|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
7-238 |
2.45e-145 |
|
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: 434.06 E-value: 2.45e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 7 ECSIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVVIG------------------------------------------- 43
Cdd:cd01369 1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIAtsetgktfsfdrvfdpnttqedvynfaakpivddvlngyngti 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 44 --------------------------------------------------VSYFEIYLDKIRDLLDVTKTNLSVHEDKNR 73
Cdd:cd01369 81 faygqtssgktytmegklgdpesmgiiprivqdifetiysmdenlefhvkVSYFEIYMEKIRDLLDVSKTNLSVHEDKNR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 74 VPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENMETEQKLSGKLYLVDLAGSEKVSKT 153
Cdd:cd01369 161 GPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEKVSKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 154 GAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQ 233
Cdd:cd01369 241 GAEGAVLDEAKKINKSLSALGNVINALTDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQ 320
|
....*
gi 1233951479 234 RAKTI 238
Cdd:cd01369 321 RAKTI 325
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
35-245 |
1.42e-98 |
|
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: 312.58 E-value: 1.42e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 35 QGDDSVVIGVSYFEIYLDKIRDLLDVTKTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSS 114
Cdd:smart00129 122 EEGWQFSVKVSYLEIYNEKIRDLLNPSSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESS 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 115 RSHSIFLINIKQE--NMETEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKS-YVPYR 191
Cdd:smart00129 202 RSHAVFTITVEQKikNSSSGSGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSrHIPYR 281
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1233951479 192 DSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTIKNTASVN 245
Cdd:smart00129 282 DSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
35-238 |
1.73e-97 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 309.12 E-value: 1.73e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 35 QGDDSVVIGVSYFEIYLDKIRDLLDVTKTN---LSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNE 111
Cdd:pfam00225 116 KERSEFSVKVSYLEIYNEKIRDLLSPSNKNkrkLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 112 HSSRSHSIFLINIKQENMET---EQKLSGKLYLVDLAGSEKVSKTG-AEGAVLDEAKNINKSLSALGNVISALAEGTKSY 187
Cdd:pfam00225 196 ESSRSHAIFTITVEQRNRSTggeESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKSKH 275
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1233951479 188 VPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTI 238
Cdd:pfam00225 276 IPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
37-236 |
6.24e-96 |
|
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: 305.33 E-value: 6.24e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 37 DDSVVIGVSYFEIYLDKIRDLLD-VTKTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSR 115
Cdd:cd00106 124 KSSFSVSASYLEIYNEKIYDLLSpVPKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSR 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 116 SHSIFLINIKQENMET--EQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDS 193
Cdd:cd00106 204 SHAVFTIHVKQRNREKsgESVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNKHIPYRDS 283
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1233951479 194 KMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAK 236
Cdd:cd00106 284 KLTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
42-240 |
3.12e-71 |
|
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: 239.03 E-value: 3.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 42 IGVSYFEIYLDKIRDLL---DVTKTNLSVHEDK-NRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSH 117
Cdd:cd01366 128 IKASMLEIYNETIRDLLapgNAPQKKLEIRHDSeKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSH 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 118 SIFLINIKQENMETEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGtKSYVPYRDSKMTR 197
Cdd:cd01366 208 SVFILHISGRNLQTGEISVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQK-QSHIPYRNSKLTY 286
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1233951479 198 ILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTIKN 240
Cdd:cd01366 287 LLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
28-238 |
1.81e-70 |
|
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: 236.46 E-value: 1.81e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 28 DKFIPIFQGDD-SVVIGVSYFEIYLDKIRDLLDVTKTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAV 106
Cdd:cd01374 106 DIFSKIQDTPDrEFLLRVSYLEIYNEKINDLLSPTSQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 107 TNMNEHSSRSHSIFLINIK---QENMETEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEG 183
Cdd:cd01374 186 TDMNERSSRSHTIFRITIEsseRGELEEGTVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEG 265
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1233951479 184 TKS-YVPYRDSKMTRILQDSLGGNCRTTMfIC-CSPSSYNDAETKSTLMFGQRAKTI 238
Cdd:cd01374 266 KVGgHIPYRDSKLTRILQPSLGGNSRTAI-ICtITPAESHVEETLNTLKFASRAKKI 321
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
41-239 |
3.82e-70 |
|
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: 236.46 E-value: 3.82e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 41 VIGVSYFEIYLDKIRDLLD---VTKTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSH 117
Cdd:cd01372 128 QLKVSFLEIYNEEIRDLLDpetDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSH 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 118 SIFLINIKQE----------NMETEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTK-- 185
Cdd:cd01372 208 AIFTITLEQTkkngpiapmsADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKkg 287
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1233951479 186 SYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTIK 239
Cdd:cd01372 288 AHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
39-245 |
2.32e-68 |
|
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.
Pssm-ID: 276816 [Multi-domain] Cd Length: 361 Bit Score: 232.24 E-value: 2.32e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 39 SVVIGVSYFEIYLDKIRDLLDVT----KTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSS 114
Cdd:cd01365 140 SYSVEVSYMEIYNEKVRDLLNPKpkknKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSS 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 115 RSHSIFLINIKQENMETEQKLSG----KLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE-------G 183
Cdd:cd01365 220 RSHAVFTIVLTQKRHDAETNLTTekvsKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADmssgkskK 299
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1233951479 184 TKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTIKNTASVN 245
Cdd:cd01365 300 KSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
35-238 |
1.43e-67 |
|
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: 229.27 E-value: 1.43e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 35 QGDDSVVIGVSYFEIYLDKIRDLL--DVTKtNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEH 112
Cdd:cd01371 127 QNNQQFLVRVSYLEIYNEEIRDLLgkDQTK-RLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNED 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 113 SSRSHSIFLINIKQENM--ETEQKLS-GKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVP 189
Cdd:cd01371 206 SSRSHAIFTITIECSEKgeDGENHIRvGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKSTHIP 285
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1233951479 190 YRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTI 238
Cdd:cd01371 286 YRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
37-238 |
4.97e-64 |
|
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: 219.52 E-value: 4.97e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 37 DDSVVIGVSYFEIYLDKIRDLLDVTKTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRS 116
Cdd:cd01370 139 EKEFEVSMSYLEIYNETIRDLLNPSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRS 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 117 HSIFLINIKQEN---METEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKS--YVPYR 191
Cdd:cd01370 219 HAVLQITVRQQDktaSINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKnkHIPYR 298
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1233951479 192 DSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTI 238
Cdd:cd01370 299 DSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
37-463 |
3.25e-57 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 207.28 E-value: 3.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 37 DDSVVIGVSYFEIYLDKIRDLLDVTKTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRS 116
Cdd:COG5059 134 TKDFAVSISYLEIYNEKIYDLLSPNEESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 117 HSIFLINIKQENMETEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSY-VPYRDSKM 195
Cdd:COG5059 214 HSIFQIELASKNKVSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSGhIPYRESKL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 196 TRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTIKNTASVNleltaeqwkkkyekekeKTKAQKETIAKLE 275
Cdd:COG5059 294 TRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVN-----------------SSSDSSREIEEIK 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 276 AELSRWRNGENVpeterlageeaalgaelceetPVNDNSSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQ-SQLIE 354
Cdd:COG5059 357 FDLSEDRSEIEI---------------------LVFREQSQLSQSSLSGIFAYMQSLKKETETLKSRIDLIMKSiISGTF 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 355 KLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEK---SQQNQLLVDELS 431
Cdd:COG5059 416 ERKKLLKEEGWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDLSSLLSSIPEETSDrveSEKASKLRSSAS 495
|
410 420 430
....*....|....*....|....*....|..
