKLEEKI-RELEERIEELKKEIEELEEKVKELKELK-----EKAEEYIKLSeFYEEYLDELREIEK- 314
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45433560 850 lvrdnadlrcELPKLEKRLRATAERVKALESALKEAKENAMRdRKRYQQEVDRIKEAVRAKNMARR 915
Cdd:PRK03918 315 ----------RLSRLEEEINGIEERIKELEEKEERLEELKKK-LKELEKRLEELEERHELYEEAKA 369
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
625-924 |
9.82e-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: 42.44 E-value: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 625 LAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQekmhevsfqdkekehltrLQDAEEVKKALEQ 704
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR------------------IAALARRIRALEQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 705 QMEshreAHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLSS-DYNKLKIEDQEREVKLEKLLLLNDKREQAREDL 783
Cdd:COG4942 77 ELA----ALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 784 KGLEETvsreLQTLHNLRklfvqdlttrvkksveldsddgggsAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPK 863
Cdd:COG4942 153 EELRAD----LAELAALR-------------------------AELEAERAELEALLAELEEERAALEALKAERQKLLAR 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45433560 864 LEKRLRATAERVKALEsalkeakenamRDRKRYQQEVDRIKEAVRAKnmARRAHSAQIAKP 924
Cdd:COG4942 204 LEKELAELAAELAELQ-----------QEAEELEALIARLEAEAAAA--AERTPAAGFAAL 251
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
604-734 |
1.00e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 604 SKQLESAQMDSNRKMNASERELAA----CQL--------LISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLR 671
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAikkeALLeakeeihkLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45433560 672 AQEKMHEVSFQDKEKEHLTRLQDAEEVKKALEQQME-----SHREAHQKQLSRLRDEIE-EKQRIIDEI 734
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIEEQLQELErisglTAEEAKEILLEKVEEEARhEAAVLIKEI 178
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
605-762 |
1.01e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 605 KQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDK 684
Cdd:pfam07888 55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 685 EKEHLTRLQDAEEVkkalEQQMESHREAHQKQLSRLRDEIEEKqriideiRDLNQKLQLEQE---RLSSDYNKLKIEDQE 761
Cdd:pfam07888 135 EEDIKTLTQRVLER----ETELERMKERAKKAGAQRKEEEAER-------KQLQAKLQQTEEelrSLSKEFQELRNSLAQ 203
|
.
gi 45433560 762 R 762
Cdd:pfam07888 204 R 204
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
683-920 |
1.03e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 683 DKEKEHLTRLQDaeeVKKALEQQMES-HREAHQ-KQLSRLRDEIEEKQRII--DEIRDLNQKLqleqERLSSDYNKLkie 758
Cdd:TIGR02168 182 ERTRENLDRLED---ILNELERQLKSlERQAEKaERYKELKAELRELELALlvLRLEELREEL----EELQEELKEA--- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 759 dqerevklekllllNDKREQAREDLKGLEETVSrELQTLHNLRKLFVQDLTTRVKksveldsddgggsaAQKQKISFLEN 838
Cdd:TIGR02168 252 --------------EEELEELTAELQELEEKLE-ELRLEVSELEEEIEELQKELY--------------ALANEISRLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 839 NLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHS 918
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
..
gi 45433560 919 AQ 920
Cdd:TIGR02168 383 TL 384
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
444-673 |
1.15e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 444 LKQQMLDQDELLAstrrDYEKIQEELTRL-QIENEAAKDEVK-EVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQ- 520
Cdd:COG4913 213 VREYMLEEPDTFE----AADALVEHFDDLeRAHEALEDAREQiELLEPIRELAERYAAARERLAELEYLRAALRLWFAQr 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 521 KTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTNDVKTLADvngvIEEEftmarlyISKMKSEVKSL 600
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ----LERE-------IERLERELEER 357
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45433560 601 VNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQN----MEQKRRQLEESQDSLSEELAKLRAQ 673
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEalaeAEAALRDLRRELRELEAEIASLERR 434
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
475-712 |
1.38e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 475 ENEAAKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQElsnhQKKRATEILNLLL 554
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA----EIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 555 KDLGEIGGIIGTNDV----KTLADvngvieeeftmarlYISKMKSeVKSLVNRSKQLESAQMDSNRKMNASERELaacql 630
Cdd:COG3883 93 RALYRSGGSVSYLDVllgsESFSD--------------FLDRLSA-LSKIADADADLLEELKADKAELEAKKAEL----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 631 lisqhEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEVKKALEQQMESHR 710
Cdd:COG3883 153 -----EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
..
