|
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: 655.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 6 ECSIKVMCRFRPLNEAEILRGDKFIPKFKGDETVVIG---QGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTI 82
Cdd:cd01369 1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIAtseTGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 83 FAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNR 162
Cdd:cd01369 81 FAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLDVSKTNLSVHEDKNR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 163 VPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEKVSKT 242
Cdd:cd01369 161 GPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEKVSKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 243 GAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQ 322
Cdd:cd01369 241 GAEGAVLDEAKKINKSLSALGNVINALTDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQ 320
|
....*
gi 4758650 323 RAKTI 327
Cdd:cd01369 321 RAKTI 325
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
8-334 |
6.43e-155 |
|
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: 459.73 E-value: 6.43e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 8 SIKVMCRFRPLNEAEILRGDKFIPKF---KGDETVVI-----GQGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYN 79
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFpdkVGKTLTVRspknrQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 80 GTIFAYGQTSSGKTHTMEGklhDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHED 159
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIG---TPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSKKLEIRED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 160 KNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQE--NVETEKKLSGKLYLVDLAGSE 237
Cdd:smart00129 158 EKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKikNSSSGSGKASKLNLVDLAGSE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 238 KVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTK-THVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKS 316
Cdd:smart00129 238 RAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKsRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLS 317
|
330
....*....|....*...
gi 4758650 317 TLMFGQRAKTIKNTVSVN 334
Cdd:smart00129 318 TLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
14-327 |
9.79e-155 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 458.96 E-value: 9.79e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 14 RFRPLNEAEILRGDKFI-----PKFKGDETVVIGQGKP---YVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAY 85
Cdd:pfam00225 1 RVRPLNEREKERGSSVIvsvesVDSETVESSHLTNKNRtktFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 86 GQTSSGKTHTMEGKLHDPqlmGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTN---LAVHEDKNR 162
Cdd:pfam00225 81 GQTGSGKTYTMEGSDEQP---GIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNkrkLRIREDPKK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 163 VPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKK---LSGKLYLVDLAGSEKV 239
Cdd:pfam00225 158 GVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEesvKTGKLNLVDLAGSERA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 240 SKTG-AEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTL 318
Cdd:pfam00225 238 SKTGaAGGQRLKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTL 317
|
....*....
gi 4758650 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 |
1.04e-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: 456.33 E-value: 1.04e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 8 SIKVMCRFRPLNEAEILRGDKFIpKFKGDETVVIG-------QGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNG 80
Cdd:cd00106 1 NVRVAVRVRPLNGREARSAKSVI-SVDGGKSVVLDppknrvaPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 81 TIFAYGQTSSGKTHTMEGKlhDPQLMGIIPRIAHDIFDHIYSMDE-NLEFHIKVSYFEIYLDKIRDLLD-VSKTNLAVHE 158
Cdd:cd00106 80 TIFAYGQTGSGKTYTMLGP--DPEQRGIIPRALEDIFERIDKRKEtKSSFSVSASYLEIYNEKIYDLLSpVPKKPLSLRE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 159 DKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVET--EKKLSGKLYLVDLAGS 236
Cdd:cd00106 158 DPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKsgESVTSSKLNLVDLAGS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 237 EKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKS 316
Cdd:cd00106 238 ERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLS 317
|
....*....
gi 4758650 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 |
2.09e-120 |
|
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: 369.74 E-value: 2.09e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 8 SIKVMCRFRPLNEAEILRGDKFIPKFKGDETVVIGQ-GKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAYG 86
Cdd:cd01374 1 KITVTVRVRPLNSREIGINEQVAWEIDNDTIYLVEPpSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 87 QTSSGKTHTMEGKLHDPqlmGIIPRIAHDIFDHIYsMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNRVPYV 166
Cdd:cd01374 81 QTSSGKTFTMSGDEDEP---GIIPLAIRDIFSKIQ-DTPDREFLLRVSYLEIYNEKINDLLSPTSQNLKIRDDVEKGVYV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 167 KGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIK---QENVETEKKLSGKLYLVDLAGSEKVSKTG 243
Cdd:cd01374 157 AGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIEsseRGELEEGTVRVSTLNLIDLAGSERAAQTG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 244 AEGAVLDEAKNINKSLSALGNVISALAEGTK-THVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQ 322
Cdd:cd01374 237 AAGVRRKEGSHINKSLLTLGTVISKLSEGKVgGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFAS 316
|
....*
gi 4758650 323 RAKTI 327
Cdd:cd01374 317 RAKKI 321
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
7-328 |
1.22e-118 |
|
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: 365.89 E-value: 1.22e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 7 CSIKVMCRFRPLNEAEILRGDKFIPKFKGDET-VVIGQGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAY 85
Cdd:cd01372 1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPqVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 86 GQTSSGKTHTMEG----KLHDPQlMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLD---VSKTNLAVHE 158
Cdd:cd01372 81 GQTGSGKTYTMGTaytaEEDEEQ-VGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDpetDKKPTISIRE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 159 DKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSG----------KL 228
Cdd:cd01372 160 DSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSaddknstftsKF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 229 YLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTK--THVPYRDSKMTRILQDSLGGNCRTTIVICCSP 306
Cdd:cd01372 240 HFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKkgAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSP 319
|
330 340
....*....|....*....|..
gi 4758650 307 SVFNEAETKSTLMFGQRAKTIK 328
Cdd:cd01372 320 ADSNFEETLNTLKYANRARNIK 341
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
8-327 |
3.03e-112 |
|
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: 348.68 E-value: 3.03e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 8 SIKVMCRFRPLNEAEILRGDK---FIPKFKGDETVVIGQG------KPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGY 78
Cdd:cd01371 2 NVKVVVRCRPLNGKEKAAGALqivDVDEKRGQVSVRNPKAtaneppKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 79 NGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLL--DVSKtNLAV 156
Cdd:cd01371 82 NGTIFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLgkDQTK-RLEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 157 HEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLS---GKLYLVDL 233
Cdd:cd01371 161 KERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENHirvGKLNLVDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 234 AGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAE 313
Cdd:cd01371 241 AGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDE 320
|
330
....*....|....
gi 4758650 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 |
2.00e-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: 338.41 E-value: 2.00e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 9 IKVMCRFRPLNEAEILRGDKFI--PKFKGDETVVIGQG---KPYVFDRVLPPNTTQEQVYNAcAKQIVKDVLEGYNGTIF 83
Cdd:cd01366 4 IRVFCRVRPLLPSEENEDTSHItfPDEDGQTIELTSIGakqKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCIF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 84 AYGQTSSGKTHTMEGklhDPQLMGIIPRIAHDIFDHIYSMDEN-LEFHIKVSYFEIYLDKIRDLL---DVSKTNLAVHED 159
Cdd:cd01366 83 AYGQTGSGKTYTMEG---PPESPGIIPRALQELFNTIKELKEKgWSYTIKASMLEIYNETIRDLLapgNAPQKKLEIRHD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 160 K-NRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEK 238
Cdd:cd01366 160 SeKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGSER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 239 VSKTGAEGAVLDEAKNINKSLSALGNVISALAEGtKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTL 318
Cdd:cd01366 240 LNKSGATGDRLKETQAINKSLSALGDVISALRQK-QSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSL 318
|
330
....*....|.
gi 4758650 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 |
2.63e-101 |
|
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: 321.22 E-value: 2.63e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 8 SIKVMCRFRPLNEAEILRGDKFIPKFKGDETVVI-------------GQGKPYVFDRVL-------PPNTTQEQVYNACA 67
Cdd:cd01365 2 NVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKnpkqadknnkatrEVPKSFSFDYSYwshdsedPNYASQEQVYEDLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 68 KQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGklhDPQLMGIIPRIAHDIFDHIYSM-DENLEFHIKVSYFEIYLDKIRDL 146
Cdd:cd01365 82 EELLQHAFEGYNVCLFAYGQTGSGKSYTMMG---TQEQPGIIPRLCEDLFSRIADTtNQNMSYSVEVSYMEIYNEKVRDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 147 LDVS----KTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEK 222
Cdd:cd01365 159 LNPKpkknKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAET 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 223 KLSG----KLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE-------GTKTHVPYRDSKMTRILQDS 291
Cdd:cd01365 239 NLTTekvsKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADmssgkskKKSSFIPYRDSVLTWLLKEN 318
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 4758650 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 |
2.66e-100 |
|
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: 317.75 E-value: 2.66e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 8 SIKVMCRFRPLNEAEILRGDK------------FIPKFKGDETVVIGQG-----------KPYVFDRVLPPNTTQEQVYN 64
Cdd:cd01370 1 SLTVAVRVRPFSEKEKNEGFRrivkvmdnhmlvFDPKDEEDGFFHGGSNnrdrrkrrnkeLKYVFDRVFDETSTQEEVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 65 ACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPqlmGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIR 144
Cdd:cd01370 81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEP---GLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 145 DLLDVSKTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQEN---VETE 221
Cdd:cd01370 158 DLLNPSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDktaSINQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 222 KKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTK--THVPYRDSKMTRILQDSLGGNCRTT 299
Cdd:cd01370 238 QVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKknKHIPYRDSKLTRLLKDSLGGNCRTV 317
|
330 340
....*....|....*....|....*...
gi 4758650 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 |
2.79e-96 |
|
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: 307.33 E-value: 2.79e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 6 ECSIKVMCRFRPLNEAEILRGDKFIPKFKGD-ETVVIGQG--------KPYVFDRVLPPNTTQEQVYNACAKQIVKDVLE 76
Cdd:cd01364 1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVrKEVSVRTGgladksstKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 77 GYNGTIFAYGQTSSGKTHTMEGK--------LHDPQLMGIIPRIAHDIFDHIYSMDEnlEFHIKVSYFEIYLDKIRDLLD 148
Cdd:cd01364 81 GYNCTIFAYGQTGTGKTYTMEGDrspneeytWELDPLAGIIPRTLHQLFEKLEDNGT--EYSVKVSYLEIYNEELFDLLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 149 VS---KTNLAVHEDKNRVP--YVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLI--NIKQENVETE 221
Cdd:cd01364 159 PSsdvSERLRMFDDPRNKRgvIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSItiHIKETTIDGE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 222 KKLS-GKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKtHVPYRDSKMTRILQDSLGGNCRTTI 300
Cdd:cd01364 239 ELVKiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAP-HVPYRESKLTRLLQDSLGGRTKTSI 317
|
330 340 350
....*....|....*....|....*....|....
gi 4758650 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 |
3.26e-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: 285.56 E-value: 3.26e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 9 IKVMCRFRPLNEAEILRGDKFIPKFKGDETVVIGQGKP--YVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAYG 86
Cdd:cd01373 3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKPPktFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 87 QTSSGKTHTMEGKLHDP-----QLMGIIPRIAHDIFDHI----YSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVH 157
Cdd:cd01373 83 QTGSGKTYTMWGPSESDnesphGLRGVIPRIFEYLFSLIqrekEKAGEGKSFLCKCSFLEIYNEQIYDLLDPASRNLKLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 158 EDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIkqENVETEKKLS----GKLYLVDL 233
Cdd:cd01373 163 EDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTI--ESWEKKACFVnirtSRLNLVDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 234 AGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE---GTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFN 310
Cdd:cd01373 241 AGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvahGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSKC 320
|
330 340
....*....|....*....|....
gi 4758650 311 EAETKSTLMFGQRAKTIKNTVSVN 334
Cdd:cd01373 321 FGETLSTLRFAQRAKLIKNKAVVN 344
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
47-334 |
8.03e-85 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 283.94 E-value: 8.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 47 YVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPqlmGIIPRIAHDIFDHIYSMDEN 126
Cdd:COG5059 58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEP---GIIPLSLKELFSKLEDLSMT 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 127 LEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSH 206
Cdd:COG5059 135 KDFAVSISYLEIYNEKIYDLLSPNEESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSH 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 207 SIFLINIKQENVETEKKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKT-HVPYRDSKMT 285
Cdd:COG5059 215 SIFQIELASKNKVSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSgHIPYRESKLT 294
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 4758650 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 |
1.45e-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: 256.94 E-value: 1.45e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 9 IKVMCRFRPLNEAEILRGDKFIPKFKGDETVVI-------------GQGKP---YVFDRVLPPNTTQEQVYNACAKQIVK 72
Cdd:cd01368 3 VKVYLRVRPLSKDELESEDEGCIEVINSTTVVLhppkgsaankserNGGQKetkFSFSKVFGPNTTQKEFFQGTALPLVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 73 DVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPqlmGIIPRIAHDIFDHIYsmdenlEFHIKVSYFEIYLDKIRDLLDVS-- 150
Cdd:cd01368 83 DLLHGKNGLLFTYGVTNSGKTYTMQGSPGDG---GILPRSLDVIFNSIG------GYSVFVSYIEIYNEYIYDLLEPSps 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 151 -----KTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLS 225
Cdd:cd01368 154 sptkkRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDGDVD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 226 --------GKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE----GTKTHVPYRDSKMTRILQDSLG 293
Cdd:cd01368 234 qdkdqitvSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLREnqlqGTNKMVPFRDSKLTHLFQNYFD 313
|
330 340 350
....*....|....*....|....*....|..
gi 4758650 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 |
1.46e-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: 248.26 E-value: 1.46e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 49 FDRVLPpNTTQEQVYNACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIySMDENLE 128
Cdd:cd01375 52 FDGVLH-NASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENYKHRGIIPRALQQVFRMI-EERPTKA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 129 FHIKVSYFEIYLDKIRDLLDV------SKTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHS 202
Cdd:cd01375 130 YTVHVSYLEIYNEQLYDLLSTlpyvgpSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 203 SRSHSIFLINIKQENVE--TEKKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYR 280
Cdd:cd01375 210 SRSHCIFTIHLEAHSRTlsSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDRTHVPFR 289
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 4758650 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 |
4.85e-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: 238.17 E-value: 4.85e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 9 IKVMCRFRPLNEAEILRGDKFIPKFKGDETVVI------GQGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTI 82
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVELadprnhGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNATV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 83 FAYGQTSSGKTHTMEGklhDPQLMGIIPRIAHDIFDHIYSMDENLEFhiKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNR 162
Cdd:cd01376 82 FAYGSTGAGKTFTMLG---SPEQPGLMPLTVMDLLQMTRKEAWALSF--TMSYLEIYQEKILDLLEPASKELVIREDKDG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 163 VPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLIN-IKQENVETEKKLSGKLYLVDLAGSEKVSK 241
Cdd:cd01376 157 NILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKvDQRERLAPFRQRTGKLNLIDLAGSEDNRR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 242 TGAEGAVLDEAKNINKSLSALGNVISALAEGTKtHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFG 321
Cdd:cd01376 237 TGNEGIRLKESGAINSSLFVLSKVVNALNKNLP-RIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFA 315
|
....