gi 1233951479 432 QKVATMlSLESELQRLQEVSGHQRKRIAEVLN 463
Cdd:COG5059 496 TKLNLR-SSRSHSKFRDHLNGSNSSTKELSLN 526
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
44-245 |
1.18e-56 |
|
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: 199.47 E-value: 1.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 44 VSYFEIYLDKIRDLL---DVTKTNLSVHEDKNRVP--FVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHS 118
Cdd:cd01364 143 VSYLEIYNEELFDLLspsSDVSERLRMFDDPRNKRgvIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHS 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 119 IFLI--NIKQENMETEQKLS-GKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEgTKSYVPYRDSKM 195
Cdd:cd01364 223 VFSItiHIKETTIDGEELVKiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE-RAPHVPYRESKL 301
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1233951479 196 TRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTIKNTASVN 245
Cdd:cd01364 302 TRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVN 351
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
45-245 |
1.76e-56 |
|
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: 198.89 E-value: 1.76e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 45 SYFEIYLDKIRDLLDVTKTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINI 124
Cdd:cd01373 139 SFLEIYNEQIYDLLDPASRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTI 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 125 kqENMETEQKLS----GKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE---GTKSYVPYRDSKMTR 197
Cdd:cd01373 219 --ESWEKKACFVnirtSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvahGKQRHVCYRDSKLTF 296
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1233951479 198 ILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTIKNTASVN 245
Cdd:cd01373 297 LLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVN 344
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
44-236 |
1.12e-48 |
|
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: 176.23 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 44 VSYFEIYLDKIRDLLDVTK------TNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSH 117
Cdd:cd01375 134 VSYLEIYNEQLYDLLSTLPyvgpsvTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSH 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 118 SIFLINI--KQENMETEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKM 195
Cdd:cd01375 214 CIFTIHLeaHSRTLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDRTHVPFRQSKL 293
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1233951479 196 TRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAK 236
Cdd:cd01375 294 THVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
42-236 |
5.35e-48 |
|
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: 174.50 E-value: 5.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 42 IGVSYFEIYLDKIRDLLDVT-------KTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSS 114
Cdd:cd01368 132 VFVSYIEIYNEYIYDLLEPSpssptkkRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 115 RSHSIFLINI--------KQENMETEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE---- 182
Cdd:cd01368 212 RSHSVFTIKLvqapgdsdGDVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLREnqlq 291
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1233951479 183 GTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAK 236
Cdd:cd01368 292 GTNKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
44-236 |
2.33e-46 |
|
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: 168.84 E-value: 2.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 44 VSYFEIYLDKIRDLLDVTKTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLIN 123
Cdd:cd01376 127 MSYLEIYQEKILDLLEPASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIK 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 124 -IKQENMETEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTkSYVPYRDSKMTRILQDS 202
Cdd:cd01376 207 vDQRERLAPFRQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNL-PRIPYRDSKLTRLLQDS 285
|
170 180 190
....*....|....*....|....*....|....
gi 1233951479 203 LGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAK 236
Cdd:cd01376 286 LGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
30-236 |
1.98e-42 |
|
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: 157.84 E-value: 1.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 30 FIPIFQGDDSVVIGVSYFEIYLDKIRDLLDvTKTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNM 109
Cdd:cd01367 125 LLNKLPYKDNLGVTVSFFEIYGGKVFDLLN-RKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSA 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 110 NEHSSRSHSIFLINIKQENmetEQKLSGKLYLVDLAGSEKVSKTGAEGA-VLDEAKNINKSLSALGNVISALAEGtKSYV 188
Cdd:cd01367 204 NSQSSRSHAILQIILRDRG---TNKLHGKLSFVDLAGSERGADTSSADRqTRMEGAEINKSLLALKECIRALGQN-KAHI 279
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1233951479 189 PYRDSKMTRILQDSL-GGNCRTTMFICCSPSSYNDAETKSTLMFGQRAK 236
Cdd:cd01367 280 PFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADRVK 328
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
45-248 |
3.69e-41 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 164.72 E-value: 3.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 45 SYFEIYLDKIRDLLDVTKTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINI 124
Cdd:PLN03188 233 SFLEIYNEQITDLLDPSQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVV 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 125 KQENMETEQKLSG----KLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAE----GTKSYVPYRDSKMT 196
Cdd:PLN03188 313 ESRCKSVADGLSSfktsRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtGKQRHIPYRDSRLT 392
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1233951479 197 RILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTIKNTASVNLEL 248
Cdd:PLN03188 393 FLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVM 444
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
12-217 |
1.17e-25 |
|
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: 104.35 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 12 VLCRFRPLNQAEILRGDKFIPIFQGDDSVVIGVSYFEIYLDKIRDLLD--------------------------VTKTNL 65
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIVFYRGFRRSESQPHVFAIADPAYQSMLDgynnqsifaygesgagktetmkgvipYLASVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 66 SVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRhVAVTNMNEHSSRSHSIFLInikqenmeteqklsgklyLVDLA 145
Cdd:cd01363 81 FNGINKGETEGWVYLTEITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------------LLDIA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1233951479 146 GSEkvsktgaegavldeakNINKSLSALGNVISAlaegtksyvpyrdskmtrilqdslggnCRTTMFICCSP 217
Cdd:cd01363 142 GFE----------------IINESLNTLMNVLRA---------------------------TRPHFVRCISP 170
|
|
| Khc_CBD_cc |
cd23649 |
cargo binding coiled-coil domain found in kinesin heavy chains; The family includes Drosophila ... |
743-812 |
3.94e-23 |
|
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: 93.42 E-value: 3.94e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 743 FLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIK 812
Cdd:cd23649 1 FLERNLEQLTLVQKQLVRQNSTLKKELALAEKKLAARNERIKSLEALLKEAQEKLEKQNQKFEEQLQRLR 70
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
320-831 |
1.22e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 320 IAPEERQKYEE--EIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKD--EV 395
Cdd:PRK03918 212 ISSELPELREEleKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 396 KEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEV-------------- 461
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELeerhelyeeakakk 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 462 --LNGLMKDLSEFSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVEChrkmEVTGRELSS 539
Cdd:PRK03918 372 eeLERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC----PVCGRELTE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 540 CQL--LISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVA--LKDKEPDTQ--DADEVKKALELQ 613
Cdd:PRK03918 448 EHRkeLLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAeqLKELEEKLKkyNLEELEKKAEEY 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 614 MESHREahhrqLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEH-----------EKSTKLQELTFLYE 682
Cdd:PRK03918 528 EKLKEK-----LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKeleelgfesveELEERLKELEPFYN 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 683 RH---EQSKQDLKGLEETVARELQTLHNLRKLFvqDVTTRVKKSAEMEPEDSGGIHSQKQkisflennLEQLTKVHKQLV 759
Cdd:PRK03918 603 EYlelKDAEKELEREEKELKKLEEELDKAFEEL--AETEKRLEELRKELEELEKKYSEEE--------YEELREEYLELS 672
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1233951479 760 RDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKR--RYQQEVDRIKEAVR-YKSSGKRGHSAQIAK 831
Cdd:PRK03918 673 RELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKleKALERVEELREKVKkYKALLKERALSKVGE 747
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
406-751 |
3.69e-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: 67.39 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 406 AVNYDQKSQEVEEKSQQNQLLVDELSQKVATmlsLESELQRLQEVSGHQRKRIAEvlnglmkdlsefsvivgngeiklpv 485
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAE---LRKELEELEEELEQLRKELEE------------------------- 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 486 eisgaIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQ------ 559
Cdd:TIGR02168 724 -----LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEqlkeel 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 560 -SVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREahhrQLARLRDEINEKQKT 638
Cdd:TIGR02168 799 kALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA----EIEELEELIEELESE 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 639 IDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLY----ERHEQSKQDLKGLEETVARELQTLHNLRKLFVQ 714
Cdd:TIGR02168 875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELeelrEKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE 954
|
330 340 350
....*....|....*....|....*....|....*..