gi 45433560 711 EA 712
Cdd:COG3883 228 AA 229
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
397-559 |
1.89e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 397 PIIDNITPVVDGISAEKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMldqdellastrrdyEKIQEELTRLQIEN 476
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI--------------DKLQAEIAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 477 EAAKDEVKEVL-----------------------------QALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTT 527
Cdd:COG3883 82 EERREELGERAralyrsggsvsyldvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA 161
|
170 180 190
....*....|....*....|....*....|..
gi 45433560 528 TQRELSQLQELSNHQKKRATEILNLLLKDLGE 559
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
599-921 |
1.94e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.04 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 599 SLVNRSKQLESAQMDSNRKMNASERELAAcqlLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHE 678
Cdd:pfam05557 10 RLSQLQNEKKQMELEHKRARIELEKKASA---LKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 679 vSFQDKEKEHLTRLQDAEEVKKALEQQM-ESHREAH--QKQLSRLRDEIEEKQRIIDEIR-------DLNQKLQLEQERL 748
Cdd:pfam05557 87 -ALNKKLNEKESQLADAREVISCLKNELsELRRQIQraELELQSTNSELEELQERLDLLKakaseaeQLRQNLEKQQSSL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 749 SSDYNKLKIEDQE-REVKLEKLLLLNDKREQAR-----EDLKGLEETVS--RELQTLHNLRKLFVQDLTTRVKKsVELDS 820
Cdd:pfam05557 166 AEAEQRIKELEFEiQSQEQDSEIVKNSKSELARipeleKELERLREHNKhlNENIENKLLLKEEVEDLKRKLER-EEKYR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 821 DDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEaKENAMRDrkrYQQEV 900
Cdd:pfam05557 245 EEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQ-LEKARRE---LEQEL 320
|
330 340
....*....|....*....|.
gi 45433560 901 DRIKEAVRAKNMARRAHSAQI 921
Cdd:pfam05557 321 AQYLKKIEDLNKKLKRHKALV 341
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
409-621 |
2.09e-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: 41.67 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 409 ISAEKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQmldqdelLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQ 488
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE-------LAALEAELAELEKEIAELRAELEAQKEELAELLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 489 ALEELAVNYDQK----SQEVEDKTRANE---QLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIg 561
Cdd:COG4942 112 ALYRLGRQPPLAlllsPEDFLDAVRRLQylkYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL- 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 562 giigTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNAS 621
Cdd:COG4942 191 ----EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
374-923 |
2.25e-03 |
|
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: 42.13 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 374 EAVPEDEQISaKDQKS--LEPCDNTPIIDNITPVVDGISAEKEKYDE---EITSLYRQLddkddeINQQSQLAEKLKQQM 448
Cdd:pfam12128 210 GVVPPKSRLN-RQQVEhwIRDIQAIAGIMKIRPEFTKLQQEFNTLESaelRLSHLHFGY------KSDETLIASRQEERQ 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 449 LDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVK---EVLQALEELAVNYDQKSQEvedkTRANEQltDELAQKTTTL 525
Cdd:pfam12128 283 ETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAkdrSELEALEDQHGAFLDADIE----TAAADQ--EQLPSWQSEL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 526 TTTQRELSQLqeLSNHQK-KRATEILNLLLKdlgeiggiigtndvKTLADVNGVIEEEFTMARLYISKMKSEVKSLVnrs 604
Cdd:pfam12128 357 ENLEERLKAL--TGKHQDvTAKYNRRRSKIK--------------EQNNRDIAGIKDKLAKIREARDRQLAVAEDDL--- 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 605 KQLESAQmdsNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSeelaklRAQEKmhevsfQDK 684
Cdd:pfam12128 418 QALESEL---REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIE------RAREE------QEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 685 EKEHLTRLQDAEEV-KKALEQQMESHREAHQKqLSRLRDEIEEKQRIIDE-----IRDLNQKLQLEQERLS--------- 749
Cdd:pfam12128 483 ANAEVERLQSELRQaRKRRDQASEALRQASRR-LEERQSALDELELQLFPqagtlLHFLRKEAPDWEQSIGkvispellh 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 750 -SDYNKLKIEDQEREVKLEKLLLLNDKREQAREDLKgLEETVSREL----QTLHNLRKLFVQDLTTRVKKSVELDSDDGG 824