gi 4758650 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 |
9.49e-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: 234.88 E-value: 9.49e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 9 IKVMCRFRPLNEAEILRGDKFIPKFKGDETVVIGQGK------------PYVFDRVLPPNTTQEQVYNACAKQIVKDVLE 76
Cdd:cd01367 2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHEPKlkvdltkyienhTFRFDYVFDESSSNETVYRSTVKPLVPHIFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 77 GYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIA-HDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDvSKTNLA 155
Cdd:cd01367 82 GGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALAaRDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLLN-RKKRVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 156 VHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENvetEKKLSGKLYLVDLAG 235
Cdd:cd01367 161 LREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRG---TNKLHGKLSFVDLAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 236 SEKVSKTGAEGA-VLDEAKNINKSLSALGNVISALAEGtKTHVPYRDSKMTRILQDSL-GGNCRTTIVICCSPSVFNEAE 313
Cdd:cd01367 238 SERGADTSSADRqTRMEGAEINKSLLALKECIRALGQN-KAHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEH 316
|
330
....*....|..
gi 4758650 314 TKSTLMFGQRAK 325
Cdd:cd01367 317 TLNTLRYADRVK 328
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
5-337 |
1.34e-62 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 231.75 E-value: 1.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 5 AECSIKVMCRFRPLNEAEilRGDKFIPKFKGDETVVIGQgkPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFA 84
Cdd:PLN03188 96 SDSGVKVIVRMKPLNKGE--EGEMIVQKMSNDSLTINGQ--TFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 85 YGQTSSGKTHTMEGK---LHDPQL----MGIIPRIAHDIFDHIYS-----MDENLEFHIKVSYFEIYLDKIRDLLDVSKT 152
Cdd:PLN03188 172 YGQTGSGKTYTMWGPangLLEEHLsgdqQGLTPRVFERLFARINEeqikhADRQLKYQCRCSFLEIYNEQITDLLDPSQK 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 153 NLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSG----KL 228
Cdd:PLN03188 252 NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVADGLSSfktsRI 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 229 YLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE----GTKTHVPYRDSKMTRILQDSLGGNCRTTIVICC 304
Cdd:PLN03188 332 NLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAI 411
|
330 340 350
....*....|....*....|....*....|...
gi 4758650 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 |
2.48e-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: 160.59 E-value: 2.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 11 VMCRFRPLNEAEILRGDKFIpkfkgdetvvigqgkpyVFDRVLPPNTTQEQVYNACAKqIVKDVLEGYNG-TIFAYGQTS 89
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKII-----------------VFYRGFRRSESQPHVFAIADP-AYQSMLDGYNNqSIFAYGESG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 90 SGKTHTMegklhdpqlMGIIPRIAHDIFDHIYSMDENLEFHikvsyfeiyldkirdlldvsktnlavhedknrvpyvkgC 169
Cdd:cd01363 63 AGKTETM---------KGVIPYLASVAFNGINKGETEGWVY--------------------------------------L 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 170 TERFVSSPEEVMDVIDEGKANRhVAVTNMNEHSSRSHSIFLInikqenvetekklsgklyLVDLAGSEkvsktgaegavl 249
Cdd:cd01363 96 TEITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------------LLDIAGFE------------ 144
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 4758650 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 ... |
836-905 |
1.25e-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: 1.25e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 836 FLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIK 905
Cdd:cd23649 1 FLERNLEQLTLVQKQLVRQNSTLKKELALAEKKLAARNERIKSLEALLKEAQEKLEKQNQKFEEQLQRLR 70
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
7-147 |
1.23e-21 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 91.90 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 7 CSIKVMCRFRP--LNEAEILRGDKFIpkfkgDETVVIGQGKPYVFDRVLPPNTTQEQVYNACaKQIVKDVLEGYNGTIFA 84
Cdd:pfam16796 20 GNIRVFARVRPelLSEAQIDYPDETS-----SDGKIGSKNKSFSFDRVFPPESEQEDVFQEI-SQLVQSCLDGYNVCIFA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4758650 85 YGQTSSGKTHTMegklhdpqlmgiIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLL 147
Cdd:pfam16796 94 YGQTGSGSNDGM------------IPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQDLL 144
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
412-907 |
2.66e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.33 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQ----------------I 475
Cdd:PRK03918 217 PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvkelkelkekaeeyI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 476 ENEAAKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQElsnhqKKRATEILNLLL 555
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-----RHELYEEAKAKK 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 556 KDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMdsnrKMNASERELAACQLLISQ 635
Cdd:PRK03918 372 EELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE----ELKKAKGKCPVCGRELTE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 636 HE---------AKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQ 706
Cdd:PRK03918 448 EHrkelleeytAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEY 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 707 MESHREAH--QKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLkiedqeremklekllllndkREQAREDL 784
Cdd:PRK03918 528 EKLKEKLIklKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL--------------------EELGFESV 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 785 KGLEETVsRELQTLHN--LRKLFVQDLTTRVKKSVELDNDDgggSAAQKQKISFLENNLEQLTKVHKQLVR-----DNAD 857
Cdd:PRK03918 588 EELEERL-KELEPFYNeyLELKDAEKELEREEKELKKLEEE---LDKAFEELAETEKRLEELRKELEELEKkyseeEYEE 663
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 4758650 858 LRCELPKLEKRLRATAERVKALESALKEAKENA------MRDRKRYQQEVDRIKEA 907
Cdd:PRK03918 664 LREEYLELSRELAGLRAELEELEKRREEIKKTLeklkeeLEEREKAKKELEKLEKA 719
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
617-924 |
1.33e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 617 RKMNASERELAACQLLISQHEAKIKSLtdymqnmEQKRRQLEESQDsLSEELAKLRAQEKMHEVSFQDKEKEHL------ 690
Cdd:COG1196 179 RKLEATEENLERLEDILGELERQLEPL-------ERQAEKAERYRE-LKEELKELEAELLLLKLRELEAELEELeaelee 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 691 --TRLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLE 768
Cdd:COG1196 251 leAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 769 KLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDNDDGGGSAAQKQKISfLENNLEQLTKVH 848
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE-LAAQLEELEEAE 409
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758650 849 KQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIAK 924
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
437-756 |
2.75e-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: 67.77 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 437 QQSQLAEKLKQQMLDQDEL--------LASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNYDQKSQEVEDK 508
Cdd:TIGR02168 207 RQAEKAERYKELKAELRELelallvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 509 TRANEQLTDELAQKTTTLTTTQRELSQLQElsnhQKKRATEILNLLLKDLGEiggiigtnDVKTLADVngviEEEFTMAR 588
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRERLANLER----QLEELEAQLEELESKLDE--------LAEELAEL----EEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 589 LYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEEL 668
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 669 AKLRAQEKMHEVSFQDKEKEHLtrlqdaeemkkaleqqmESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEK 748
Cdd:TIGR02168 431 EEAELKELQAELEELEEELEEL-----------------QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
....*...
gi 4758650 749 LSSDYNKL 756
Cdd:TIGR02168 494 LERLQENL 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
428-750 |
1.14e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 428 LDDKDDEINQQsqlAEKLKQQmldqdellASTRRDYEKIQEELTRLQIEneaakdevkEVLQALEELAVNYDQKSQEVED 507
Cdd:COG1196 191 LEDILGELERQ---LEPLERQ--------AEKAERYRELKEELKELEAE---------LLLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 508 KTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRateiLNLLLKDLGEIGGIIG---------TNDVKTLADVNG 578
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAE----EYELLAELARLEQDIArleerrrelEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 579 VIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLE 658
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 659 ESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEEKQKIIDEIRDL 738
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
330
....*....|..
gi 4758650 739 NQKLQLEQEKLS 750
Cdd:COG1196 487 AEAAARLLLLLE 498
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
593-907 |
1.94e-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: 65.09 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 593 KMKSEVKSLVNRSKQLEsaqmdsnRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAkLR 672
Cdd:TIGR02169 220 KREYEGYELLKEKEALE-------RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-LR 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 673 AQEKMHEV-----SFQDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQE 747
Cdd:TIGR02169 292 VKEKIGELeaeiaSLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 748 KLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRklfvQDLTTRVKKSVELDNDdgggS 827
Cdd:TIGR02169 372 ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKINELEEE----K 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 828 AAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRAtaervKALESALKEAKENAMRDRKRYQQEVDRIKEA 907
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK-----LQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
412-798 |
2.30e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQAL 491
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 492 EELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTT-TQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTN-- 568
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEaAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLig 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 569 ---------DVKTLADVNGVIEEEFTMARLYISKMKSEVKSLV-----NRSKQLESAQMDSNRKMNASERELAACQL--- 631
Cdd:COG1196 532 veaayeaalEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtflplDKIRARAALAAALARGAIGAAVDLVASDLrea 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 632 -----LISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMhevsFQDKEKEHLTRLQDAEEMKKALEQQ 706
Cdd:COG1196 612 daryyVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSL----TGGSRRELLAALLEAEAELEELAER 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 707 MESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKG 786
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
410
....*....|..
gi 4758650 787 LEETVSRELQTL 798
Cdd:COG1196 768 ELERLEREIEAL 779
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
411-752 |
3.94e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 411 TEEKEKYDEEISSLYRQLDDKDDEINQQSQL--AEKLKQQMLDQDELLASTRRDYEKIQ---EELTRLQIENEAAKDEVK 485
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEerlEELRELEEELEELEAELA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 486 EVLQALEELAVNYD-QKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQE--------LSNHQKKRATEILNLLLK 556
Cdd:COG4717 174 ELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEeleqleneLEAAALEERLKEARLLLL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 557 DLGEIGGIIGTNDV--KTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLIS 634
Cdd:COG4717 254 IAAALLALLGLGGSllSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 635 QHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEK-----EHLTRLQDAEEMKKALEQQMES 709
Cdd:COG4717 334 LSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEElraalEQAEEYQELKEELEELEEQLEE 413
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 4758650 710 H------------REAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSD 752
Cdd:COG4717 414 LlgeleellealdEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
398-792 |
7.80e-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: 7.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 398 IIDNIApvvaGIST--EEKEKYDEEIsslyrqlddkdDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQi 475
Cdd:TIGR02169 158 IIDEIA----GVAEfdRKKEKALEEL-----------EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKR- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 476 eneaaKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLqelsNHQKKRATEILNLLL 555
Cdd:TIGR02169 222 -----EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL----NKKIKDLGEEEQLRV 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 556 KdlgeiggiigtndvKTLADVNGVIEEeftmARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQ 635
Cdd:TIGR02169 293 K--------------EKIGELEAEIAS----LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 636 HEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRaqEKMHEVsfQDKEKEHLTRLQDAEEMKKALEQQMESHREAHQ 715
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR--EKLEKL--KREINELKRELDRLQEELQRLSEELADLNAAIA 430
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4758650 716 KQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSdynklkiEDQEREMKLEKLLLLNDKREQAREDLKGLEETVS 792
Cdd:TIGR02169 431 GIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK-------YEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
409-730 |
8.66e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 8.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 409 ISTEEKEKYDEEISSLYRQLDDKDDEINQQSQLAEklkqqmldqdELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVL 488
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELE----------AELEELEAELAELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 489 QALEELAvnyDQKSQEVEDKTRANEQLTDELAQKtttltttQRELSQLQELSNHQKKRATEILNLllkdlgeiggiigtn 568
Cdd:COG1196 288 AEEYELL---AELARLEQDIARLEERRRELEERL-------EELEEELAELEEELEELEEELEEL--------------- 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 569 dvktladvngviEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQ 648
Cdd:COG1196 343 ------------EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 649 NMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEEK 728
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
..
gi 4758650 729 QK 730
Cdd:COG1196 491 AR 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
580-917 |
1.18e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 580 IEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEE 659
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 660 SQDSLSEELAKLRAQEKMHEvsfqDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEEKQKIIDEIRDLN 739
Cdd:COG1196 317 RLEELEEELAELEEELEELE----EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 740 QKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRV--KKSV 817
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAelLEEA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 818 ELDNDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRD--NADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRK 895
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvkAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIV 552
|
330 340
....*....|....*....|..