gi 1233951479 715 DVttrvkksAEMEPEDSGGIHSQKQKISFLENNLEQL 751
Cdd:TIGR02168 955 EA-------EALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
329-662 |
5.10e-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: 67.00 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 329 EEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELavn 408
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA--- 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 409 yDQKSQEVEEKSQQNQLLVDELSQKVATmlsLESELQRLQEVSGHQRKRIAEVLNGLMKDLSEfsvivgngeiklpveiS 488
Cdd:TIGR02168 774 -EEELAEAEAEIEELEAQIEQLKEELKA---LREALDELRAELTLLNEEAANLRERLESLERR----------------I 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 489 GAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHL 568
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 569 EESYDSLSDELAKLQAQETVHEVALKDKEP----DTQDADEVKKALELQMESHREAHHRQLARLRDEINE----KQKTID 640
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLQErlseEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvNLAAIE 993
|
330 340
....*....|....*....|..
gi 1233951479 641 ELKDLNQKLQlELEKLQADYEK 662
Cdd:TIGR02168 994 EYEELKERYD-FLTAQKEDLTE 1014
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
348-678 |
7.73e-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: 66.23 E-value: 7.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 348 QQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLV 427
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 428 DELSQKVATMLSLESELQRLQEVSGHQRKRIAEVlnglmkdlsefsvivgngeiklpveisgaiEEEFTVARLYISKIKS 507
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEEL------------------------------EAQIEQLKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 508 EVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQET 587
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 588 VHEVALKDKEPDTQDADEVKKALELQMESHREAHHR---QLARLRDEINEKQKTIDELKD-LNQKLQLELEKLQADYEKL 663
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEElreKLAQLELRLEGLEVRIDNLQErLSEEYSLTLEEAEALENKI 963
|
330
....*....|....*
gi 1233951479 664 KSEEHEKSTKLQELT 678
Cdd:TIGR02168 964 EDDEEEARRRLKRLE 978
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
546-816 |
9.13e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 9.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 546 QHEAKIRSLTEYMqsveLKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREA---HH 622
Cdd:COG1196 219 KEELKELEAELLL----LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyeLL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 623 RQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTflyERHEQSKQDLKGLEETVAREL 702
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE---EELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 703 QTLHNLRKLFVQdvttrvKKSAEMEPEdsggihsqkQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAER 782
Cdd:COG1196 372 AELAEAEEELEE------LAEELLEAL---------RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
250 260 270
....*....|....*....|....*....|....
gi 1233951479 783 VKALEGALKEAKEGAMKDKRRYQQEVDRIKEAVR 816
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
393-814 |
9.86e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.86 E-value: 9.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 393 DEVKEvlQALEELAvnydqksqEVEEKSQQNQLLVDELSQkvatmlslesELQRLQEvsghqRKRIAEVLNGLMKDLSEF 472
Cdd:TIGR02169 169 DRKKE--KALEELE--------EVEENIERLDLIIDEKRQ----------QLERLRR-----EREKAERYQALLKEKREY 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 473 SVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTG--------RELSSCQLLI 544
Cdd:TIGR02169 224 EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGeeeqlrvkEKIGELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 545 SQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQaqETVHEVAlKDKEPDTQDADEVKKALELqmeshreahhrq 624
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE--REIEEER-KRRDKLTEEYAELKEELED------------ 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 625 larLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTflyERHEQSKQDLKGLEETVArELQT 704
Cdd:TIGR02169 369 ---LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS---EELADLNAAIAGIEAKIN-ELEE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 705 lhnlrklfvqdvttrVKKSAEMEpedsggIHSQKQKisfLENNLEQLTKVHKQLVRDNADLRcelpKLEKRLRAtaervK 784
Cdd:TIGR02169 442 ---------------EKEDKALE------IKKQEWK---LEQLAADLSKYEQELYDLKEEYD----RVEKELSK-----L 488
|
410 420 430
....*....|....*....|....*....|
gi 1233951479 785 ALEGALKEAKEGAMKDKRRYQQEVDRIKEA 814
Cdd:TIGR02169 489 QRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
323-795 |
1.01e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 323 EERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQAL 402
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 403 EELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRL-QEVSGHQRKRIAEVLNGLMKDLSEFSVIVGNGEI 481
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqQEIEELLKKLEEAELKELQAELEELEEELEELQE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 482 KLP--VEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQvECHRKMEVTGRELSSCQLLISQH------------ 547
Cdd:TIGR02168 455 ELErlEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ-ENLEGFSEGVKALLKNQSGLSGIlgvlselisvde 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 548 --EAKI-------------RSLTEYMQSVELKKRH-----------LEESYDSLSDELAKLQAQETVHEVALKDKEPDTQ 601
Cdd:TIGR02168 534 gyEAAIeaalggrlqavvvENLNAAKKAIAFLKQNelgrvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPK 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 602 D-------------ADEVKKALELQMESHRE-----------------------------AHHRQLARLRDEINEKQKTI 639
Cdd:TIGR02168 614 LrkalsyllggvlvVDDLDNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssilERRREIEELEEKIEELEEKI 693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 640 DELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDlkgLEETVARELQTLHNLRKLFVQdVTTR 719
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ---LEERIAQLSKELTELEAEIEE-LEER 769
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 720 VKKSAEMEPEDSGGIHSQKQKISFLENNLEQLT-------KVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKE 792
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALRealdelrAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
...