Cdd:pfam12128 562 rTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAA-SEEELRERLdkaeEALQSAREKQAAAEEQLVQANGELEKASRE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 825 GSAAqKQKISFLENNLEQLTKVHKQL-VRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRD-------RKRY 896
Cdd:pfam12128 641 ETFA-RTALKNARLDLRRLFDEKQSEkDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQkrearteKQAY 719
|
570 580 590
....*....|....*....|....*....|....*
gi 45433560 897 QQEV--------DRIKEAVRAKNMARRAHSAQIAK 923
Cdd:pfam12128 720 WQVVegaldaqlALLKAAIAARRSGAKAELKALET 754
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
453-727 |
2.97e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 453 ELLASTRRdyeKIQEELTRLQI---ENEAAKDEVKEVLQALEELavnyDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQ 529
Cdd:PHA02562 146 QLSAPARR---KLVEDLLDISVlseMDKLNKDKIRELNQQIQTL----DMKIDHIQQQIKTYNKNIEEQRKKNGENIARK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 530 RE-----LSQLQELSNHQKKRATEILNLllkdlgeiggiigtndVKTLADVNGVIEEeFTMARlyiSKMKSEVKSLvnrS 604
Cdd:PHA02562 219 QNkydelVEEAKTIKAEIEELTDELLNL----------------VMDIEDPSAALNK-LNTAA---AKIKSKIEQF---Q 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 605 KQLesaqmdsnrKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLR-AQEKMHEVSFQ- 682
Cdd:PHA02562 276 KVI---------KMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNeQSKKLLELKNKi 346
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 45433560 683 DKEKEHLTRLQD-AEEVKKALEqQMESHREAHQKQLSRLRDEIEEK 727
Cdd:PHA02562 347 STNKQSLITLVDkAKKVKAAIE-ELQAEFVDNAEELAKLQDELDKI 391
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
399-822 |
3.24e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 399 IDNITPVVDGISAEKEKYDEEITSLYRQLDDKDDEINQQSQLaEKLKQQMLDQDEL---LASTRRDYEKIQEELTRLQIE 475
Cdd:PRK01156 307 IENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRY-DDLNNQILELEGYemdYNSYLKSIESLKKKIEEYSKN 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 476 NEAAKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKK-------RATE 548
Cdd:PRK01156 386 IERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgttLGEE 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 549 ILNLLLKDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNaSERELAAC 628
Cdd:PRK01156 466 KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKI-KINELKDK 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 629 QLLISQHEAKIKSL---------TDYMQNMEQKRRQLEESQDSLSEELAKL--RAQEKMHEV--------SFQDKEKEHL 689
Cdd:PRK01156 545 HDKYEEIKNRYKSLkledldskrTSWLNALAVISLIDIETNRSRSNEIKKQlnDLESRLQEIeigfpddkSYIDKSIREI 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 690 TRLQDAEEVKKALEQQMESHREAHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLS-------------------- 749
Cdd:PRK01156 625 ENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKksrkalddakanrarlesti 704
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 750 ----SDYNKLKIEDQEREVKLEKLlllnDKREQAREDLKGLEETVSRE-LQTLhnLRKLFVQDLTTRVKK---SVELDSD 821
Cdd:PRK01156 705 eilrTRINELSDRINDINETLESM----KKIKKAIGDLKRLREAFDKSgVPAM--IRKSASQAMTSLTRKylfEFNLDFD 778
|
.
gi 45433560 822 D 822
Cdd:PRK01156 779 D 779
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
412-740 |
3.63e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.35 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 412 EKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEE-------LTRLQiENEAAKDEVK 484
Cdd:pfam10174 374 EKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDssntdtaLTTLE-EALSEKERII 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 485 EVLQalEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEI---- 560
Cdd:pfam10174 453 ERLK--EQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVeqkk 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 561 -GGIIGTNDVKT-------------LADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNaserELA 626
Cdd:pfam10174 531 eECSKLENQLKKahnaeeavrtnpeINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIA----ELE 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 627 ACQLLISQHEAKIKSLTDYMQNMEQKRR--QLEES---QDSLSEELAKLRAQEKMHEVSfqdKEKEHLtrlqDAEEVKKA 701
Cdd:pfam10174 607 SLTLRQMKEQNKKVANIKHGQQEMKKKGaqLLEEArrrEDNLADNSQQLQLEELMGALE---KTRQEL----DATKARLS 679
|
330 340 350
....*....|....*....|....*....|....*....