gi 4758650 896 RYQQEVDRIKEAVRAKNMARRA 917
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRA 574
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
591-904 |
1.43e-09 |
|
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: 62.38 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 591 ISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAK 670
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 671 LRAQEKmhevSFQDKEKEHLTRLQDAEEMKKALEQQMEshreAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLS 750
Cdd:TIGR02168 759 LEAEIE----ELEERLEEAEEELAEAEAEIEELEAQIE----QLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 751 SDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDNDDGGGSaaq 830
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE--- 907
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4758650 831 kQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRA----TAERVKALESALKEAKENAMRDRKRYQQEVDRI 904
Cdd:TIGR02168 908 -SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeyslTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
648-924 |
1.63e-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: 62.01 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 648 QNMEQKRRQLEESQDSLSEELAKLRAQekmhevsFQDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEE 727
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEE-------ISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 728 KQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQ 807
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 808 DLTTRVKKSVELdnddgggsaaqKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAK 887
Cdd:TIGR02169 386 ELKDYREKLEKL-----------KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE 454
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 4758650 888 ENAMR---DRKRYQQEVDRIKEAVRAKNMARRAHSAQIAK 924
Cdd:TIGR02169 455 WKLEQlaaDLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
591-796 |
1.84e-09 |
|
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: 60.55 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 591 ISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAK 670
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 671 -LRAQEKMHEVSF------QDKEKEHLTRLQDAEEMKKALEQQMESHReAHQKQLSRLRDEIEEKQKiidEIRDLNQKLQ 743
Cdd:COG4942 109 lLRALYRLGRQPPlalllsPEDFLDAVRRLQYLKYLAPARREQAEELR-ADLAELAALRAELEAERA---ELEALLAELE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 4758650 744 LEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQ 796
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
412-757 |
1.85e-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: 62.01 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQieneaakdevkevlQAL 491
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK--------------ERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 492 EELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQL-QELSNHQKKRATEILNLLLKDLGEIGGIIGTNDV 570
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 571 KTladvnGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNM 650
Cdd:TIGR02169 820 KL-----NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 651 EQKRRQLEESQDSLSEELAKLRA-----QEKMHEVSFQDKEKEHLTR-----------LQDAEEMKKALEQQMESHREAH 714
Cdd:TIGR02169 895 EAQLRELERKIEELEAQIEKKRKrlselKAKLEALEEELSEIEDPKGedeeipeeelsLEDVQAELQRVEEEIRALEPVN 974
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 4758650 715 QKQLsrlrDEIEEKQKIIDEIRDLNQKLQLEQE---KLSSDYNKLK 757
Cdd:TIGR02169 975 MLAI----QEYEEVLKRLDELKEKRAKLEEERKailERIEEYEKKK 1016
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
595-807 |
2.29e-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: 61.29 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 595 KSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQ 674
Cdd:pfam17380 367 QEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 675 EkMHEVSFQDKEKEH---LTRLQDAEEMKKALEQQMESHREAHQKQLSR--LRDEIEE-KQKIIDEIRD---LNQKLQLE 745
Cdd:pfam17380 447 E-MERVRLEEQERQQqveRLRQQEEERKRKKLELEKEKRDRKRAEEQRRkiLEKELEErKQAMIEEERKrklLEKEMEER 525
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4758650 746 QEKLSSDYNKLKIEDQEREMKLEkllllnDKREQAREDLKGLEETVSReLQTLHNLRKLFVQ 807
Cdd:pfam17380 526 QKAIYEEERRREAEEERRKQQEM------EERRRIQEQMRKATEERSR-LEAMEREREMMRQ 580
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
412-802 |
3.17e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQ--QMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQ 489
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 490 ALEELAVNYDQ------------------KSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQE--------LSNHQ 543
Cdd:COG4717 161 LEEELEELEAElaelqeeleelleqlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEeleqleneLEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 544 KKRATEILNLLLKDLGEIGGIIGTNDV--KTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNA 621
Cdd:COG4717 241 LEERLKEARLLLLIAAALLALLGLGGSllSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 622 SERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEK-----EHLTRLQDA 696
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEElraalEQAEEYQEL 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 697 EEMKKALEQQMESH-----REAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLL 771
Cdd:COG4717 401 KEELEELEEQLEELlgeleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEE 480
|
410 420 430
....*....|....*....|....*....|...
gi 4758650 772 LLNDKREQARED--LKGLEETVSRELQTLHNLR 802
Cdd:COG4717 481 LKAELRELAEEWaaLKLALELLEEAREEYREER 513
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
426-922 |
2.25e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 426 RQLDDKDDEINQ-QSQLAEKLKQqmlDQDELLASTRRDYEKIQEELTRLQIENEAA---KDEVKEVLQAleelavnYDQK 501
Cdd:PRK02224 180 RVLSDQRGSLDQlKAQIEEKEEK---DLHERLNGLESELAELDEEIERYEEQREQAretRDEADEVLEE-------HEER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 502 SQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTNDvkTLADVNGVIE 581
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE--ELEDRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 582 EEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQK-------R 654
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 655 RQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKehltRLQDAEEMKKA-----LEQQMEShreahqkqlSRLRDEIEEKQ 729
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRTARE----RVEEAEALLEAgkcpeCGQPVEG---------SPHVETIEEDR 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 730 KIIDEIRDLNQKLQLEQEKLSSDYNKLKiedqEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLfVQDL 809
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERAE----DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER-AAEL 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 810 TT--RVKKSVELDNDDGGGSAAQK-----QKISFLENNLEQLTKVHKQLVrDNADLRCELPKL-EKR------------- 868
Cdd:PRK02224 550 EAeaEEKREAAAEAEEEAEEAREEvaelnSKLAELKERIESLERIRTLLA-AIADAEDEIERLrEKRealaelnderrer 628
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 4758650 869 LRATAERVKALESALKEAK-ENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQI 922
Cdd:PRK02224 629 LAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEI 683
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
411-910 |
2.54e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 411 TEEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQA 490
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 491 LEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILnlllkdlgeiggiigtNDV 570
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE----------------EEL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 571 KTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNM 650
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 651 EQ-----KRRQLEESQDSLSEELAKLRAQEKMHE--------VSFQDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQ 717
Cdd:COG1196 504 EGflegvKAALLLAGLRGLAGAVAVLIGVEAAYEaaleaalaAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIR 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 718 LSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQARE---DLKGLEETVSRE 794
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREvtlEGEGGSAGGSLT 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 795 LQTLHNLRKLFVQDLTTRVKKSVELDNDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAE 874
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
490 500 510
....*....|....*....|....*....|....*.
gi 4758650 875 RVKALESALKEAKENAMrDRKRYQQEVDRIKEAVRA 910
Cdd:COG1196 744 EEELLEEEALEELPEPP-DLEELERELERLEREIEA 778
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
412-904 |
5.98e-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: 56.90 E-value: 5.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 412 EEKEKYDEEISSLYRQLDDKDDEinQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVlqAL 491
Cdd:TIGR00618 386 QQKTTLTQKLQSLCKELDILQRE--QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKI--HL 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 492 EELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTNDVK 571
Cdd:TIGR00618 462 QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLE 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 572 T-LADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNR------------KMNASERELAAC----QLLIS 634
Cdd:TIGR00618 542 TsEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNlqnitvrlqdltEKLSEAEDMLACeqhaLLRKL 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 635 QHEAKIKSLTDYMQNMEQK---------RRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQ 705
Cdd:TIGR00618 622 QPEQDLQDVRLHLQQCSQElalkltalhALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ 701
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 706 QMESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLssdyNKLKIEDQEREMKLEKLLLLNDKREQAREDLK 785
Cdd:TIGR00618 702 CQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSL----KELMHQARTVLKARTEAHFNNNEEVTAALQTG 777
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 786 GLEETVSRELQTLHNLRKLFVQDL-TTRVKKSVELDNDDGGGSAAQKQKISFLENNLEQLTKVHKQLVrdnaDLRCELPK 864
Cdd:TIGR00618 778 AELSHLAAEIQFFNRLREEDTHLLkTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLG----EITHQLLK 853
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 4758650 865 LEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRI 904
Cdd:TIGR00618 854 YEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDAL 893
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
579-886 |
1.39e-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: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 579 VIEEEFTMARLYISKMKSEVKslvnrskQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLE 658
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIE-------ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 659 ESQDSLSEELAKLRAQEKmhevSFQDKEKEHLTRLQDAEEMKKALEQQMESHREA---HQKQLSRLRDEIEEKQKIIDEI 735
Cdd:TIGR02168 337 EELAELEEKLEELKEELE----SLEAELEELEAELEELESRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLERL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 736 RDLNQKLQLEQEKLSSDYNKLKIEDQEREMklekllllnDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKK 815
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEEAELKELQAEL---------EELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4758650 816 SVELdnddgggsAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEA 886
Cdd:TIGR02168 484 LAQL--------QARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGR 546
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
440-740 |
2.08e-07 |
|
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: 55.34 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 440 QLAEKLKQQMLDQDEL---LASTRRDYEKIQEELTRLQIENEAAKDEVKE-------VLQALEEL---AVNYDQKSQEVE 506
Cdd:COG3096 344 RQQEKIERYQEDLEELterLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSlksqladYQQALDVQqtrAIQYQQAVQALE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 507 DKTR-------ANEQLTDELAQ---KTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEI----GGIIGTNDVKT 572
Cdd:COG3096 424 KARAlcglpdlTPENAEDYLAAfraKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVersqAWQTARELLRR 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 573 LADVNGVIEEEFTMARLYiskmkSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQ 652
Cdd:COG3096 504 YRSQQALAQRLQQLRAQL-----AELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVE 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 653 KRRQLEESQDSLSEELAKLRAQE----KMHEVSFQDKEKEHLTrLQDAEEMKKALEQQMESHREAhqkqlSRLRDEIEE- 727
Cdd:COG3096 579 QRSELRQQLEQLRARIKELAARApawlAAQDALERLREQSGEA-LADSQEVTAAMQQLLEREREA-----TVERDELAAr 652
|
330
....*....|...
gi 4758650 728 KQKIIDEIRDLNQ 740
Cdd:COG3096 653 KQALESQIERLSQ 665
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
622-906 |
2.25e-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: 54.74 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 622 SERELAACQLLISQHEAKI--KSLTDYMQNMEQ---------------KRRQLEESQDSLSEELAKLRAQEKMHEVSFQD 684
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVseRQQQEKFEKMEQerlrqekeekareveRRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 685 KEKEhLTRLQdAEEMKKALEQ--------QMESHREAHQKQLSR------LRDEIE--EKQKIIDEIRD---LNQKLQLE 745
Cdd:pfam17380 346 RERE-LERIR-QEERKRELERirqeeiamEISRMRELERLQMERqqknerVRQELEaaRKVKILEEERQrkiQQQKVEME 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 746 Q---EKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKgleetvsrelqtlhnlrklfvQDLTTRVKKSVELDND 822
Cdd:pfam17380 424 QiraEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLR---------------------QQEEERKRKKLELEKE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 823 DGGGSAAQKQKISFLENNLEQltkvHKQLVRDNADLRCELPK-LEKRLRATAERVKALESALKEAKENAMRDRKRYQQEV 901
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEE----RKQAMIEEERKRKLLEKeMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQM 558
|
....*
gi 4758650 902 DRIKE 906
Cdd:pfam17380 559 RKATE 563
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
452-676 |
2.82e-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: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 452 QDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELavnydqkSQEVEDKTRANEQLTDELAQKTTTLTTTQR 531
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-------ERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 532 ELSQLQELSNHQKKRATEILNLLLK--DLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLE 609
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4758650 610 SAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEK 676
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
412-863 |
3.01e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 412 EEKEKYDEeissLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQAL 491
Cdd:PTZ00121 1441 EEAKKADE----AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 492 EELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQrELSQLQELSN-HQKKRATEILNLLLKDLGEIGGIigtnDV 570
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKaEEAKKAEEDKNMALRKAEEAKKA----EE 1591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 571 KTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNM 650
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 651 EQKRRQLE----ESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTR---LQDAEEMKKALEQQMESHREAHQKQLSRLRD 723
Cdd:PTZ00121 1672 EDKKKAEEakkaEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 724 EIEEKQKIIDEIRDLNQKL-QLEQEKLSSDYNKLKIEDQEREMKLEKLLLL-----------NDKREQAREDLKGLEETV 791
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEEKKAeEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDifdnfaniiegGKEGNLVINDSKEMEDSA 1831
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758650 792 SRELQTLHNLR----KLFVQDLTTRVKKSVELDNDDGGGSAAQKQKISFLENNLEqlTKVHKQLvrDNADLRCELP 863
Cdd:PTZ00121 1832 IKEVADSKNMQleeaDAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEE--ADEIEKI--DKDDIEREIP 1903
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
411-907 |
3.65e-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: 54.29 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 411 TEEKEKYDEEISSLYRQLDDKDDEInqqsqlaEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQA 490
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQL-------EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 491 LEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQL-QELSNHQKKRATEILNLLLKDLGEIGGIIgTND 569
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqQEIEELLKKLEEAELKELQAELEELEEEL-EEL 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 570 VKTLADVNG---VIEEEFTMARLYISKMKSEVKSLVNRSKQLES-------------AQMDSNRKMN------------A 621
Cdd:TIGR02168 453 QEELERLEEaleELREELEEAEQALDAAERELAQLQARLDSLERlqenlegfsegvkALLKNQSGLSgilgvlselisvD 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 622 SERELA-------ACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLT--- 691
Cdd:TIGR02168 533 EGYEAAieaalggRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKfdp 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 692 -----------------RLQDAEEMKKALEQQME-----------------SHREAHQKQLSRlRDEIEEKQKIIDEIRD 737
Cdd:TIGR02168 613 klrkalsyllggvlvvdDLDNALELAKKLRPGYRivtldgdlvrpggvitgGSAKTNSSILER-RREIEELEEKIEELEE 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 738 LNQKLQLEQEKLSSDYNKLKiedQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLrklfvQDLTTRVKKSV 817
Cdd:TIGR02168 692 KIAELEKALAELRKELEELE---EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL-----SKELTELEAEI 763
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 818 ELDNDDGGGSAAQKQKisfLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRY 897
Cdd:TIGR02168 764 EELEERLEEAEEELAE---AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
570
....*....|
gi 4758650 898 QQEVDRIKEA 907
Cdd:TIGR02168 841 EDLEEQIEEL 850
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
412-911 |
7.97e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 7.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQAL 491
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 492 E--ELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQElsnhQKKRATEilnllLKDLGEiggiigtnD 569
Cdd:PTZ00121 1367 EaaEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA----AKKKADE-----AKKKAE--------E 1429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 570 VKTLADVNGVIEEEFTMARLyiSKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAAcQLLISQHEAKIKSltDYMQN 649
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEA--KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD-EAKKKAEEAKKKA--DEAKK 1504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 650 MEQKRRQLEESQDS----LSEELAKLRAQEKMHEV--SFQDKEKEHLTR---LQDAEEMKKALEQQMESHREAHQKQLSR 720
Cdd:PTZ00121 1505 AAEAKKKADEAKKAeeakKADEAKKAEEAKKADEAkkAEEKKKADELKKaeeLKKAEEKKKAEEAKKAEEDKNMALRKAE 1584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 721 LRDEIEEKQkiideirdlnqklQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHN 800
Cdd:PTZ00121 1585 EAKKAEEAR-------------IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE 1651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 801 LRKlfvQDLTTRVKKSVELDNDDgggsaAQKQKISFLENNLEQLTKVHKQLVRDNADLRcelpKLEKRLRATAERVKALE 880
Cdd:PTZ00121 1652 LKK---AEEENKIKAAEEAKKAE-----EDKKKAEEAKKAEEDEKKAAEALKKEAEEAK----KAEELKKKEAEEKKKAE 1719
|
490 500 510
....*....|....*....|....*....|.