gi 1233951479 793 AKE 795
Cdd:TIGR02168 850 LSE 852
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
491-792 |
1.05e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 491 IEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEE 570
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 571 SYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQ----------LARLRDEINEKQKTID 640
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeaanlrerLESLERRIAATERRLE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 641 ELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNlrklfvqdvtTRV 720
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES----------KRS 911
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1233951479 721 KKSAEMEpEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELP-KLEKRLRATAERVKALEGALKE 792
Cdd:TIGR02168 912 ELRRELE-ELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEnKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
353-793 |
2.13e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 353 IEKLKQQMLDQEELLVSTRGDNEKVQrelshlqsenDAAKdEVKEVLQALE---ELAVNYDQKSQEVEEKsqQNQLLVDE 429
Cdd:TIGR02168 167 ISKYKERRKETERKLERTRENLDRLE----------DILN-ELERQLKSLErqaEKAERYKELKAELREL--ELALLVLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 430 LSQKVATMLSLESELQRLQevsgHQRKRIAEVLNGLMKDLSEFSVIVGNGEIKLpveisGAIEEEFTVARLYISKIKSEV 509
Cdd:TIGR02168 234 LEELREELEELQEELKEAE----EELEELTAELQELEEKLEELRLEVSELEEEI-----EELQKELYALANEISRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 510 KSVVKRCRQLENLQVEchrkmevtgrelsscqllisqheakirsLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVH 589
Cdd:TIGR02168 305 QILRERLANLERQLEE----------------------------LEAQLEELESKLDELAEELAELEEKLEELKEELESL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 590 EVALKDKEPDTQDADEVKKALELQMESHREAhhrqLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADyeklkSEEHE 669
Cdd:TIGR02168 357 EAELEELEAELEELESRLEELEEQLETLRSK----VAQLELQIASLNNEIERLEARLERLEDRRERLQQE-----IEELL 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 670 KSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVTTRVKKSAEMEpEDSGGIHSQKQkisfLENNLE 749
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA-QLQARLDSLER----LQENLE 502
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1233951479 750 QLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEA 793
Cdd:TIGR02168 503 GFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGR 546
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
322-696 |
1.82e-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: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 322 PEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEellvstrgdnekvqRELSHLQSENDAAKDEVKEVLQA 401
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAS--------------RKIGEIEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 402 LEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIaevlnglmkdlsefsvivgngei 481
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPE----------------------- 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 482 klpveisgaIEEEftvarlyISKIKSEVKSVVKRCRQLEnlqvechrkmevtgRELSSCQLLISQHEAKIRSLTEYMQSV 561
Cdd:TIGR02169 796 ---------IQAE-------LSKLEEEVSRIEARLREIE--------------QKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 562 ELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEpdtqdadEVKKALELQMESHrEAHHRQLARLRDEINEK-QKTID 640
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE-------SRLGDLKKERDEL-EAQLRELERKIEELEAQiEKKRK 917
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1233951479 641 ELKDLNQKLQLELEKLqADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEE 696
Cdd:TIGR02169 918 RLSELKAKLEALEEEL-SEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEP 972
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
323-801 |
2.36e-09 |
|
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: 61.29 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 323 EERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQAL 402
Cdd:pfam15921 335 EAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 403 EELAVNYDQKSQEVEEKSQQNQLLVDELS-QKVATMLSLESELQRLQEVSG--HQRKRIAEVLNGLMKDLSEFSVIVGNG 479
Cdd:pfam15921 415 DHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSSltAQLESTKEMLRKVVEELTAKKMTLESS 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 480 EiKLPVEISGAIEEE---FTVARLYISKIKS-------EVKSVVKRCRQLENLQVECHR-KMEVTGRElSSCQLLISQHE 548
Cdd:pfam15921 495 E-RTVSDLTASLQEKeraIEATNAEITKLRSrvdlklqELQHLKNEGDHLRNVQTECEAlKLQMAEKD-KVIEILRQQIE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 549 AKIRSLTEYMQS---VELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDadevkkaLELQMESHREAHHRQL 625
Cdd:pfam15921 573 NMTQLVGQHGRTagaMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD-------LELEKVKLVNAGSERL 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 626 ARLRDEINEKQKTIDELKDLNQklqlELEKLQADYEKL------KSEEHEKST-KLQ-ELTFLYERHEQSKQDLKGLEET 697
Cdd:pfam15921 646 RAVKDIKQERDQLLNEVKTSRN----ELNSLSEDYEVLkrnfrnKSEEMETTTnKLKmQLKSAQSELEQTRNTLKSMEGS 721
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 698 VARELQTLHNLRKlfvqDVTTRvkksaemepedSGGIHSQKQKISFLEnnlEQLTKVHKQlvrdNADLRCELPKLEKRLR 777
Cdd:pfam15921 722 DGHAMKVAMGMQK----QITAK-----------RGQIDALQSKIQFLE---EAMTNANKE----KHFLKEEKNKLSQELS 779
|
490 500
....*....|....*....|....*.
gi 1233951479 778 ATAERVKALEGALK--EAKEGAMKDK 801
Cdd:pfam15921 780 TVATEKNKMAGELEvlRSQERRLKEK 805
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
323-817 |
9.11e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 9.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 323 EERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQAL 402
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 403 EELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLMKDLSEfsvivgngEIK 482
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER--------LER 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 483 LPVEISGAIEEEFTVARLyISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELsscqlliSQHEAKIRSLTEYMQSVE 562
Cdd:COG1196 419 LEEELEELEEALAELEEE-EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA-------ALLEAALAELLEELAEAA 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 563 LKKRHLEESYDSLSDELAklQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQLARLRDEINEKQktIDEL 642
Cdd:COG1196 491 ARLLLLLEAEADYEGFLE--GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAA--IEYL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 643 KDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFL-YERHEQSKQDLKGLEETVARELQT--LHNLRKLFVQDVTTR 719
Cdd:COG1196 567 KAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVaSDLREADARYYVLGDTLLGRTLVAarLEAALRRAVTLAGRL 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 720 VKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMK 799
Cdd:COG1196 647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
|
490
....*....|....*...
gi 1233951479 800 DKRRYQQEVDRIKEAVRY 817
Cdd:COG1196 727 EEQLEAEREELLEELLEE 744
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
548-795 |
2.29e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 548 EAKIRSLTEYMQSVELKKRHLEESYDSLsdelaKLQAQETVHEVALKDKEPDTQ------DADEVKKALElQMESHREAH 621
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELERQLKSL-----ERQAEKAERYKELKAELRELElallvlRLEELREELE-ELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 622 HRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTflyERHEQSKQDLKGLEETVARE 701
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR---ERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 702 LQTLHNLRKLF--VQDVTTRVKKSAEMEPEDsggIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRAT 779
Cdd:TIGR02168 329 ESKLDELAEELaeLEEKLEELKEELESLEAE---LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
250
....*....|....*.