gi 45433560 702 LEQQMESHREAHqkqLSRLRdeiEEKQRIIDEIRDLNQK 740
Cdd:pfam10174 680 STQQSLAEKDGH---LTNLR---AERRKQLEEILEMKQE 712
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
410-758 |
4.07e-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: 40.86 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 410 SAEKEKYDEEITSLYRQLDDKDDEINQQSQL-AEKLKQQMLDQDELLA-------------------------STRRDYE 463
Cdd:pfam05483 249 ITEKENKMKDLTFLLEESRDKANQLEEKTKLqDENLKELIEKKDHLTKeledikmslqrsmstqkaleedlqiATKTICQ 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 464 KIQEELTRLQIENEAAK------DEVKEVLQALEELAVNYDQKSQEVEDK----TRANEQLTDELAQKTTTLTTTQRELS 533
Cdd:pfam05483 329 LTEEKEAQMEELNKAKAahsfvvTEFEATTCSLEELLRTEQQRLEKNEDQlkiiTMELQKKSSELEEMTKFKNNKEVELE 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 534 QLQELSN------HQKKRATEILNLLLKDLGEIGGIIGTNDvKTLADVNgVIEEEFTMARLYISKMKSEVKSLVNRSKqL 607
Cdd:pfam05483 409 ELKKILAedekllDEKKQFEKIAEELKGKEQELIFLLQARE-KEIHDLE-IQLTAIKTSEEHYLKEVEDLKTELEKEK-L 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 608 ESAQMDSNRKMNASE-----RELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQekmhevsFQ 682
Cdd:pfam05483 486 KNIELTAHCDKLLLEnkeltQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREE-------FI 558
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45433560 683 DKEKEHLTRLQDAEEVKKALEQQM---ESHREAHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLSSDYNKLKIE 758
Cdd:pfam05483 559 QKGDEVKCKLDKSEENARSIEYEVlkkEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIK 637
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
630-742 |
4.09e-03 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 39.42 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 630 LLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEvkkALEQQMESH 709
Cdd:pfam06785 76 KLTELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEE---QLAEKQLLI 152
|
90 100 110
....*....|....*....|....*....|...
gi 45433560 710 REaHQKQLSRLRDEIEEKQriiDEIRDLNQKLQ 742
Cdd:pfam06785 153 NE-YQQTIEEQRSVLEKRQ---DQIENLESKVR 181
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
419-517 |
4.16e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 419 EITSLYRQLDDKDDEINQ-QSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNY 497
Cdd:COG0542 405 EIDSKPEELDELERRLEQlEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRY 484
|
90 100
....*....|....*....|
gi 45433560 498 DQKSQEVEDKTRANEQLTDE 517
Cdd:COG0542 485 GKIPELEKELAELEEELAEL 504
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
385-909 |
4.40e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.19 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 385 KDQKSLEPCDNTPII--DNI-TPVVDGISAEKEKYDEEITSLYRQLDDKDdEINQQSQLAEKLKQQMLDqdellastrrd 461
Cdd:TIGR01612 1204 KDKTSLEEVKGINLSygKNLgKLFLEKIDEEKKKSEHMIKAMEAYIEDLD-EIKEKSPEIENEMGIEMD----------- 1271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 462 yekIQEELTRLQIENEAAKDEvkevlqalEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNH 541
Cdd:TIGR01612 1272 ---IKAEMETFNISHDDDKDH--------HIISKKHDENISDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQKHNSD 1340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 542 QKKRATEILNL--LLKdLGEIGGIIgtNDVK----TLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKqLESAQMDsn 615
Cdd:TIGR01612 1341 INLYLNEIANIynILK-LNKIKKII--DEVKeytkEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSK-IESTLDD-- 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 616 RKMNASERELAACQLLISQHEAKIKSltdYMQNMEQKRRQLE------ESQDSLSEELAKLRAQEKMHEVSFQDKE-KEH 688
Cdd:TIGR01612 1415 KDIDECIKKIKELKNHILSEESNIDT---YFKNADENNENVLllfkniEMADNKSQHILKIKKDNATNDHDFNINElKEH 1491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 689 LTRLQ----DAEEVKKALEQQMESHrEAHQKQLSRLRDEIEE-------------KQRIIDEIRDLNQKLQLEQERLSSD 751
Cdd:TIGR01612 1492 IDKSKgckdEADKNAKAIEKNKELF-EQYKKDVTELLNKYSAlaiknkfaktkkdSEIIIKEIKDAHKKFILEAEKSEQK 1570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 752 YNKLKIEdqerEVKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDL--TTRVKKSVELDSDDgggsaAQ 829
Cdd:TIGR01612 1571 IKEIKKE----KFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLkeTESIEKKISSFSID-----SQ 1641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 830 KQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKrlrataervkaLESALKEAKENAMRDRKRYQQE-VDRIKEAVR 908
Cdd:TIGR01612 1642 DTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDE-----------LDSEIEKIEIDVDQHKKNYEIGiIEKIKEIAI 1710
|
.