gi 4758650 881 SALKEAKENAMRDRKRYQQEVDRIKEAVRAK 911
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
412-894 |
8.33e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 8.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDellastRRDYEKIQEELTRLQIENEAAKDEVKEVLQAL 491
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG------GDRLEQLEREIERLERELEERERRRARLEALL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 492 -----------EELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRAT-------EILNL 553
Cdd:COG4913 369 aalglplpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSniparllALRDA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 554 LLKDLGE------------------------IGGIIGTN------DVKTLADVNGVIEEEFTMARLYISKMKSEVK---- 599
Cdd:COG4913 449 LAEALGLdeaelpfvgelievrpeeerwrgaIERVLGGFaltllvPPEHYAAALRWVNRLHLRGRLVYERVRTGLPdper 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 600 ------SLVNR-----SKQLESAQMDSNRKMN----ASEREL--------AACQL--------------LISQH------ 636
Cdd:COG4913 529 prldpdSLAGKldfkpHPFRAWLEAELGRRFDyvcvDSPEELrrhpraitRAGQVkgngtrhekddrrrIRSRYvlgfdn 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 637 EAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQ----EKMHEVSFQDKE-KEHLTRLQDAEEMKKALE------Q 705
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERrealQRLAEYSWDEIDvASAEREIAELEAELERLDassddlA 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 706 QMESHREAHQKQLSRLRDEIEEKQKII----DEIRDLNQKLQLEQEKLSSDYNKLKIED----QEREMKLEKLLLLNDKR 777
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIgrleKELEQAEEELDELQDRLEAAEDLARLELrallEERFAAALGDAVERELR 768
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 778 EQAREDLKGLEETVSRELQTLHNLRKLFVQDLTtrvkksveLDNDDGGGSAAqkqkisflenNLEQLTKVHKQLVRDNad 857
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAMRAFNREWP--------AETADLDADLE----------SLPEYLALLDRLEEDG-- 828
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 4758650 858 lrceLPKLEKRLR-----ATAERVKALESALKEAKENAmRDR 894
Cdd:COG4913 829 ----LPEYEERFKellneNSIEFVADLLSKLRRAIREI-KER 865
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
412-896 |
1.09e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMldqdellastrrdyEKIQEELTRLQIENEAAKDEVKEVLQAL 491
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI--------------AGIEAKINELEEEKEDKALEIKKQEWKL 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 492 EELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHqKKRATEILNlllkdlGEIGGIIGTndVK 571
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG-GRAVEEVLK------ASIQGVHGT--VA 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 572 TLADV-----------------NGVIEEEFTMAR---------------LYISKMKSEVK---------------SLVNR 604
Cdd:TIGR02169 529 QLGSVgeryataievaagnrlnNVVVEDDAVAKEaiellkrrkagratfLPLNKMRDERRdlsilsedgvigfavDLVEF 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 605 SKQLESA------------QMDSNR------KMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSE 666
Cdd:TIGR02169 609 DPKYEPAfkyvfgdtlvveDIEAARrlmgkyRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKR 688
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 667 ELAKLRAqekmhEVSFQDKE-KEHLTRLQDAEEMKKALE---QQMESHREAHQKQLSRLRDEIEEKQKII----DEIRDL 738
Cdd:TIGR02169 689 ELSSLQS-----ELRRIENRlDELSQELSDASRKIGEIEkeiEQLEQEEEKLKERLEELEEDLSSLEQEIenvkSELKEL 763
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 739 NQKLQLEQEKLSSDynKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVS---RELQTLHNLRKLFVQDLTTRVKK 815
Cdd:TIGR02169 764 EARIEELEEDLHKL--EEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLReieQKLNRLTLEKEYLEKEIQELQEQ 841
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 816 SVELDNDdgggSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRK 895
Cdd:TIGR02169 842 RIDLKEQ----IKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
.
gi 4758650 896 R 896
Cdd:TIGR02169 918 R 918
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
412-743 |
1.09e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQ-QMLDQDEL-LASTRRDYEKIQEELTRLqienEAAKDEVKEVLQ 489
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRlAEYSWDEIdVASAEREIAELEAELERL----DASSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 490 ALEELAVNYDQKSQEVEDKTRANEQLTDELAQktttlttTQRELSQLQELSNHQKKRATEILNLLLKDLgeIGGIIGTND 569
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQ-------AEEELDELQDRLEAAEDLARLELRALLEER--FAAALGDAV 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 570 VKTLAdvngvieeeftmarlyiskmksevkslvnrsKQLESAQMDSNRKMNASERELAACqllisqheakiksltdymqn 649
Cdd:COG4913 764 ERELR-------------------------------ENLEERIDALRARLNRAEEELERA-------------------- 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 650 MEQKRRQLEESQDSLSEELAKLRAQEKMHEvsfqDKEKEHLTRLQdaEEMKKALEQQMESHREAHQkqlSRLRDEIEEkq 729
Cdd:COG4913 793 MRAFNREWPAETADLDADLESLPEYLALLD----RLEEDGLPEYE--ERFKELLNENSIEFVADLL---SKLRRAIRE-- 861
|
330
....*....|....
gi 4758650 730 kIIDEIRDLNQKLQ 743
Cdd:COG4913 862 -IKERIDPLNDSLK 874
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
419-858 |
1.25e-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: 52.33 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 419 EEISSLYRQLDDKDDEINQQSQLAEKLKQQMldqdellastrrdyEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNY 498
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQI--------------SQLKKELTNSESENSEKQRELEEKQNEIEKLKKEN 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 499 DQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTNDVKtladvng 578
Cdd:TIGR04523 380 QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK------- 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 579 vieeeftmarlyiskmKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLE 658
Cdd:TIGR04523 453 ----------------ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLT 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 659 ESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQD--AEEMKKALEQQMESHREAHQKQLSrLRDEIEEKQKIID--- 733
Cdd:TIGR04523 517 KKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKS-LKKKQEEKQELIDqke 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 734 -EIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLfVQDLTTR 812
Cdd:TIGR04523 596 kEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKK-IKESKTK 674
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 4758650 813 VKKSVELDND-DGGGSAAQKQKISFL--ENNLEQLTKVHKQLVRDNADL 858
Cdd:TIGR04523 675 IDDIIELMKDwLKELSLHYKKYITRMirIKDLPKLEEKYKEIEKELKKL 723
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
415-894 |
1.48e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 415 EKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEel 494
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ-- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 495 avnydqksqeVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEIlnlllkdlgeiggiigtndvktlA 574
Cdd:COG4717 127 ----------LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL-----------------------A 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 575 DVNGVIEEEFTMARLyisKMKSEVKSLVNRSKQLEsaqmdsnRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKR 654
Cdd:COG4717 174 ELQEELEELLEQLSL---ATEEELQDLAEELEELQ-------QRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 655 RQLEESQ-------------------DSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKkALEQQMESHREAHQ 715
Cdd:COG4717 244 RLKEARLllliaaallallglggsllSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ-ALPALEELEEEELE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 716 KQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKgleetVSREL 795
Cdd:COG4717 323 ELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALE-----QAEEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 796 QTLHNLRKLFVQDLTTRVKKSVELDndDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEK--RLRATA 873
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELL--EALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELL 475
|
490 500
....*....|....*....|.
gi 4758650 874 ERVKALESALKEAKENAMRDR 894
Cdd:COG4717 476 QELEELKAELRELAEEWAALK 496
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
411-911 |
1.98e-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: 52.15 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 411 TEEKEKYDEEISSLYRQLDDKDDEIN-QQSQLAEKLKQQMLDQDELLAS--TRRDYEKIQEELTRLQIENEAAKDEVKEV 487
Cdd:pfam12128 411 AVAEDDLQALESELREQLEAGKLEFNeEEYRLKSRLGELKLRLNQATATpeLLLQLENFDERIERAREEQEAANAEVERL 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 488 LQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQREL-----SQLQELSNHQKKRAT-----------EIL 551
Cdd:pfam12128 491 QSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLlhflrKEAPDWEQSIGKVISpellhrtdldpEVW 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 552 NLLLKDLGEIGGIigTNDVKTLaDVNGVIEEEFTMaRLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQL 631
Cdd:pfam12128 571 DGSVGGELNLYGV--KLDLKRI-DVPEWAASEEEL-RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFART 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 632 LISQHEAKIKSLTDYMQNME-QKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQMESH 710
Cdd:pfam12128 647 ALKNARLDLRRLFDEKQSEKdKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGA 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 711 REAhqkQLSRLRDEIEEKQKIID-EIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEE 789
Cdd:pfam12128 727 LDA---QLALLKAAIAARRSGAKaELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQE 803
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 790 TVSRELQTLhnlrklfVQDLTTRVKKSVELDNDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKL-EKR 868
Cdd:pfam12128 804 TWLQRRPRL-------ATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLaTLK 876
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 4758650 869 LRATAERVKALESALKEAKENAMRDRKR----YQQEVDRIKEAVRAK 911
Cdd:pfam12128 877 EDANSEQAQGSIGERLAQLEDLKLKRDYlsesVKKYVEHFKNVIADH 923
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
415-869 |
2.29e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 415 EKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEEL 494
Cdd:TIGR04523 99 NKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 495 AVNYDQKSQEVED---KTRANEQLTDELAQKTTTLTTTQRELSQLQElsnhQKKRATEILNLLLKDLGEIGGIIGTND-- 569
Cdd:TIGR04523 179 EKEKLNIQKNIDKiknKLLKLELLLSNLKKKIQKNKSLESQISELKK----QNNQLKDNIEKKQQEINEKTTEISNTQtq 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 570 VKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNAS------------ERELAACQLLISQHE 637
Cdd:TIGR04523 255 LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDwnkelkselknqEKKLEEIQNQISQNN 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 638 AKIKSLTDYMQNMEQKRRQLEESQDSLSEELaklraQEKMHEVSFQDKEKE-HLTRLQDAEEMKKALEQQMEshreaHQK 716
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQREL-----EEKQNEIEKLKKENQsYKQEIKNLESQINDLESKIQ-----NQE 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 717 QLSrlrdeiEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQ 796
Cdd:TIGR04523 405 KLN------QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN 478
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758650 797 TLHNLRKLFVQDLTTRVKKSVELDNDDGGGSAAQK---QKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRL 869
Cdd:TIGR04523 479 KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKdltKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL 554
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
452-740 |
2.63e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 452 QDELLASTRRDYEK------IQEELTRLQIENEAAKDEVKE-------VLQALEEL---AVNYDQKSQEVEdktRAN--- 512
Cdd:PRK04863 354 QADLEELEERLEEQnevveeADEQQEENEARAEAAEEEVDElksqladYQQALDVQqtrAIQYQQAVQALE---RAKqlc 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 513 -------EQLTDELAQKTTTLTTTQRELSQL-QELSNHQ--KKRATEILNLLLKdlgeIGGIIGTNDVKTLA-DVNGVIE 581
Cdd:PRK04863 431 glpdltaDNAEDWLEEFQAKEQEATEELLSLeQKLSVAQaaHSQFEQAYQLVRK----IAGEVSRSEAWDVArELLRRLR 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 582 EEFTMA-RLYISKMK-SEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEE 659
Cdd:PRK04863 507 EQRHLAeQLQQLRMRlSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQ 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 660 SQDSLSEELAKLRAQE-KMHEvsFQDKekehLTRLQ----DAEEMKKALEQQMESHREaHQKQLSRLRDEIEEKQKIID- 733
Cdd:PRK04863 587 QLEQLQARIQRLAARApAWLA--AQDA----LARLReqsgEEFEDSQDVTEYMQQLLE-RERELTVERDELAARKQALDe 659
|
....*..
gi 4758650 734 EIRDLNQ 740
Cdd:PRK04863 660 EIERLSQ 666
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
687-923 |
3.27e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 687 KEHLTRLQDA-EEMKKALEQQMeshreaHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREM 765
Cdd:COG4913 231 VEHFDDLERAhEALEDAREQIE------LLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 766 klekllllnDKREQAREDLKGLEETVSRELQTLHNLRklfvqdlttrvkksveldNDDGGgsaaqkQKISFLENNLEQLT 845
Cdd:COG4913 305 ---------ARLEAELERLEARLDALREELDELEAQI------------------RGNGG------DRLEQLEREIERLE 351
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4758650 846 KVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIA 923
Cdd:COG4913 352 RELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
418-762 |
3.60e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.27 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 418 DEEISSLYRQL---DDKDDEINQQSQ-LAEKLKQQMLDQDELL---------------ASTRRDYEKIQeelTRLQIENE 478
Cdd:pfam15921 230 DTEISYLKGRIfpvEDQLEALKSESQnKIELLLQQHQDRIEQLiseheveitgltekaSSARSQANSIQ---SQLEIIQE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 479 AAKDE--------------VKEVLQALEELAVNYDQKSQEVEDK-TRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQ 543
Cdd:pfam15921 307 QARNQnsmymrqlsdlestVSQLRSELREAKRMYEDKIEELEKQlVLANSELTEARTERDQFSQESGNLDDQLQKLLADL 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 544 KKRATEI-----LNLLLKDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYIS----KMKSEVKSLVNRSKQLE----- 609
Cdd:pfam15921 387 HKREKELslekeQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSecqgQMERQMAAIQGKNESLEkvssl 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 610 SAQMDSNRKM-NASERELAACQLLISQHEAKIKSLTDYMQnmeQKRRQLEESqdslSEELAKLRAQE--KMHEVSFQDKE 686
Cdd:pfam15921 467 TAQLESTKEMlRKVVEELTAKKMTLESSERTVSDLTASLQ---EKERAIEAT----NAEITKLRSRVdlKLQELQHLKNE 539
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758650 687 KEHLTRLQDAEEmkkALEQQMESHreahQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQE 762
Cdd:pfam15921 540 GDHLRNVQTECE---ALKLQMAEK----DKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQE 608
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
711-938 |
3.80e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 711 REAHQKQLSRLRDEIEEKQKIID----EIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKG 786
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAalkkEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 787 LEETVSRelqtlhNLRKLFVQDLTTRVKksVELDNDDGGGSAAQ----KQKISFLENNLEQLTKVHKQLVRDNADLRCEL 862
Cdd:COG4942 102 QKEELAE------LLRALYRLGRQPPLA--LLLSPEDFLDAVRRlqylKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758650 863 PKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIAKPIRPGHYPASSPTA 938
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
516-748 |
4.94e-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: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 516 TDELAQKTTTLTTTQRELSQLQELSNHQKKRATEilnlLLKDLGEIggiigTNDVKTLADVNGVIEEEFTMARLYISKMK 595
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAAL-----ERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 596 SEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQe 675
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE- 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758650 676 kmhevsFQDKEKEHLTRLQDAEEMKKALEQQMESHREA---HQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEK 748
Cdd:COG4942 169 ------LEAERAELEALLAELEEERAALEALKAERQKLlarLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
413-888 |
5.37e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 413 EKEKYDEEISSLYRQLDDKDDEINQ-------QSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVK 485
Cdd:PRK02224 273 EREELAEEVRDLRERLEELEEERDDllaeaglDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDAD 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 486 EvlqaLEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGII 565
Cdd:PRK02224 353 D----LEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 566 GTNDVkTLADVNGVIEEEftmARLY--------------------ISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERE 625
Cdd:PRK02224 429 AELEA-TLRTARERVEEA---EALLeagkcpecgqpvegsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 626 LAAcqllisqhEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMK---KA 702
Cdd:PRK02224 505 VEA--------EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAReevAE 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 703 LEQQMESHREAHQkQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKlssdynklkiEDQEREMKLekllllnDKREQARE 782
Cdd:PRK02224 577 LNSKLAELKERIE-SLERIRTLLAAIADAEDEIERLREKREALAEL----------NDERRERLA-------EKRERKRE 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 783 dlkgLEETVSRE-LQTLHNLRKLFVQDLTTRVKKSVELDNDdgggSAAQKQKISFLENNLEqltkvhkqlvrdnadlrcE 861
Cdd:PRK02224 639 ----LEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREE----RDDLQAEIGAVENELE------------------E 692
|
490 500
....*....|....*....|....*..