gi 1233951479 780 AERVKALEGALKEAKE 795
Cdd:TIGR02168 406 EARLERLEDRRERLQQ 421
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
327-792 |
2.32e-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: 58.06 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 327 KYEEEIRRLyKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELA 406
Cdd:TIGR00618 294 PLAAHIKAV-TQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISC 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 407 vnyDQKSQEVEEKSQQNQLLVDELSQKvatmlSLESELQRLQEVSGHQRKRIAEvLNGLMKDLsefsvIVGNGEIKLPVE 486
Cdd:TIGR00618 373 ---QQHTLTQHIHTLQQQKTTLTQKLQ-----SLCKELDILQREQATIDTRTSA-FRDLQGQL-----AHAKKQQELQQR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 487 ISG----AIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQsve 562
Cdd:TIGR00618 439 YAElcaaAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNP--- 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 563 lkkrHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAHhrQLARLRDEINEKQKTIDEL 642
Cdd:TIGR00618 516 ----ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ--SFSILTQCDNRSKEDIPNL 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 643 KDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQdlkgLEETVARELQTLHNLRKLFVQDVTTRVKK 722
Cdd:TIGR00618 590 QNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQ----CSQELALKLTALHALQLTLTQERVREHAL 665
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 723 SAEMEPEDSGGIHSQKQKisFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKE 792
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQ--KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSD 733
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
323-698 |
2.61e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 323 EERQKYEEEIRRLYKQLDDKDdeinqqsQLIEKLKQQMldqeellvstrgdnEKVQRELSHlqsendaaKDEVKEVLQAL 402
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLD-------LIIDEKRQQL--------------ERLRREREK--------AERYQALLKEK 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 403 EELavnydqksqEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEvLNGLMKDLSEfsvivgngeik 482
Cdd:TIGR02169 221 REY---------EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEE-IEQLLEELNK----------- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 483 lpvEISGAIEEEftvarlyISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVE 562
Cdd:TIGR02169 280 ---KIKDLGEEE-------QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 563 LKKRHLEESYDSLSDELAKLQAQ---------ETVHEVA--------LKDKEPDTQDADEVKKALELQMESHREAHHRQL 625
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAEleevdkefaETRDELKdyreklekLKREINELKRELDRLQEELQRLSEELADLNAAI 429
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1233951479 626 ARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTflyERHEQSKQDLKGLEETV 698
Cdd:TIGR02169 430 AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE---KELSKLQRELAEAEAQA 499
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
330-678 |
4.18e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 57.34 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 330 EEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNY 409
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 410 DQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEvlngLMKDLSEFSVIVGNGEIKlpveiSG 489
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD----LTNQDSVKELIIKNLDNT-----RE 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 490 AIEEEFTVARLYISKIKSEvksvvkrcrqLENLQVEchrkmevtgrelsscqllISQHEAKIRSLTEYMQSVELKKRHLE 569
Cdd:TIGR04523 465 SLETQLKVLSRSINKIKQN----------LEQKQKE------------------LKSKEKELKKLNEEKKELEEKVKDLT 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 570 ESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQmeshreahhRQLARLRDEINEKQKTIDELKDLNQKL 649
Cdd:TIGR04523 517 KKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLE---------KEIDEKNKEIEELKQTQKSLKKKQEEK 587
|
330 340
....*....|....*....|....*....
gi 1233951479 650 QLELEKLQADYEKLKSEEHEKSTKLQELT 678
Cdd:TIGR04523 588 QELIDQKEKEKKDLIKEIEEKEKKISSLE 616
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
325-828 |
7.24e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.67 E-value: 7.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 325 RQKYEEEIRRLYKQLDDKDDEINQQSQLIEK----LKQQMLDqeellvstrgdnekVQRELSHLQSENDAAKDEVKEVLQ 400
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKqkfyLRQSVID--------------LQTKLQEMQMERDAMADIRRRESQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 401 ALEELAVNYDQKSQEVE-EKSQQNQLLVD---ELSQKVATMLSLESELQRL-------QEVSGhqrKRIAEVLNGLMKDL 469
Cdd:pfam15921 139 SQEDLRNQLQNTVHELEaAKCLKEDMLEDsntQIEQLRKMMLSHEGVLQEIrsilvdfEEASG---KKIYEHDSMSTMHF 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 470 SEFSVIVGNGEIKLPVEISgaieeeFTVARLYISKiksevksvvkrcRQLENLQVECHRKMEVTGRELSS-CQLLISQHE 548
Cdd:pfam15921 216 RSLGSAISKILRELDTEIS------YLKGRIFPVE------------DQLEALKSESQNKIELLLQQHQDrIEQLISEHE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 549 AKIRSLTEYMQSVELKKRHLEESYDSLSDElakLQAQETVHEVALKDKEPD-TQDADEVKKALELqMESHREAHHRQLAR 627
Cdd:pfam15921 278 VEITGLTEKASSARSQANSIQSQLEIIQEQ---ARNQNSMYMRQLSDLESTvSQLRSELREAKRM-YEDKIEELEKQLVL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 628 LRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKlksEEHEKSTKLQELTFLYERHEQSKQDLKGLEetvaRELQTlhn 707
Cdd:pfam15921 354 ANSELTEARTERDQFSQESGNLDDQLQKLLADLHK---REKELSLEKEQNKRLWDRDTGNSITIDHLR----RELDD--- 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 708 lRKLFVQDVTTRVKKsaeMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRC---ELPKLEKRLRATAERVK 784
Cdd:pfam15921 424 -RNMEVQRLEALLKA---MKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKvveELTAKKMTLESSERTVS 499
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1233951479 785 ALEGALKE---AKEGAMKDKRRYQQEVD-RIKEAVRYKSSGKRGHSAQ 828
Cdd:pfam15921 500 DLTASLQEkerAIEATNAEITKLRSRVDlKLQELQHLKNEGDHLRNVQ 547
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
314-820 |
9.94e-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: 56.13 E-value: 9.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 314 SSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEEllvstrgdNEKVQRELSHLQSENDAAKD 393
Cdd:TIGR00618 203 SQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEE--------QLKKQQLLKQLRARIEELRA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 394 EVKEVLQALEEL-----AVNYDQKSQEVEEKSQQNQLLVDELSQKvatMLSLESELQRLQEVSgHQRKRIAEVLNGLMKD 468
Cdd:TIGR00618 275 QEAVLEETQERInrarkAAPLAAHIKAVTQIEQQAQRIHTELQSK---MRSRAKLLMKRAAHV-KQQSSIEEQRRLLQTL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 469 LSEfsvivgNGEIKLPVEISGAIEEEFTVARLYISKIKS--EVKSVVKR-----CRQLENLQVECHRKMEVTGREL---- 537
Cdd:TIGR00618 351 HSQ------EIHIRDAHEVATSIREISCQQHTLTQHIHTlqQQKTTLTQklqslCKELDILQREQATIDTRTSAFRdlqg 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 538 ------SSCQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALE 611
Cdd:TIGR00618 425 qlahakKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPC 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 612 LQMESHREAH-HRQLA--------RLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEkstkLQELTFLYE 682
Cdd:TIGR00618 505 PLCGSCIHPNpARQDIdnpgpltrRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS----FSILTQCDN 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 683 RHEQSKQDLKGLEETVARELQTLHNLRKLfvqdvttrvKKSAEMEPEDSGGIHSQKQKISFLENNLEQ---LTKVHKqlv 759
Cdd:TIGR00618 581 RSKEDIPNLQNITVRLQDLTEKLSEAEDM---------LACEQHALLRKLQPEQDLQDVRLHLQQCSQelaLKLTAL--- 648
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1233951479 760 rdnADLRCELPKLEKRLRATAERV-KALEGALKEAKEGAMKDKRryqQEVDRIKEAVRYKSS 820
Cdd:TIGR00618 649 ---HALQLTLTQERVREHALSIRVlPKELLASRQLALQKMQSEK---EQLTYWKEMLAQCQT 704
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
579-834 |
1.58e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 579 LAKLQAQETVHEVALKDKEPDTQDADEVKKALElQMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQA 658
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELA-ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 659 DYEKLKSEEHEKSTKLQE-LTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDvttrvKKSAEmepedsgGIHSQ 737
Cdd:COG4942 91 EIAELRAELEAQKEELAElLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPAR-----REQAE-------ELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 738 KQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRI-----K 812
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLeaeaaA 238
|
250 260
....*....|....*....|..