gi 45433560 909 A 909
Cdd:TIGR01612 1711 A 1711
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
590-735 |
5.98e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.06 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 590 ISKMKSEVKSLVNRSKQLESAQmdsnrkmNASERELAAcQLLISQHEAKIKSLTDYMQNMEQKRRQ--------LEESQD 661
Cdd:PRK11637 98 LNQLNKQIDELNASIAKLEQQQ-------AAQERLLAA-QLDAAFRQGEHTGLQLILSGEESQRGErilayfgyLNQARQ 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45433560 662 SLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDaeevKKALEQQMESHREAHQKQLSRLRDEIEEKQRIIDEIR 735
Cdd:PRK11637 170 ETIAELKQTREELAAQKAELEEKQSQQKTLLYE----QQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELR 239
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
647-806 |
6.63e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 647 QNMEQKRRQLEESQDSLSEELAKLR-----AQEKMHE-------VSFQDKEKEHLTRLQDAEEVKKALEQQM---ESHRE 711
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRkeleeAEAALEEfrqknglVDLSEEAKLLLQQLSELESQLAEARAELaeaEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 712 AHQKQLSRLRDEIEEK------QRIIDEIRDLNQKLQLEQERLSSDYNKLK--------IEDQEREVKLEKLLLLNDKRE 777
Cdd:COG3206 244 ALRAQLGSGPDALPELlqspviQQLRAQLAELEAELAELSARYTPNHPDVIalraqiaaLRAQLQQEAQRILASLEAELE 323
|
170 180
....*....|....*....|....*....
gi 45433560 778 QAREDLKGLEETVSRELQTLHNLRKLFVQ 806
Cdd:COG3206 324 ALQAREASLQAQLAQLEARLAELPELEAE 352
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
496-923 |
6.96e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 496 NYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNllLKDLGEIGGIIGTNDVKTLADV 575
Cdd:PTZ00121 1080 DFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARK--AEDARKAEEARKAEDAKRVEIA 1157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 576 NGVIEEEftmaRLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQlliSQHEAKIKSLTDY--MQNMEQKR 653
Cdd:PTZ00121 1158 RKAEDAR----KAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARK---AEEERKAEEARKAedAKKAEAVK 1230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 654 RQLEESQDslsEELAKLRAQEKMHEV--SFQDKEKEHLTRLQD---AEEVKKALE-QQMESHREAHQKQLSRLRDEIEEK 727
Cdd:PTZ00121 1231 KAEEAKKD---AEEAKKAEEERNNEEirKFEEARMAHFARRQAaikAEEARKADElKKAEEKKKADEAKKAEEKKKADEA 1307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 728 QRIIDEIRDLNQ-KLQLEQERLSSDYNKLKIEDQEREV--KLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLF 804
Cdd:PTZ00121 1308 KKKAEEAKKADEaKKKAEEAKKKADAAKKKAEEAKKAAeaAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA 1387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 805 VQ-DLTTRVKKSVELD---SDDGGGSAAQKQKISFLENNLEQLTKVhkqlvrDNADLRCELPKLEKRLRATAERVKALES 880
Cdd:PTZ00121 1388 EEkKKADEAKKKAEEDkkkADELKKAAAAKKKADEAKKKAEEKKKA------DEAKKKAEEAKKADEAKKKAEEAKKAEE 1461
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 45433560 881 ALKEAKENAMRDRKRYQQEVDR-----IKEAVRAKNMARRAHSAQIAK 923
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKkadeaKKKAEEAKKKADEAKKAAEAK 1509
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
567-954 |
7.23e-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: 40.34 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 567 NDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNrKMNASERELAACQLLISQHEAKIKSLTDYM 646
Cdd:pfam02463 184 NLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL-KLNEERIDLLQELLRDEQEEIESSKQEIEK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 647 QNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEVKKALEQQMEshrEAHQKQLSRLRDEIEE 726