gi 4758650 862 LPKLEKRLRATAERVKALESALKEAKE 888
Cdd:PRK02224 693 LEELRERREALENRVEALEALYDEAEE 719
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
421-759 |
5.94e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.50 E-value: 5.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 421 ISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNYDQ 500
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLES 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 501 KSQEVED-------KTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKdlgeiggiigtndvktL 573
Cdd:pfam15921 494 SERTVSDltaslqeKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQ----------------M 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 574 ADVNGVIEeeftMARLYISKMKSEV--KSLVNRSKQLESAQMDsnRKMNASERELAACQLLISQHEAKIKSLTDYMQNME 651
Cdd:pfam15921 558 AEKDKVIE----ILRQQIENMTQLVgqHGRTAGAMQVEKAQLE--KEINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 652 ---------------------QKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQMESH 710
Cdd:pfam15921 632 lekvklvnagserlravkdikQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQT 711
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758650 711 R---------EAH--------QKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIE 759
Cdd:pfam15921 712 RntlksmegsDGHamkvamgmQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQE 777
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
696-925 |
6.47e-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: 49.38 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 696 AEEMKKALEQQMESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSsdynklKIEdQEREMKLEKLLLLND 775
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR------ALE-QELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 776 KREQAREDLKGLEETVSRELQTLHNLRK------LFVQD-------LTTRVKKSVELDNDDGGGSAAQKQKISFLENNLE 842
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRqpplalLLSPEdfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 843 QLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKnmARRAHSAQI 922
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA--AERTPAAGF 248
|
...
gi 4758650 923 AKP 925
Cdd:COG4942 249 AAL 251
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
444-800 |
7.46e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.83 E-value: 7.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 444 KLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNYDQKSQEVEDktrANEQLTDELAQkt 523
Cdd:PRK04778 102 KAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGP---ALDELEKQLEN-- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 524 ttlttTQRELSQLQELS---NHQKkrATEILNLLLKDLGEIGGIIgtNDVKTL-ADVNGVIEEEFTMARLYISKMKSE-- 597
Cdd:PRK04778 177 -----LEEEFSQFVELTesgDYVE--AREILDQLEEELAALEQIM--EEIPELlKELQTELPDQLQELKAGYRELVEEgy 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 598 ---VKSLVNRSKQLEsAQMDSNRKMnASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQ 674
Cdd:PRK04778 248 hldHLDIEKEIQDLK-EQIDENLAL-LEELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQ 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 675 EK--MHEVSF-----------QDKEKEHLTRLQDAEEMKKALEQQMESHREAHqkqlSRLRDEIEEKQKIIDEIrdlnqk 741
Cdd:PRK04778 326 NKelKEEIDRvkqsytlneseLESVRQLEKQLESLEKQYDEITERIAEQEIAY----SELQEELEEILKQLEEI------ 395
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4758650 742 lQLEQEKLSSDYNKLKIEDQE--REMKLEKLLLLNDKREQAREDLKGLEE-------TVSRELQTLHN 800
Cdd:PRK04778 396 -EKEQEKLSEMLQGLRKDELEarEKLERYRNKLHEIKRYLEKSNLPGLPEdylemffEVSDEIEALAE 462
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
6-269 |
1.09e-05 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 49.35 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 6 ECSIKVMCRFRPLNEA--EILRGDKFIPKFKGDETVVI---GQGKP-----YVFDRVLPPNTTQEQVYNaCAKQIVKDVL 75
Cdd:COG5059 304 NCNTRVICTISPSSNSfeETINTLKFASRAKSIKNKIQvnsSSDSSreieeIKFDLSEDRSEIEILVFR-EQSQLSQSSL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 76 EGyngtIFAYGQTSSGKTHTMEGKLHDPQ---LMGIIPRIAHDIFDHIYSMDENLEFHIKVSYfeiyldKIRDLLDVSKT 152
Cdd:COG5059 383 SG----IFAYMQSLKKETETLKSRIDLIMksiISGTFERKKLLKEEGWKYKSTLQFLRIEIDR------LLLLREEELSK 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 153 NLAVHEDKNRVpyvKGCTERFVS-SPEEVMDVIDEGKA--NRHVAVTNMNEHSSRSHSIFlINIKQENVETEKKLSgkLY 229
Cdd:COG5059 453 KKTKIHKLNKL---RHDLSSLLSsIPEETSDRVESEKAskLRSSASTKLNLRSSRSHSKF-RDHLNGSNSSTKELS--LN 526
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 4758650 230 LVDLAGSEKVSKTgAEGAVLDEAKNINKSLSALGNVISAL 269
Cdd:COG5059 527 QVDLAGSERKVSQ-SVGELLRETQSLNKSLSSLGDVIHAL 565
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
411-741 |
2.03e-05 |
|
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: 48.66 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 411 TEEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEE-------LTRLQiENEAAKDE 483
Cdd:pfam10174 372 TEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDssntdtaLTTLE-EALSEKER 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 484 VKEVLQalEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEI-- 561
Cdd:pfam10174 451 IIERLK--EQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVeq 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 562 ---GGIIGTNDVKT-------------LADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNaserE 625
Cdd:pfam10174 529 kkeECSKLENQLKKahnaeeavrtnpeINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIA----E 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 626 LAACQLLISQHEAKIKSLTDYMQNMEQKRR--QLEES---QDSLSEELAKLRAQEKMHEVSfqdKEKEHLtrlqDAEEMK 700
Cdd:pfam10174 605 LESLTLRQMKEQNKKVANIKHGQQEMKKKGaqLLEEArrrEDNLADNSQQLQLEELMGALE---KTRQEL----DATKAR 677
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 4758650 701 KALEQQMESHREAHqkqLSRLRdeiEEKQKIIDEIRDLNQK 741
Cdd:pfam10174 678 LSSTQQSLAEKDGH---LTNLR---AERRKQLEEILEMKQE 712
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
411-748 |
2.66e-05 |
|
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: 48.18 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 411 TEEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQA 490
Cdd:pfam05483 400 KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 491 LE-------ELAVNYDQKSQEVEDKTRANEQLTDELAQKTTT----LTTTQRELSQLQELSNHQKKRATEILNL---LLK 556
Cdd:pfam05483 480 LEkeklkniELTAHCDKLLLENKELTQEASDMTLELKKHQEDiincKKQEERMLKQIENLEEKEMNLRDELESVreeFIQ 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 557 DLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYiSKMKSEVKSLVNRSKQLESAQMDS----------NRKMNASEREL 626
Cdd:pfam05483 560 KGDEVKCKLDKSEENARSIEYEVLKKEKQMKILE-NKCNNLKKQIENKNKNIEELHQENkalkkkgsaeNKQLNAYEIKV 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 627 AACQLLISQHEAKIKSLTD-YMQNMEQKRRQLE------ESQDSLSEELAKL------RAQEKMHE-VSFQDKEKEHLTR 692
Cdd:pfam05483 639 NKLELELASAKQKFEEIIDnYQKEIEDKKISEEklleevEKAKAIADEAVKLqkeidkRCQHKIAEmVALMEKHKHQYDK 718
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 693 LQDAEE----MKKALEQQMESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEK 748
Cdd:pfam05483 719 IIEERDselgLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
412-762 |
3.33e-05 |
|
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: 47.54 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 412 EEKEKYDEeISSlyRQLDDKDDEINQQSQLAEKL-----KQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKE 486
Cdd:pfam06160 49 EWRKKWDD-IVT--KSLPDIEELLFEAEELNDKYrfkkaKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 487 VLQALEELAVNYDQKSQEVEDktrANEQLTDELAQktttlttTQRELSQLQEL-SNHQKKRATEILNLLLKDLGEIGGII 565
Cdd:pfam06160 126 LKDKYRELRKTLLANRFSYGP---AIDELEKQLAE-------IEEEFSQFEELtESGDYLEAREVLEKLEEETDALEELM 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 566 gtNDVKTL-ADVNGVIEEEFTMARLYISKMKSEVKSL--VNRSKQLESAQMDSNRKMNASER-ELAACQLLISQHEAKIK 641
Cdd:pfam06160 196 --EDIPPLyEELKTELPDQLEELKEGYREMEEEGYALehLNVDKEIQQLEEQLEENLALLENlELDEAEEALEEIEERID 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 642 SLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQ-----EKMHEV--SFQDKEKEhLTRLQDAEEMKKALEQQMESHREA- 713
Cdd:pfam06160 274 QLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQnkelkEELERVqqSYTLNENE-LERVRGLEKQLEELEKRYDEIVERl 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 4758650 714 --HQKQLSRLRDEIEEKQKIIDEIRDlnqklqlEQEKLSSDYNKLKIEDQE 762
Cdd:pfam06160 353 eeKEVAYSELQEELEEILEQLEEIEE-------EQEEFKESLQSLRKDELE 396
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
410-915 |
3.49e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 410 STEEKEKYDE--EISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVK-- 485
Cdd:PTZ00121 1373 KEEAKKKADAakKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKkk 1452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 486 -EVLQALEELAVNYDQKSQEVEDKTRANE-QLTDELAQKTTTLTTTQRELSQLQElsnhQKKRATEILNLLLKDLGEIgg 563
Cdd:PTZ00121 1453 aEEAKKAEEAKKKAEEAKKADEAKKKAEEaKKADEAKKKAEEAKKKADEAKKAAE----AKKKADEAKKAEEAKKADE-- 1526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 564 iIGTNDVKTLADVNGVIEEEFTMARLYIS---KMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKI 640
Cdd:PTZ00121 1527 -AKKAEEAKKADEAKKAEEKKKADELKKAeelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 641 KSLTDYMQNMEQKRRQLEESQDSlsEELAKLRAQEKMHEvsfqDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQLSR 720
Cdd:PTZ00121 1606 KMKAEEAKKAEEAKIKAEELKKA--EEEKKKVEQLKKKE----AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 721 LRDEIEEKQKIIDEI-RDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDlkgleetvsrelqtlh 799
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALkKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK---------------- 1743
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 800 nlrklfvqdlttrvKKSVELDNDDGGGSAAQKQKISfLENNLEQLTKVHKQLVRDNADLRCELPKLEKRlRATAERVKAL 879
Cdd:PTZ00121 1744 --------------KKAEEAKKDEEEKKKIAHLKKE-EEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD-KKIKDIFDNF 1807
|
490 500 510
....*....|....*....|....*....|....*.
gi 4758650 880 ESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMAR 915
Cdd:PTZ00121 1808 ANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQL 1843
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
593-924 |
3.89e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 593 KMKSEVKSLVNRSKQLESAQmdSNRKMNASERELAACQLLISQHEAK---IKSLTDYMQNMEQKRRQLEESQDSLSEELA 669
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEA--AADEAEAAEEKAEAAEKKKEEAKKKadaAKKKAEEKKKADEAKKKAEEDKKKADELKK 1412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 670 KLRAQEKMHEVSFQDKEKEHLTRLQD-AEEMKKALEQQMESHReahQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEK 748
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADEAKKkAEEAKKADEAKKKAEE---AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK 1489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 749 LSSDYNKLKIEDQEREMKLEKLLLLNDKREQARedlKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDNDDGGGSA 828
Cdd:PTZ00121 1490 KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK---KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKA 1566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 829 AQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATA------ERVKALESALKEAKENAMRDRKRYQQEVD 902
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakkaeeAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646
|
330 340
....*....|....*....|..