gi 1233951479 813 EAVRYKSSGKRGHSAQIAKPVR 834
Cdd:COG4942 239 AAERTPAAGFAALKGKLPWPVS 260
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
490-727 |
1.64e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 490 AIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLE 569
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 570 ESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKL 649
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1233951479 650 QLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVTTRVKKSAEME 727
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
270-816 |
1.95e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 270 TIAKLEAELSRWRN--GENVPETERLAGEEAALGAELCEETPVNDnsSIVVRIAPEER--QKYEEEIRRLYKQLDDKDDE 345
Cdd:TIGR02169 323 RLAKLEAEIDKLLAeiEELEREIEEERKRRDKLTEEYAELKEELE--DLRAELEEVDKefAETRDELKDYREKLEKLKRE 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 346 IN----QQSQLIEKLKQQMLDQEELlvstRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQ 421
Cdd:TIGR02169 401 INelkrELDRLQEELQRLSEELADL----NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 422 QNQLLVDELSQKVATMLSLESELQRLQEVSGHqRKRIAEVLN-------GLMKDLsefsvivgngeIKLPVEISGAIEee 494
Cdd:TIGR02169 477 EYDRVEKELSKLQRELAEAEAQARASEERVRG-GRAVEEVLKasiqgvhGTVAQL-----------GSVGERYATAIE-- 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 495 fTVARLYISKIKSEVKSVVKRC------RQLENLQVECHRKMEVTGRELSSCQL---------LIsQHEAKIRSLTEY-- 557
Cdd:TIGR02169 543 -VAAGNRLNNVVVEDDAVAKEAiellkrRKAGRATFLPLNKMRDERRDLSILSEdgvigfavdLV-EFDPKYEPAFKYvf 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 558 -----MQSVELKKRHLEE-SYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEvkkalELQMESHR-EAHHRQLARLRD 630
Cdd:TIGR02169 621 gdtlvVEDIEAARRLMGKyRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPA-----ELQRLRERlEGLKRELSSLQS 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 631 EINEKQKTIDELKDLNQ-------KLQLELEKLQADYEKLKSEEHEKSTKLQELTflyERHEQSKQDLKGLEETVARELQ 703
Cdd:TIGR02169 696 ELRRIENRLDELSQELSdasrkigEIEKEIEQLEQEEEKLKERLEELEEDLSSLE---QEIENVKSELKELEARIEELEE 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 704 TLHNLRKL-----------FVQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADL------- 765
Cdd:TIGR02169 773 DLHKLEEAlndlearlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqiksi 852
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1233951479 766 RCELPKLEKRLRATAERVKALEGALKE---AKEGAMKDKRRYQQEVDRIKEAVR 816
Cdd:TIGR02169 853 EKEIENLNGKKEELEEELEELEAALRDlesRLGDLKKERDELEAQLRELERKIE 906
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
586-722 |
5.58e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 53.32 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 586 ETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKS 665
Cdd:COG2433 376 LSIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARS 455
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 666 EEHEKSTKLQELTFLYERHEQSKQDLKGLEETV---ARELQTLHNLRKLFVQDVTTRVKK 722
Cdd:COG2433 456 EERREIRKDREISRLDREIERLERELEEERERIeelKRKLERLKELWKLEHSGELVPVKV 515
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
323-462 |
1.56e-06 |
|
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: 50.31 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 323 EERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNE--KVQRELSHLQSENDAAKDEVKEVLQ 400
Cdd:COG1579 38 DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyeALQKEIESLKRRISDLEDEILELME 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1233951479 401 ALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATmlsLESELQRLQEvsghQRKRIAEVL 462
Cdd:COG1579 118 RIEELEEELAELEAELAELEAELEEKKAELDEELAE---LEAELEELEA----EREELAAKI 172
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
323-664 |
1.62e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 323 EERQKYEEEIRRL------YKQLDDKDDEINQQSQLIEKLKQQMLDQEELL-VSTRGDNEKVQRELSHLQSENDAAKDEV 395
Cdd:COG4717 136 ALEAELAELPERLeeleerLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEEL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 396 KEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKV-ATMLSLESELQRLQEVSGHQRKRIAEVL-----NGLMKDL 469
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIaAALLALLGLGGSLLSLILTIAGVLFLVLgllalLFLLLAR 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 470 SEFSVIVGNGEIKLPVEISG----AIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEvtgrelsscQLLIS 545
Cdd:COG4717 296 EKASLGKEAEELQALPALEEleeeELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE---------ELQLE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 546 QHEAKIRSLTEYMQSVEL----KKRHLEESYDSLSDELAKLQAQ------ETVHEVALKDKEPDTQDADEVKKALElQME 615
Cdd:COG4717 367 ELEQEIAALLAEAGVEDEeelrAALEQAEEYQELKEELEELEEQleellgELEELLEALDEEELEEELEELEEELE-ELE 445
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1233951479 616 SHREAHHRQLARLRDEIN--EKQKTIDELKDLNQKLQLELEKLQADYEKLK 664
Cdd:COG4717 446 EELEELREELAELEAELEqlEEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
284-708 |
2.42e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.51 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 284 GENVPETERLAGEEAALGAELCEETPVNdnssivvRIAPEERQKYEEEIRRLyKQLDDKDDEINQQSQLIEKLKQQMLDQ 363
Cdd:TIGR00618 431 KQQELQQRYAELCAAAITCTAQCEKLEK-------IHLQESAQSLKEREQQL-QTKEQIHLQETRKKAVVLARLLELQEE 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 364 EELLV-STRGDNEKVQR--ELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKV------ 434
Cdd:TIGR00618 503 PCPLCgSCIHPNPARQDidNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTqcdnrs 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 435 -ATMLSLESELQRLQ----EVSGHQRKRIAEVLNGLMK-----DLSEFSVIVGNGEIKLPVEISG--AIEEEFTVARLYI 502
Cdd:TIGR00618 583 kEDIPNLQNITVRLQdlteKLSEAEDMLACEQHALLRKlqpeqDLQDVRLHLQQCSQELALKLTAlhALQLTLTQERVRE 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 503 SKIKSEVKSVVKRCRQLENLQVECHRKMEVTG--RELSSCQLLISQHEAKIRSLTEYMQSVEL----KKRHLEESYDSLS 576
Cdd:TIGR00618 663 HALSIRVLPKELLASRQLALQKMQSEKEQLTYwkEMLAQCQTLLRELETHIEEYDREFNEIENasssLGSDLAAREDALN 742
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 577 DELAKLQAQEtvhEVALKDKEPDTQDADEVKKALEL------QMESHREAHHRQLARLRDEINEKQKTIDE-LKDLNQKL 649
Cdd:TIGR00618 743 QSLKELMHQA---RTVLKARTEAHFNNNEEVTAALQtgaelsHLAAEIQFFNRLREEDTHLLKTLEAEIGQeIPSDEDIL 819
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1233951479 650 QLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNL 708
Cdd:TIGR00618 820 NLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
528-816 |
2.76e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 528 RKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEEsYDSLSDELAKLQAQETVHEvalkdkepdtqdadevK 607
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEGYELLKE----------------K 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 608 KALELQmeshREAHHRQLARLRDEINEKQKTIDE-----------LKDLNQK-----------LQLELEKLQADYEKLKS 665
Cdd:TIGR02169 233 EALERQ----KEAIERQLASLEEELEKLTEEISElekrleeieqlLEELNKKikdlgeeeqlrVKEKIGELEAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 666 EEHEKSTKLQ-----------ELTFLYERHEQSK---QDLKGLEETVARELQTLHNLRKLFVQDV--------TTRVK-K 722