Cdd:pfam02463 263 EEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK---KKAEKELKKEKEEIEE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 727 KQRIIDEIRDLNQKLQLEQERLSSDYNKLKIEDQEREVKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQ 806
Cdd:pfam02463 340 LEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLED 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 807 DLTTRVKKSVELDSDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEA- 885
Cdd:pfam02463 420 LLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERs 499
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 886 -KENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIAKPIRPGHYPASSPTAVHAVRGGGGGSSNSTHY 954
Cdd:pfam02463 500 qKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRA 569
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
625-898 |
7.95e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 39.68 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 625 LAACQLLI--SQHEAKIKS-LTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKmhevsfqdkekehltrlqdaeevkkA 701
Cdd:PRK11637 29 LSAGVLLCafSAHASDNRDqLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEE-------------------------A 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 702 LEQQMESHREAhQKQLSRLRDEIEEkqrIIDEIRDLnQKLQLEQERLSS----------DYNKLKI-----EDQEREVKL 766
Cdd:PRK11637 84 ISQASRKLRET-QNTLNQLNKQIDE---LNASIAKL-EQQQAAQERLLAaqldaafrqgEHTGLQLilsgeESQRGERIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 767 EKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDsddgGGSAAQKQKISFLENNLEqltKV 846
Cdd:PRK11637 159 AYFGYLNQARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLE----QARNERKKTLTGLESSLQ---KD 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 45433560 847 HKQLVrdnadlrcELPKLEKRLR---ATAERvKALESALKEAKEnAMRDRKRYQQ 898
Cdd:PRK11637 232 QQQLS--------ELRANESRLRdsiARAER-EAKARAEREARE-AARVRDKQKQ 276
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
650-792 |
7.99e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 39.93 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 650 EQKRRQLEESQDSLSEELaKLRAQeKMHEVSFQDKEKEHLTRLQDAEEVKKALEQQMESHREAHQKQLSRLRDEIE---- 725
Cdd:pfam15709 372 EKMREELELEQQRRFEEI-RLRKQ-RLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAEraea 449
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45433560 726 EKQRiideIRDLNQKLQLEQERLssdynkLKIEDQEREVKLEKLLLLNDKREQAREDLKGLEETVSR 792
Cdd:pfam15709 450 EKQR----QKELEMQLAEEQKRL------MEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAAR 506
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
644-887 |
9.03e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.06 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 644 DYMQNMEQKRRQLEESQDSLSEelaklraQEKMHEVSFQDKEKehLTRLQDAEEVKKALEQQMESHREAHQKQLSRLRDE 723
Cdd:COG5022 872 QSAQRVELAERQLQELKIDVKS-------ISSLKLVNLELESE--IIELKKSLSSDLIENLEFKTELIARLKKLLNNIDL 942
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 724 IE------EKQRIIDEIRDLNQKLQLEQERLSSDYNKLKIEDQEREVKLEKLLLLNDKREQAREDLKGLEETVSRelqtl 797
Cdd:COG5022 943 EEgpsieyVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQ----- 1017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433560 798 HNLRKLFVQDLTTRVKKSVELDSddgggSAAQKQKISFLENNLEQLTKVHKQLVRdNADLRCELPKLEKRLRATAERVKA 877
Cdd:COG5022 1018 LKELPVEVAELQSASKIISSEST-----ELSILKPLQKLKGLLLLENNQLQARYK-ALKLRRENSLLDDKQLYQLESTEN 1091
|
250
....*....|
gi 45433560 878 LESALKEAKE 887
Cdd:COG5022 1092 LLKTINVKDL 1101
|
|
| |