gi 4758650 903 RIKEAVRAKNMARRAHSAQIAK 924
Cdd:PTZ00121 1647 KKAEELKKAEEENKIKAAEEAK 1668
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
412-535 |
4.16e-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: 46.07 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDqdellASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQAL 491
Cdd:COG1579 45 ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-----VRNNKEYEALQKEIESLKRRISDLEDEILELMERI 119
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 4758650 492 EELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQ 535
Cdd:COG1579 120 EELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
414-911 |
4.33e-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: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 414 KEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMldqdellastRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEE 493
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYL----------RQSVIDLQTKLQEMQMERDAMADIRRRESQSQED 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 494 LAVNYDQKSQEVEDKTRANEQLTDElaqktttlttTQRELSQLQELSNHQKKRATEILNLLLkDLGEIGGiigtndvKTL 573
Cdd:pfam15921 143 LRNQLQNTVHELEAAKCLKEDMLED----------SNTQIEQLRKMMLSHEGVLQEIRSILV-DFEEASG-------KKI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 574 ADVNGVIEEEFTMARLYISKMKSEVKSLVNRSK--------QLESAQMDSNRKMNAS-ERELAACQLLISQHEAKIKSLT 644
Cdd:pfam15921 205 YEHDSMSTMHFRSLGSAISKILRELDTEISYLKgrifpvedQLEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLT 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 645 dymQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQMEShreaHQKQLSRLRDE 724
Cdd:pfam15921 285 ---EKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEE----LEKQLVLANSE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 725 IEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEdqeremklEKLLLLNDKREQAREDLKGLE-ETVSRELQTlhnlRK 803
Cdd:pfam15921 358 LTEARTERDQFSQESGNLDDQLQKLLADLHKREKE--------LSLEKEQNKRLWDRDTGNSITiDHLRRELDD----RN 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 804 LFVQDLTTRVKKsveLDNDDGGgsaAQKQKISFLENNLEQLTKVhkqlvrdnADLRCELPKLEKRLRATAERVKALESAL 883
Cdd:pfam15921 426 MEVQRLEALLKA---MKSECQG---QMERQMAAIQGKNESLEKV--------SSLTAQLESTKEMLRKVVEELTAKKMTL 491
|
490 500
....*....|....*....|....*...
gi 4758650 884 kEAKENAMRDRKRYQQEVDRIKEAVRAK 911
Cdd:pfam15921 492 -ESSERTVSDLTASLQEKERAIEATNAE 518
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
601-919 |
4.41e-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: 47.73 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 601 LVNRSKQLESAQMDSNRKMNASErELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEelaklraqeKMHEV 680
Cdd:TIGR00606 226 ITSKEAQLESSREIVKSYENELD-PLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELEL---------KMEKV 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 681 SFQDKEKehltrLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIED 760
Cdd:TIGR00606 296 FQGTDEQ-----LNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 761 QEREMKLEKLLLLNDK--REQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDNDDGGGSAAQKQKISFLE 838
Cdd:TIGR00606 371 QSLATRLELDGFERGPfsERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 839 NNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAH 918
Cdd:TIGR00606 451 KKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHH 530
|
.
gi 4758650 919 S 919
Cdd:TIGR00606 531 T 531
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
380-730 |
4.51e-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: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 380 EQISAKdQKNLEPCDNTpiidnIAPVVAGISTEEK--EKYDEEISSLYRQLDDKDDEI----NQQSQL------AEKLKQ 447
Cdd:pfam15921 482 EELTAK-KMTLESSERT-----VSDLTASLQEKERaiEATNAEITKLRSRVDLKLQELqhlkNEGDHLrnvqteCEALKL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 448 QMLDQDELLASTRRDYEKIQEELTR-------LQIENEAAKDEVKEVLQALEELAVNYDQKSQEVEDktrANEQLTDELA 520
Cdd:pfam15921 556 QMAEKDKVIEILRQQIENMTQLVGQhgrtagaMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRE---LEARVSDLEL 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 521 QKTTTLTTTQRELSQLQELsnhqKKRATEILNLLLKDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARL--YISKMKSEV 598
Cdd:pfam15921 633 EKVKLVNAGSERLRAVKDI----KQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLkmQLKSAQSEL 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 599 KSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLrAQEKmh 678
Cdd:pfam15921 709 EQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTV-ATEK-- 785
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 4758650 679 evsfqDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEEKQK 730
Cdd:pfam15921 786 -----NKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQ 832
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
421-804 |
7.02e-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: 46.67 E-value: 7.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 421 ISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRdyEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNYDQ 500
Cdd:pfam07111 272 VQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWR--EKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTS 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 501 KSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKR---ATEILNLLlkdlgeIGGIIGTNDvktladvn 577
Cdd:pfam07111 350 QSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQtasAEEQLKFV------VNAMSSTQI-------- 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 578 gviEEEFTMARLyiSKMKSEVKSLVNR----SKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQK 653
Cdd:pfam07111 416 ---WLETTMTRV--EQAVARIPSLSNRlsyaVRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREER 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 654 RR---QLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQMESHREAHQ---KQLSRLRDEIEE 727
Cdd:pfam07111 491 NRldaELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQestEEAASLRQELTQ 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 728 KQKIIDeirdlnqklQLEQEKLSSDYNKLK--IEDQEREMKLEkllllndKREQARE--DLKGLEETVSRELQTLHNLRK 803
Cdd:pfam07111 571 QQEIYG---------QALQEKVAEVETRLReqLSDTKRRLNEA-------RREQAKAvvSLRQIQHRATQEKERNQELRR 634
|
.
gi 4758650 804 L 804
Cdd:pfam07111 635 L 635
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
374-924 |
7.16e-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: 46.76 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 374 EAVPEDEQISAKDQKN-LEPCDNTPIIDNIAPVVAGISTEEK--EKYDEEISSLYRQLddkddeINQQSQLAEKLKQQML 450
Cdd:pfam12128 210 GVVPPKSRLNRQQVEHwIRDIQAIAGIMKIRPEFTKLQQEFNtlESAELRLSHLHFGY------KSDETLIASRQEERQE 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 451 DQDELLASTRRDYEKIQEELTRLQIENEAAKDEVK---EVLQALEELAVNYDQKSQEvedkTRANEQltDELAQKTTTLT 527
Cdd:pfam12128 284 TSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAkdrSELEALEDQHGAFLDADIE----TAAADQ--EQLPSWQSELE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 528 TTQRELSQLqeLSNHQK-KRATEILNLLLKdlgeiggiigtndvKTLADVNGVIEEEFTMARLYISKMKSEVKSLVnrsK 606
Cdd:pfam12128 358 NLEERLKAL--TGKHQDvTAKYNRRRSKIK--------------EQNNRDIAGIKDKLAKIREARDRQLAVAEDDL---Q 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 607 QLESAQmdsNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSeelaklRAQEKmhevsfQDKE 686
Cdd:pfam12128 419 ALESEL---REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIE------RAREE------QEAA 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 687 KEHLTRLQDAE-EMKKALEQQMESHREAHQKqLSRLRDEIEEKQKIIDE-----IRDLNQKLQLEQEKLS---------- 750
Cdd:pfam12128 484 NAEVERLQSELrQARKRRDQASEALRQASRR-LEERQSALDELELQLFPqagtlLHFLRKEAPDWEQSIGkvispellhr 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 751 SDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKgLEETVSREL----QTLHNLRKLFVQDLTTRVKKSVELDNDDGGG 826
Cdd:pfam12128 563 TDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAA-SEEELRERLdkaeEALQSAREKQAAAEEQLVQANGELEKASREE 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 827 SAAqKQKISFLENNLEQLTKVHKQL-VRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRD-------RKRYQ 898
Cdd:pfam12128 642 TFA-RTALKNARLDLRRLFDEKQSEkDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQkrearteKQAYW 720
|
570 580 590
....*....|....*....|....*....|....
gi 4758650 899 QEV--------DRIKEAVRAKNMARRAHSAQIAK 924
Cdd:pfam12128 721 QVVegaldaqlALLKAAIAARRSGAKAELKALET 754
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
378-916 |
9.45e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 9.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 378 EDEQISAKDQKNLEPCDN--TPIIDNIAPVVAGISTEEKEKYDEEisslyrqldDKDDEINQQSQLAEKLKQQMLDQDEL 455
Cdd:PTZ00121 1239 AEEAKKAEEERNNEEIRKfeEARMAHFARRQAAIKAEEARKADEL---------KKAEEKKKADEAKKAEEKKKADEAKK 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 456 LASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNYDQKSQEVE---DKTRANEQLTDELAQKTTTLTTTQRE 532
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaaeEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 533 LSQLQELsnhqKKRATEILNlllkdlgeiggiiGTNDVKTLADVNGVIEEeftmarlyISKMKSEVKSLVNRSKQLESAQ 612
Cdd:PTZ00121 1390 KKKADEA----KKKAEEDKK-------------KADELKKAAAAKKKADE--------AKKKAEEKKKADEAKKKAEEAK 1444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 613 MDSNRKMNASERELAacQLLISQHEAKIKSltDYMQNMEQKRRQLEESQDSLSEelaklrAQEKMHEVSFQDKEKEHLTR 692
Cdd:PTZ00121 1445 KADEAKKKAEEAKKA--EEAKKKAEEAKKA--DEAKKKAEEAKKADEAKKKAEE------AKKKADEAKKAAEAKKKADE 1514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 693 LQDAEEMKKAleqqmESHREAHQKQLSRLRDEIEEKQKIiDEIRdlnqklqlEQEKLSSDYNKLKIEDQEREMKleklll 772
Cdd:PTZ00121 1515 AKKAEEAKKA-----DEAKKAEEAKKADEAKKAEEKKKA-DELK--------KAEELKKAEEKKKAEEAKKAEE------ 1574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 773 lnDKREQAR--EDLKGLEETVSRELQTLHNLRKlfvqdlttRVKKSVELDNDDGGGSAAQKQKISFLENNLEQLTKVHKQ 850
Cdd:PTZ00121 1575 --DKNMALRkaEEAKKAEEARIEEVMKLYEEEK--------KMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4758650 851 LVRDNADLRCElpKLEKRLRATAERVKALESALK--EAKENAMRDRKRYQQEVDRIKEAVRAKNMARR 916
Cdd:PTZ00121 1645 EKKKAEELKKA--EEENKIKAAEEAKKAEEDKKKaeEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
623-894 |
9.58e-05 |
|
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: 46.50 E-value: 9.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 623 ERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHE--VSFQDKEKEHLTRLQDAEEMK 700
Cdd:TIGR00618 197 ELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEeqLKKQQLLKQLRARIEELRAQE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 701 KALEQQMEshREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLN------ 774
Cdd:TIGR00618 277 AVLEETQE--RINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQtlhsqe 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 775 DKREQAREDLKGLEETVSRELQTLHNLRKLfVQDLTTrvkksveldnddgggsaaQKQKISFLENNLEQLTK-VHKQLVR 853
Cdd:TIGR00618 355 IHIRDAHEVATSIREISCQQHTLTQHIHTL-QQQKTT------------------LTQKLQSLCKELDILQReQATIDTR 415
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 4758650 854 DNA--DLRCELPKLEKRLRATAERVKALESAL-KEAKENAMRDR 894
Cdd:TIGR00618 416 TSAfrDLQGQLAHAKKQQELQQRYAELCAAAItCTAQCEKLEKI 459
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
419-674 |
1.32e-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: 45.53 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 419 EEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNY 498
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 499 DQKSQEVEDKTRA----NEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEIlnlllkdlgeiggiigTNDVKTLA 574
Cdd:COG4942 100 EAQKEELAELLRAlyrlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL----------------RADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 575 DVNGVIEEEftmarlyiskmksevkslvnrSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKR 654
Cdd:COG4942 164 ALRAELEAE---------------------RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
250 260
....*....|....*....|
gi 4758650 655 RQLEESQDSLSEELAKLRAQ 674
Cdd:COG4942 223 EELEALIARLEAEAAAAAER 242
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
446-788 |
1.33e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 446 KQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALeelavnydqKSQEVEDKTRAN-EQLTDELAQKTT 524
Cdd:PRK04863 299 RRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAL---------RQQEKIERYQADlEELEERLEEQNE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 525 TltttqRELSQLQELSNHQKKRATEILNLLLKdlgeiggiigtndvKTLADVNGVIEEEFTMARLYiskmkSEVKSLVNR 604
Cdd:PRK04863 370 V-----VEEADEQQEENEARAEAAEEEVDELK--------------SQLADYQQALDVQQTRAIQY-----QQAVQALER 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 605 SKQLesaqmdsnrkMNASERELAACQLLISQHEAKIKSLTDYMQNMEQK-------RRQLEESQD---SLSEELAKLRAQ 674
Cdd:PRK04863 426 AKQL----------CGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKlsvaqaaHSQFEQAYQlvrKIAGEVSRSEAW 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 675 EKMHEVSFQDKEKEHL-TRLQDAEEMKKALEQQMESHREAHqkqlsRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDY 753
Cdd:PRK04863 496 DVARELLRRLREQRHLaEQLQQLRMRLSELEQRLRQQQRAE-----RLLAEFCKRLGKNLDDEDELEQLQEELEARLESL 570
|
330 340 350
....*....|....*....|....*....|....*
gi 4758650 754 NKLKIEDQEREMKLEkllllnDKREQAREDLKGLE 788
Cdd:PRK04863 571 SESVSEARERRMALR------QQLEQLQARIQRLA 599
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
598-794 |
1.78e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 598 VKSLVNRSKQLESAQmDSNRKMNASERELAACQL-LISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEK 676
Cdd:COG4717 48 LERLEKEADELFKPQ-GRKPELNLKELKELEEELkEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 677 MHEvsfqdkekeHLTRLQDAEEMKKALEQQMESHREAHQ------KQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQ-EKL 749
Cdd:COG4717 127 LLP---------LYQELEALEAELAELPERLEELEERLEelreleEELEELEAELAELQEELEELLEQLSLATEEElQDL 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 4758650 750 SSDYNKLKiedQEREMKLEKLLLLNDKREQAREDLKGLEETVSRE 794
Cdd:COG4717 198 AEELEELQ---QRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
625-784 |
1.90e-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: 44.15 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 625 ELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKE------KEHLTRLQDAEE 698
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEarikkyEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 699 MKkALEQQMESHReahqKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIE-DQEREMKLEKLLLLNDKR 777
Cdd:COG1579 91 YE-ALQKEIESLK----RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAElDEELAELEAELEELEAER 165
|
....*..