Cdd:TIGR02169 309 SIAEKERELEdaeerlakleaEIDKLLAEIEELEreiEEERKRRDKLTEEYAELKEELEDLRAELeevdkefaETRDElK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 723 SAEMEPEDSGG-IHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEgamkDK 801
Cdd:TIGR02169 389 DYREKLEKLKReINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA----DL 464
|
330
....*....|....*
gi 1233951479 802 RRYQQEVDRIKEAVR 816
Cdd:TIGR02169 465 SKYEQELYDLKEEYD 479
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
490-727 |
4.02e-06 |
|
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: 50.89 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 490 AIEEEFTVARLYISKIKSEVKSV--------VKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSV 561
Cdd:pfam17380 343 AMERERELERIRQEERKRELERIrqeeiameISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEM 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 562 ELKKRHLEESYDSLSDELAKLQAQEtVHEVALKDKEPDTQ-------DADEVKKALELQMESHREAHHRQLAR--LRDEI 632
Cdd:pfam17380 423 EQIRAEQEEARQREVRRLEEERARE-MERVRLEEQERQQQverlrqqEEERKRKKLELEKEKRDRKRAEEQRRkiLEKEL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 633 NEKQKTIDELKDLNQKLQLELEKLQ-ADYEKLKSEEHEKSTKLQELtfLYERHEQSKQDLKGLEETvaRELQTLHNLRKL 711
Cdd:pfam17380 502 EERKQAMIEEERKRKLLEKEMEERQkAIYEEERRREAEEERRKQQE--MEERRRIQEQMRKATEER--SRLEAMEREREM 577
|
250
....*....|....*.
gi 1233951479 712 FVQDVTTRvKKSAEME 727
Cdd:pfam17380 578 MRQIVESE-KARAEYE 592
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
527-705 |
5.91e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 527 HRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKR----HLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQD 602
Cdd:COG4913 241 HEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAAlrlwFAQRRLELLEAELEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 603 ADEVKKALELQMESH----REAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELT 678
Cdd:COG4913 321 LREELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
|
170 180 190
....*....|....*....|....*....|.
gi 1233951479 679 FLYE----RHEQSKQDLKGLEETVARELQTL 705
Cdd:COG4913 401 EALEealaEAEAALRDLRRELRELEAEIASL 431
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
363-586 |
7.18e-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: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 363 QEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQkvatmlsLES 442
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-------LEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 443 ELQRLQEVSGHQRKRIAEVLNGL--MKDLSEFSVIVGNGEIkLPVEISGAIEEEFTVARL-YISKIKSEVKSVVKRCRQL 519
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALyrLGRQPPLALLLSPEDF-LDAVRRLQYLKYLAPARReQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1233951479 520 ENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQE 586
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
546-701 |
1.28e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 546 QHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKK--ALELQMESHREAHhR 623
Cdd:COG4717 85 EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERleELEERLEELRELE-E 163
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1233951479 624 QLARLRDEINEKQKTIDEL-KDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTflyERHEQSKQDLKGLEETVARE 701
Cdd:COG4717 164 ELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ---EELEELEEELEQLENELEAA 239
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
320-557 |
1.34e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 320 IAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVL 399
Cdd:TIGR02169 277 LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 400 QALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEvsghQRKRIAEVLNGLMKDLSEFsvivgNG 479
Cdd:TIGR02169 357 EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR----ELDRLQEELQRLSEELADL-----NA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 480 EIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRC----RQLENLQVEcHRKMEvtgRELSSCQLLISQHEAKIRSLT 555
Cdd:TIGR02169 428 AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLskyeQELYDLKEE-YDRVE---KELSKLQRELAEAEAQARASE 503
|
..
gi 1233951479 556 EY 557
Cdd:TIGR02169 504 ER 505
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
520-826 |
1.55e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.89 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 520 ENLQVECHRKMEVTGRE--LSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDSL-SDELAKLQAQETVHEVALKDK 596
Cdd:TIGR00606 214 QYKEKACEIRDQITSKEaqLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIkALKSRKKQMEKDNSELELKME 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 597 EPdTQDADEVKKALELQMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQE 676
Cdd:TIGR00606 294 KV-FQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQS 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 677 LTF-----LYERHEQSKQDLKGLEETV----ARELQTLHNLRKLFVQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENN 747
Cdd:TIGR00606 373 LATrleldGFERGPFSERQIKNFHTLVierqEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKK 452
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1233951479 748 LEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIKEAVRYKSSGKRGHS 826
Cdd:TIGR00606 453 QEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHT 531
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
325-817 |
1.58e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 325 RQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEe 404
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 405 lAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEvsghQRKRIAEVLNGLMKDLSEfsvivgngeiklp 484
Cdd:COG4717 127 -LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA----ELAELQEELEELLEQLSL------------- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 485 veisgaieeeftVARLYISKIKSEVKSVVKRCRQLEnlqvechrkmevtgRELSSCQLLISQHEAKIRSLTEYMQSVELK 564
Cdd:COG4717 189 ------------ATEEELQDLAEELEELQQRLAELE--------------EELEEAQEELEELEEELEQLENELEAAALE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 565 KRHLEESYDS---------LSDELAKLQAQETVHEVAL--------------KDKEPDTQDADEVKkALELQMESHREAH 621
Cdd:COG4717 243 ERLKEARLLLliaaallalLGLGGSLLSLILTIAGVLFlvlgllallflllaREKASLGKEAEELQ-ALPALEELEEEEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 622 HRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKS----------TKLQELTFLYERHEQsKQDL 691
Cdd:COG4717 322 EELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiaallaeagvEDEEELRAALEQAEE-YQEL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 692 KGLEETVARELQTLHNLRKLFVQDVTTrvkksaemepedsggiHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPK 771
Cdd:COG4717 401 KEELEELEEQLEELLGELEELLEALDE----------------EELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1233951479 772 LEK----------------RLRATAER---VKALEGALKEAKEGAmkdKRRYQQEVdrIKEAVRY 817
Cdd:COG4717 465 LEEdgelaellqeleelkaELRELAEEwaaLKLALELLEEAREEY---REERLPPV--LERASEY 524
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
320-816 |
1.81e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 320 IAPEERQKYEEEIRRLYKQLDDKDDEINQqsqlIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVL 399