gi 4758650 778 EQAREDL 784
Cdd:COG1579 166 EELAAKI 172
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
419-560 |
2.52e-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: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 419 EEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELtrlqienEAAKDEVKEVLQALEELAVNY 498
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-------EALLNERASLEEALALLRSEL 896
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4758650 499 DQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGE 560
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEA 958
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
412-688 |
2.60e-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: 44.73 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 412 EEKEKYDEEISSlYRQLDDKDD----EINQQSQL-AEKLKQQMLDQDEL----LASTRRDYEKIQE-----------ELT 471
Cdd:pfam17380 303 QEKEEKAREVER-RRKLEEAEKarqaEMDRQAAIyAEQERMAMERERELerirQEERKRELERIRQeeiameisrmrELE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 472 RLQIENEAAKDEVKEVLQALEElavnydQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQElsnhqkKRATEIL 551
Cdd:pfam17380 382 RLQMERQQKNERVRQELEAARK------VKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEE------ERAREME 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 552 NLLLKDLGEiggiigTNDVKTLADVngviEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSN--------RKMNASE 623
Cdd:pfam17380 450 RVRLEEQER------QQQVERLRQQ----EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERkqamieeeRKRKLLE 519
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758650 624 RELAACQLLISQHEAKIKSLTDYMQNME-QKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKE 688
Cdd:pfam17380 520 KEMEERQKAIYEEERRREAEEERRKQQEmEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESE 585
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
455-892 |
2.63e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.04 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 455 LLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQAleelAVNYDQKSQEVEDKTRANEQLTDELAQktttlttTQRELS 534
Cdd:PRK10929 17 AYAATAPDEKQITQELEQAKAAKTPAQAEIVEALQS----ALNWLEERKGSLERAKQYQQVIDNFPK-------LSAELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 535 qlQELSNHQKKRATEILNLLLKDLGEigGIIGTNDvkTLADVNGVIEEEFTMARlyiskmksEVKSLVNrskQLESAQMD 614
Cdd:PRK10929 86 --QQLNNERDEPRSVPPNMSTDALEQ--EILQVSS--QLLEKSRQAQQEQDRAR--------EISDSLS---QLPQQQTE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 615 SNRKMNASERELAA----------CQLLISQHE-AKIKSLTDymqnmeqkrrQLEESQDSLS--EELAKLRAQ--EKMHE 679
Cdd:PRK10929 149 ARRQLNEIERRLQTlgtpntplaqAQLTALQAEsAALKALVD----------ELELAQLSANnrQELARLRSElaKKRSQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 680 ------------VSFQDKEK-----EHLTRL-QDAEEMKKALEQQMESHREAHQ---KQLSRLrDEIEEKQKIIDeirdl 738
Cdd:PRK10929 219 qldaylqalrnqLNSQRQREaeralESTELLaEQSGDLPKSIVAQFKINRELSQalnQQAQRM-DLIASQQRQAA----- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 739 NQKLQLEQeklssdynklkiedqeremklekllLLNDKREQAR--EDLKGLEET----VSR-----ELQTLHN------L 801
Cdd:PRK10929 293 SQTLQVRQ-------------------------ALNTLREQSQwlGVSNALGEAlraqVARlpempKPQQLDTemaqlrV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 802 RKLFVQDLTTRVKKSVELDNDDGGGSAAQKQKIsflennLEQLTKVHKQLVR------DNADLrcELPKLEKrlrATAEr 875
Cdd:PRK10929 348 QRLRYEDLLNKQPQLRQIRQADGQPLTAEQNRI------LDAQLRTQRELLNsllsggDTLIL--ELTKLKV---ANSQ- 415
|
490
....*....|....*..
gi 4758650 876 vkaLESALKEAKENAMR 892
Cdd:PRK10929 416 ---LEDALKEVNEATHR 429
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
580-885 |
2.90e-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: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 580 IEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEE 659
Cdd:pfam01576 136 LEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 660 SQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQMESHREAhQKQLSRLRDEIEEKqkiideiRDLN 739
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIREL-EAQISELQEDLESE-------RAAR 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 740 QKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLK--GLEETVSRELQtlhnlrklfVQDLTTRVKKSV 817
Cdd:pfam01576 288 NKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKkaLEEETRSHEAQ---------LQEMRQKHTQAL 358
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4758650 818 ELDNDdgggsaaqkqKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKE 885
Cdd:pfam01576 359 EELTE----------QLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE 416
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
645-746 |
3.26e-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: 44.94 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 645 DYMQNMEQKR-----------------RQLEESQDSL---SEELAKLRAQEKMHEVSFQDKEkEHLTRLQDA-------- 696
Cdd:COG3096 272 DYMRHANERRelseralelrrelfgarRQLAEEQYRLvemARELEELSARESDLEQDYQAAS-DHLNLVQTAlrqqekie 350
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 697 ------EEMKKALEQQMESHREAHQkQLSRLRDEIEEKQKIIDEIR----DLNQKLQLEQ 746
Cdd:COG3096 351 ryqedlEELTERLEEQEEVVEEAAE-QLAEAEARLEAAEEEVDSLKsqlaDYQQALDVQQ 409
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
416-911 |
3.40e-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: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 416 KYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQ---ALE 492
Cdd:pfam01576 240 KKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDttaAQQ 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 493 ELAVNYDQKSQE----VEDKTRANEQLTDELAQKTTTLTTtqrELSQLQELSNHQKKRATEILNLLLKDLGEIggiigTN 568
Cdd:pfam01576 320 ELRSKREQEVTElkkaLEEETRSHEAQLQEMRQKHTQALE---ELTEQLEQAKRNKANLEKAKQALESENAEL-----QA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 569 DVKTLADVNGVIEEEFtmarlyiSKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQ 648
Cdd:pfam01576 392 ELRTLQQAKQDSEHKR-------KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVS 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 649 NMEQkrrQLEESQDSLSEEL-AKLRAQEKMHevSFQDKEKEHLTRLQDAEEMKKALEQQMESHreahQKQLSRLRDEIEE 727
Cdd:pfam01576 465 SLES---QLQDTQELLQEETrQKLNLSTRLR--QLEDERNSLQEQLEEEEEAKRNVERQLSTL----QAQLSDMKKKLEE 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 728 KQKIIDEIRDLNQKLQLEQEKLSSDYnklkiedQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQ 807
Cdd:pfam01576 536 DAGTLEALEEGKKRLQRELEALTQQL-------EEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQ 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 808 DLTTRVKKSVEL--DNDDGGGSAAQKQ-KISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESAlK 884
Cdd:pfam01576 609 MLAEEKAISARYaeERDRAEAEAREKEtRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERS-K 687
|
490 500
....*....|....*....|....*...
gi 4758650 885 EAKENAMRDRKRYQQEV-DRIKEAVRAK 911
Cdd:pfam01576 688 RALEQQVEEMKTQLEELeDELQATEDAK 715
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
605-735 |
3.62e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 605 SKQLESAQMDSNRKMNASERELAA----CQL--------LISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLR 672
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAikkeALLeakeeihkLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4758650 673 AQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQME-----SHREAHQKQLSRLRDEIE-EKQKIIDEI 735
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIEEQLQELErisglTAEEAKEILLEKVEEEARhEAAVLIKEI 178
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
591-736 |
6.13e-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: 42.60 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 591 ISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDyMQNMEQKRRQLEesqdSLSEELAK 670
Cdd:COG1579 26 LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE-QLGNVRNNKEYE----ALQKEIES 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758650 671 LRAQEKMHEvsfqDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEEKQKIIDEIR 736
Cdd:COG1579 101 LKRRISDLE----DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
651-746 |
8.96e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 8.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 651 EQKRRQLEESQDSLSEELAKLRAQEKmhevSFQDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEE--- 727
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELER----ELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQaik 580
|
90 100
....*....|....*....|.
gi 4758650 728 --KQKIIDEIRDLNQKLQLEQ 746
Cdd:PRK00409 581 eaKKEADEIIKELRQLQKGGY 601
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
568-904 |
9.31e-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: 43.42 E-value: 9.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 568 NDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNrKMNASERELAACQLLISQHEAKIKSLTDYM 647
Cdd:pfam02463 184 NLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL-KLNEERIDLLQELLRDEQEEIESSKQEIEK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 648 QNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQMEshrEAHQKQLSRLRDEIEE 727
Cdd:pfam02463 263 EEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK---KKAEKELKKEKEEIEE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 728 KQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKlfVQ 807
Cdd:pfam02463 340 LEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELAR--QL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 808 DLTTRVKKSVELDNDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAK 887
Cdd:pfam02463 418 EDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEE 497
|
330
....*....|....*..
gi 4758650 888 ENAMRDRKRYQQEVDRI 904
Cdd:pfam02463 498 RSQKESKARSGLKVLLA 514
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
715-916 |
1.14e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 715 QKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKiedqEREMKLEKLLLLNDKREQareDLKGLEETVsRE 794
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLEG---SKRKLEEKI-RE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 795 LQTLHNLRKLFVQDLTTRVKKSVELDnddggGSAAQKQKIS-FLENNLEQLTKVHKqlvrdnadlrcELPKLEKRLRATA 873
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVKELKELK-----EKAEEYIKLSeFYEEYLDELREIEK-----------RLSRLEEEINGIE 327
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 4758650 874 ERVKALESALKEAKENAMRdRKRYQQEVDRIKEAVRAKNMARR 916
Cdd:PRK03918 328 ERIKELEEKEERLEELKKK-LKELEKRLEELEERHELYEEAKA 369
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
413-560 |
1.26e-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: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 413 EKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVL---- 488
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 489 -------------------------QALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQ 543
Cdd:COG3883 97 rsggsvsyldvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170
....*....|....*..
gi 4758650 544 KKRATEILNLLLKDLGE 560
Cdd:COG3883 177 QAEQEALLAQLSAEEAA 193
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
412-759 |
1.37e-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: 42.40 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 412 EEKEKYDEEIsslYRQLDDKDDEINQQSQ-----LAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAK----- 481
Cdd:pfam05483 274 EEKTKLQDEN---LKELIEKKDHLTKELEdikmsLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAahsfv 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 482 -DEVKEVLQALEELAVNYDQKSQEVEDK----TRANEQLTDELAQKTTTLTTTQRELSQLQELSN------HQKKRATEI 550
Cdd:pfam05483 351 vTEFEATTCSLEELLRTEQQRLEKNEDQlkiiTMELQKKSSELEEMTKFKNNKEVELEELKKILAedekllDEKKQFEKI 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 551 LNLLLKDLGEIGGIIGTNDvKTLADVNgVIEEEFTMARLYISKMKSEVKSLVNRSKqLESAQMDSNRKMNASE-----RE 625
Cdd:pfam05483 431 AEELKGKEQELIFLLQARE-KEIHDLE-IQLTAIKTSEEHYLKEVEDLKTELEKEK-LKNIELTAHCDKLLLEnkeltQE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 626 LAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQekmhevsFQDKEKEHLTRLQDAEEMKKALEQ 705
Cdd:pfam05483 508 ASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREE-------FIQKGDEVKCKLDKSEENARSIEY 580
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 4758650 706 QM---ESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIE 759
Cdd:pfam05483 581 EVlkkEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIK 637
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
412-622 |
1.80e-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: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQmldqdelLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQAL 491
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQE-------LAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 492 EELAVNYDQK----SQEVEDKTRANE---QLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIggi 564
Cdd:COG4942 114 YRLGRQPPLAlllsPEDFLDAVRRLQylkYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL--- 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 4758650 565 igTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNAS 622
Cdd:COG4942 191 --EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
606-763 |
1.98e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 606 KQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDK 685
Cdd:pfam07888 55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 686 EKEHLTRLQDAEEMkkalEQQMESHREAHQKQLSRLRDEIEEKqkiideiRDLNQKLQLEQEK---LSSDYNKLKIEDQE 762
Cdd:pfam07888 135 EEDIKTLTQRVLER----ETELERMKERAKKAGAQRKEEEAER-------KQLQAKLQQTEEElrsLSKEFQELRNSLAQ 203
|
.
gi 4758650 763 R 763
Cdd:pfam07888 204 R 204
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
476-713 |
2.17e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 476 ENEAAKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQElsnhQKKRATEILNLLL 555
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA----EIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 556 KDLGEIGGIIGTNDV----KTLADvngvieeeftmarlYISKMKSeVKSLVNRSKQLESAQMDSNRKMNASERELaacql 631
Cdd:COG3883 93 RALYRSGGSVSYLDVllgsESFSD--------------FLDRLSA-LSKIADADADLLEELKADKAELEAKKAEL----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 632 lisqhEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQMESHR 711
Cdd:COG3883 153 -----EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
..
gi 4758650 712 EA 713
Cdd:COG3883 228 AA 229
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
497-924 |
2.47e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 497 NYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNllLKDLGEIGGIIGTNDVKTLADV 576
Cdd:PTZ00121 1080 DFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARK--AEDARKAEEARKAEDAKRVEIA 1157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 577 NGVIEEEftmaRLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQlliSQHEAKIKSLTDY--MQNMEQKR 654
Cdd:PTZ00121 1158 RKAEDAR----KAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARK---AEEERKAEEARKAedAKKAEAVK 1230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 655 RQLEESQDslsEELAKLRAQEKMHEV--SFQDKEKEHLTRLQD---AEEMKKALE-QQMESHREAHQKQLSRLRDEIEEK 728
Cdd:PTZ00121 1231 KAEEAKKD---AEEAKKAEEERNNEEirKFEEARMAHFARRQAaikAEEARKADElKKAEEKKKADEAKKAEEKKKADEA 1307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 729 QKIIDEIRDLNQ-KLQLEQEKLSSDYNKLKIEDQEREM--KLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLF 805
Cdd:PTZ00121 1308 KKKAEEAKKADEaKKKAEEAKKKADAAKKKAEEAKKAAeaAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA 1387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 806 VQ-DLTTRVKKSVELDN---DDGGGSAAQKQKISFLENNLEQLTKVhkqlvrDNADLRCELPKLEKRLRATAERVKALES 881
Cdd:PTZ00121 1388 EEkKKADEAKKKAEEDKkkaDELKKAAAAKKKADEAKKKAEEKKKA------DEAKKKAEEAKKADEAKKKAEEAKKAEE 1461
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 4758650 882 ALKEAKENAMRDRKRYQQEVDR-----IKEAVRAKNMARRAHSAQIAK 924
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKkadeaKKKAEEAKKKADEAKKAAEAK 1509
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
580-706 |
2.60e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 580 IEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMD--SNRKMNASERELAACQLLISQHEAKIKSLtdyMQNMEQKRRQL 657
Cdd:COG1579 50 AKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKEYEALQKEIESLKRRISDLEDEILEL---MERIEELEEEL 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 4758650 658 EESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQ 706
Cdd:COG1579 127 AELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
684-921 |
2.70e-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: 41.58 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 684 DKEKEHLTRLQD-AEEMKKaleqQMES-HREAHQ-KQLSRLRDEIEEKQKII--DEIRDLNQKLqleqEKLSSDYNKLki 758
Cdd:TIGR02168 182 ERTRENLDRLEDiLNELER----QLKSlERQAEKaERYKELKAELRELELALlvLRLEELREEL----EELQEELKEA-- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 759 edqeremklekllllNDKREQAREDLKGLEETVSrELQTLHNLRKLFVQDLTTRVKksveldnddgggsaAQKQKISFLE 838
Cdd:TIGR02168 252 ---------------EEELEELTAELQELEEKLE-ELRLEVSELEEEIEELQKELY--------------ALANEISRLE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 839 NNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAH 918
Cdd:TIGR02168 302 QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
...
gi 4758650 919 SAQ 921
Cdd:TIGR02168 382 ETL 384
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
412-803 |
2.89e-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: 41.58 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 412 EEKEKYDEEISSLYRQLDDKDdEINQQSQLAEKLKQQMLDqdellastrrdyekIQEELTRLQIENEAAKDEvkevlqal 491
Cdd:TIGR01612 1233 EEKKKSEHMIKAMEAYIEDLD-EIKEKSPEIENEMGIEMD--------------IKAEMETFNISHDDDKDH-------- 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 492 EELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNL--LLKdLGEIGGIIgtND 569
Cdd:TIGR01612 1290 HIISKKHDENISDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIynILK-LNKIKKII--DE 1366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 570 VK----TLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKqLESAQMDsnRKMNASERELAACQLLISQHEAKIKSltd 645
Cdd:TIGR01612 1367 VKeytkEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSK-IESTLDD--KDIDECIKKIKELKNHILSEESNIDT--- 1440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 646 YMQNMEQKRRQLE------ESQDSLSEELAKLRAQEKMHEVSFQDKE-KEHLTRLQ----DAEEMKKALEQQMESHrEAH 714
Cdd:TIGR01612 1441 YFKNADENNENVLllfkniEMADNKSQHILKIKKDNATNDHDFNINElKEHIDKSKgckdEADKNAKAIEKNKELF-EQY 1519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 715 QKQLSRLRD---EIEEKQK----------IIDEIRDLNQKLQLEQEKLSSDYNKLKIEdqerEMKLEKLLLLNDKREQAR 781
Cdd:TIGR01612 1520 KKDVTELLNkysALAIKNKfaktkkdseiIIKEIKDAHKKFILEAEKSEQKIKEIKKE----KFRIEDDAAKNDKSNKAA 1595
|
410 420
....*....|....*....|..
gi 4758650 782 EDLKGLEETVSRELQTLHNLRK 803
Cdd:TIGR01612 1596 IDIQLSLENFENKFLKISDIKK 1617
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
614-746 |
2.99e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 41.51 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 614 DSNRKMNASERELA-ACQLLISQHEakIKSLT--------DYMQNMEQKRRQLEE-------------SQDSLSEELAKL 671
Cdd:pfam13779 486 DAERRLRAAQERLSeALERGASDEE--IAKLMqelrealdDYMQALAEQAQQNPQdlqqpddpnaqemTQQDLQRMLDRI 563
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4758650 672 raQEKMHEVSfQDKEKEHLTRLQDA-EEMKKAL-EQQMESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQ 746
Cdd:pfam13779 564 --EELARSGR-RAEAQQMLSQLQQMlENLQAGQpQQQQQQGQSEMQQAMDELGDLLREQQQLLDETFRQLQQQGGQQ 637
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
420-518 |
3.34e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 420 EISSLYRQLDDKDDEINQ-QSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNY 498
Cdd:COG0542 405 EIDSKPEELDELERRLEQlEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRY 484
|
90 100
....*....|....*....|
gi 4758650 499 DQKSQEVEDKTRANEQLTDE 518
Cdd:COG0542 485 GKIPELEKELAELEEELAEL 504
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
600-922 |
3.56e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.26 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 600 SLVNRSKQLESAQMDSNRKMNASERELAAcqlLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHE 679
Cdd:pfam05557 10 RLSQLQNEKKQMELEHKRARIELEKKASA---LKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 680 vSFQDKEKEHLTRLQDAEEMKKALEQQM-ESHREAHQKQLS---------RLRDEIEEKQKIIDEIRDLNQKLQLEQEKL 749
Cdd:pfam05557 87 -ALNKKLNEKESQLADAREVISCLKNELsELRRQIQRAELElqstnseleELQERLDLLKAKASEAEQLRQNLEKQQSSL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 750 SSDYNKLKIEDQE-REMKLEKLLLLNDKREQAR-----EDLKGLEETVS--RELQTLHNLRKLFVQDLTTRVKKsVELDN 821
Cdd:pfam05557 166 AEAEQRIKELEFEiQSQEQDSEIVKNSKSELARipeleKELERLREHNKhlNENIENKLLLKEEVEDLKRKLER-EEKYR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 822 DDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEaKENAMRDrkrYQQEV 901
Cdd:pfam05557 245 EEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQ-LEKARRE---LEQEL 320
|
330 340
....*....|....*....|.
gi 4758650 902 DRIKEAVRAKNMARRAHSAQI 922
Cdd:pfam05557 321 AQYLKKIEDLNKKLKRHKALV 341
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
412-814 |
3.76e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 40.90 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRdyEKIQEELTRLQIENEAAKD-EVKEVLQA 490
Cdd:pfam09731 52 GEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKIPRQSGVSSEV--AEEEKEATKDAAEAKAQLPkSEQEKEKA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 491 LEELAvnyDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQElsnHQKKRATEILNLLLKDLGEiggiigtnDV 570
Cdd:pfam09731 130 LEEVL---KEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAE---ISREKATDSALQKAEALAE--------KL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 571 KTLADVNGVIEEEFTM-----ARLYISKMKSEVKSLVNR--SKQLESAQMDSNRKMNASERELAACQL-------LISQH 636
Cdd:pfam09731 196 KEVINLAKQSEEEAAPplldaAPETPPKLPEHLDNVEEKveKAQSLAKLVDQYKELVASERIVFQQELvsifpdiIPVLK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 637 EAKIKSLTDYMQNMEQKRRQLeesqDSLSEELAKLRAQEKMHEVSFQDKEKEHLtrlqdaEEMKKALEQQMESHREahqK 716
Cdd:pfam09731 276 EDNLLSNDDLNSLIAHAHREI----DQLSKKLAELKKREEKHIERALEKQKEEL------DKLAEELSARLEEVRA---A 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 717 QLSRLRDEIEEKQKIIDEirDLNQKLQLEQEKLSSDYNKlKIEDQEREMklekllllndKREQAREDLKGLEETVSRElq 796
Cdd:pfam09731 343 DEAQLRLEFEREREEIRE--SYEEKLRTELERQAEAHEE-HLKDVLVEQ----------EIELQREFLQDIKEKVEEE-- 407
|
410
....*....|....*...
gi 4758650 797 tlHNLRKLFVQDLTTRVK 814
Cdd:pfam09731 408 --RAGRLLKLNELLANLK 423
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
631-743 |
4.13e-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: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 631 LLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEmkkALEQQMESH 710
Cdd:pfam06785 76 KLTELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEE---QLAEKQLLI 152
|
90 100 110
....*....|....*....|....*....|...
gi 4758650 711 REaHQKQLSRLRDEIEEKQkiiDEIRDLNQKLQ 743
Cdd:pfam06785 153 NE-YQQTIEEQRSVLEKRQ---DQIENLESKVR 181
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
686-921 |
4.96e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.88 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 686 EKEHLTRLQDAEEMKKALEQQMESHREAHQKQlSRLRDEIEEKQKIIDEIRDLNQK---LQLEQEKLSSDYNKLKIEDQE 762
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQ-ERLRQEKEEKAREVERRRKLEEAekaRQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 763 REMKLEKLLLLNDKR--EQAREDLKGLEETVSRELQTLHNLRklfvQDLTTRVKKSVEldnddgggsAAQKQKIsfLEnn 840
Cdd:pfam17380 346 RERELERIRQEERKRelERIRQEEIAMEISRMRELERLQMER----QQKNERVRQELE---------AARKVKI--LE-- 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 841 lEQLTKVHKQLVRDNADLRCELPKLEKR--LRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAH 918
Cdd:pfam17380 409 -EERQRKIQQQKVEMEQIRAEQEEARQRevRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRK 487
|
...
gi 4758650 919 SAQ 921
Cdd:pfam17380 488 RAE 490
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
454-763 |
4.97e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 454 ELLASTRRdyeKIQEELTRLQI---ENEAAKDEVKEVLQALEELavnyDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQ 530
Cdd:PHA02562 146 QLSAPARR---KLVEDLLDISVlseMDKLNKDKIRELNQQIQTL----DMKIDHIQQQIKTYNKNIEEQRKKNGENIARK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 531 RE-----LSQLQELSNHQKKRATEILNLllkdlgeiggiigtndVKTLADVNGVIEEeFTMARlyiSKMKSEVKSLvnrS 605
Cdd:PHA02562 219 QNkydelVEEAKTIKAEIEELTDELLNL----------------VMDIEDPSAALNK-LNTAA---AKIKSKIEQF---Q 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 606 KQLesaqmdsnrKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLseelaklraQEKMHEVSFQDK 685
Cdd:PHA02562 276 KVI---------KMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDEL---------EEIMDEFNEQSK 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 686 EkehltrlqdAEEMKKALEQqmeshreaHQKQLSRLRDEIEEKQKIIDEIRDLN-------QKLQLEQEKLSSDYNKLKI 758
Cdd:PHA02562 338 K---------LLELKNKIST--------NKQSLITLVDKAKKVKAAIEELQAEFvdnaeelAKLQDELDKIVKTKSELVK 400
|
....*
gi 4758650 759 EDQER 763
Cdd:PHA02562 401 EKYHR 405
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
591-736 |
5.94e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.06 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 591 ISKMKSEVKSLVNRSKQLESAQmdsnrkmNASERELAAcQLLISQHEAKIKSLTDYMQNMEQKRRQ--------LEESQD 662
Cdd:PRK11637 98 LNQLNKQIDELNASIAKLEQQQ-------AAQERLLAA-QLDAAFRQGEHTGLQLILSGEESQRGErilayfgyLNQARQ 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4758650 663 SLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDaeemKKALEQQMESHREAHQKQLSRLRDEIEEKQKIIDEIR 736
Cdd:PRK11637 170 ETIAELKQTREELAAQKAELEEKQSQQKTLLYE----QQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELR 239
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
645-888 |
6.73e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.45 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 645 DYMQNMEQKRRQLEESQDSLSEelaklraQEKMHEVSFQDKEKehLTRLQDAEEMKKALEQQMESHREAHQKQLSRLRDE 724
Cdd:COG5022 872 QSAQRVELAERQLQELKIDVKS-------ISSLKLVNLELESE--IIELKKSLSSDLIENLEFKTELIARLKKLLNNIDL 942
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 725 IE------EKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVS------ 792
Cdd:COG5022 943 EEgpsieyVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKqlkelp 1022
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 793 RELQTLHNLRKlfvQDLTTRVKKSVELDnddgggsaAQKQKIsfleNNLEQLTKVHKQLVrdNADLRCELPKLEKRLRAT 872
Cdd:COG5022 1023 VEVAELQSASK---IISSESTELSILKP--------LQKLKG----LLLLENNQLQARYK--ALKLRRENSLLDDKQLYQ 1085
|
250
....*....|....*.
gi 4758650 873 AERVKALESALKEAKE 888
Cdd:COG5022 1086 LESTENLLKTINVKDL 1101
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
412-552 |
6.93e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 412 EEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQAL 491
Cdd:PRK04778 348 ESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKL 427
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4758650 492 EE------------LAVNYDQKSQEVEDKTranEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILN 552
Cdd:PRK04778 428 HEikryleksnlpgLPEDYLEMFFEVSDEI---EALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVE 497
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
648-852 |
7.61e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 648 QNMEQKRRQLEESQDSLSEELAKLR-----AQEKMHE-------VSFQDKEKEHLTRLQDAEEMKKALEQQM---ESHRE 712
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRkeleeAEAALEEfrqknglVDLSEEAKLLLQQLSELESQLAEARAELaeaEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 713 AHQKQLSRLRDEIEEK------QKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQERemklekLLLLNDKREQAREDLKG 786
Cdd:COG3206 244 ALRAQLGSGPDALPELlqspviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQI------AALRAQLQQEAQRILAS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758650 787 LEETVSRELQTLHNLRKLfVQDLTTRVKKsveldnddgggSAAQKQKISFLENNLEQLTKVHKQLV 852
Cdd:COG3206 318 LEAELEALQAREASLQAQ-LAQLEARLAE-----------LPELEAELRRLEREVEVARELYESLL 371
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
626-899 |
9.13e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 39.68 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 626 LAACQLLI--SQHEAKIKS-LTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKmhevsfqdkekehltrlqdaeemkkA 702
Cdd:PRK11637 29 LSAGVLLCafSAHASDNRDqLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEE-------------------------A 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 703 LEQQMESHREAhQKQLSRLRDEIEEkqkIIDEIRDLnQKLQLEQEKLSS----------DYNKLKI-----EDQEREMKL 767
Cdd:PRK11637 84 ISQASRKLRET-QNTLNQLNKQIDE---LNASIAKL-EQQQAAQERLLAaqldaafrqgEHTGLQLilsgeESQRGERIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758650 768 EKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDnddgGGSAAQKQKISFLENNLEqltKV 847
Cdd:PRK11637 159 AYFGYLNQARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLE----QARNERKKTLTGLESSLQ---KD 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 4758650 848 HKQLVrdnadlrcELPKLEKRLR---ATAERvKALESALKEAKEnAMRDRKRYQQ 899
Cdd:PRK11637 232 QQQLS--------ELRANESRLRdsiARAER-EAKARAEREARE-AARVRDKQKQ 276
|
|
| |