Cdd:PRK02224 196 IEEKEEKDLHERLNGLESELAELDEEIER----YEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 400 QALEELavnydqkSQEVEEKSQQNQLLVDELSQKVAtmlslESELQRLQEvsghqrKRIAEVLNGLMKDLSEfsvivgng 479
Cdd:PRK02224 272 REREEL-------AEEVRDLRERLEELEEERDDLLA-----EAGLDDADA------EAVEARREELEDRDEE-------- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 480 eiklpveisgaIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQ 559
Cdd:PRK02224 326 -----------LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 560 SvelkkrhLEESYDSLSDELAKLqaqETVHEVALKDKEPDTQDADEVKKALELQMESHREAhhrqlARLRDEIN------ 633
Cdd:PRK02224 395 E-------LRERFGDAPVDLGNA---EDFLEELREERDELREREAELEATLRTARERVEEA-----EALLEAGKcpecgq 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 634 -----EKQKTIDELKDLNQKLQLELEKLQADYEKLKsEEHEKSTKLQELTFLYERHEQSKQDLKGL----EETVARELQT 704
Cdd:PRK02224 460 pvegsPHVETIEEDRERVEELEAELEDLEEEVEEVE-ERLERAEDLVEAEDRIERLEERREDLEELiaerRETIEEKRER 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 705 LHNLRKLfVQDVTT--RVKKSAEMEPEDSGGIHSQK-----QKISFLENNLEQLTKVHKQLVrDNADLRCELPKL-EKR- 775
Cdd:PRK02224 539 AEELRER-AAELEAeaEEKREAAAEAEEEAEEAREEvaelnSKLAELKERIESLERIRTLLA-AIADAEDEIERLrEKRe 616
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1233951479 776 ------------LRATAERVKALEGALKEAK-EGAMKDKRRYQQEVDRIKEAVR 816
Cdd:PRK02224 617 alaelnderrerLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLD 670
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
380-682 |
2.23e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.09 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 380 ELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVeeKSQQNqlLVDELSQKVAtmlsleSELQRLQEVSGHQRKRIA 459
Cdd:PHA02562 161 DISVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQI--KTYNK--NIEEQRKKNG------ENIARKQNKYDELVEEAK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 460 EVLNGLMKDLSEFSVIVGNGEiklpveisgAIEEEFTVARLYISKIKSEVKSVVKRcrqlenlqvechRKMEVTGRELSS 539
Cdd:PHA02562 231 TIKAEIEELTDELLNLVMDIE---------DPSAALNKLNTAAAKIKSKIEQFQKV------------IKMYEKGGVCPT 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 540 CQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDslsdelaklQAQETVHEVAlkdkepdtqdaDEVKKALELQmeSHRE 619
Cdd:PHA02562 290 CTQQISEGPDRITKIKDKLKELQHSLEKLDTAID---------ELEEIMDEFN-----------EQSKKLLELK--NKIS 347
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1233951479 620 AHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYE 682
Cdd:PHA02562 348 TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGIVTD 410
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
597-816 |
2.26e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 597 EPDT-QDADEVKKalelQMESHREAHH------RQLARLRdEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHE 669
Cdd:COG4913 220 EPDTfEAADALVE----HFDDLERAHEaledarEQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 670 KstKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRklfvqdvttrvkksaemepEDSGGihsqkQKISFLENNLE 749
Cdd:COG4913 295 A--ELEELRAELARLEAELERLEARLDALREELDELEAQI-------------------RGNGG-----DRLEQLEREIE 348
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1233951479 750 QLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIKEAVR 816
Cdd:COG4913 349 RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR 415
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
428-662 |
2.46e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 428 DELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLmkDLSEFSVIVGNGEIKlpveisgAIEEEFTVARLYISKIKS 507
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL--AALERRIAALARRIR-------ALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 508 EVKSVVKRCRQLENLQVECHRKMEVTGRElSSCQLLISQHEAK--IRSLtEYMQSVelkKRHLEESYDSLSDELAKLQAQ 585
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQ-PPLALLLSPEDFLdaVRRL-QYLKYL---APARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1233951479 586 ETVHEVALKDKEPDTQDADEVKKALELQMESHREAhhrqLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEK 662
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKL----LARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
564-803 |
2.70e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 564 KKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALEL---QMESHREAHHRQLARLRDEINEKQKTID 640
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKeieQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 641 ELKDLNQKLQLELEKLQADYEKLKSEE-----HEKSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQD 715
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 716 VTTRVKKSAEMEPEdsggIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKE 795
Cdd:TIGR02169 835 IQELQEQRIDLKEQ----IKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEA 910
|
....*...
gi 1233951479 796 GAMKDKRR 803
Cdd:TIGR02169 911 QIEKKRKR 918
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
613-809 |
2.70e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 613 QMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQaDYEKLKSE--EHEKSTKLQELTFLYERHEQSKQD 690
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEkrEYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 691 LKGLEETVA---RELQ----TLHNLRKLfVQDVTTRVKKSAEMEP--------EDSGGIHSQKQKISFLENNLEQLTKVH 755
Cdd:TIGR02169 246 LASLEEELEkltEEISelekRLEEIEQL-LEELNKKIKDLGEEEQlrvkekigELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1233951479 756 KQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEgAMKDKRRYQQEVD 809
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE-ELEDLRAELEEVD 377
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
323-831 |
3.60e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 323 EERQKYEEEirRLYKQLDDKDDEinQQSQLIEKLKQQMLDQEEllvSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQAL 402
Cdd:PTZ00121 1203 EAARKAEEE--RKAEEARKAEDA--KKAEAVKKAEEAKKDAEE---AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 403 EELAVNYDQKSQEV----EEKSQQNQLLVDELSQKVATMLSLESELQRLQEVsghqrKRIAEVLnglmKDLSEfsvivgn 478
Cdd:PTZ00121 1276 EARKADELKKAEEKkkadEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA-----KKKADAA----KKKAE------- 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 479 gEIKLPVEISGAIEEeftvarlyisKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQlliSQHEAKIRSLTEYM 558
Cdd:PTZ00121 1340 -EAKKAAEAAKAEAE----------AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK---KADEAKKKAEEDKK 1405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 559 QSVELKKRHLEESYdslSDELAKlQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQLARLRDEIN---EK 635
Cdd:PTZ00121 1406 KADELKKAAAAKKK---ADEAKK-KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKkkaEE 1481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 636 QKTIDELKDLNQKLQLELEKL-QADYEKLKSEEHEKSTKLQELTFLYERHEQSKQD--LKGLEETVARELQTLHNLRKlf 712
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAkKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADeaKKAEEKKKADELKKAEELKK-- 1559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 713 vqdvtTRVKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEgalkE 792
Cdd:PTZ00121 1560 -----AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE----E 1630
|
490 500 510
....*....|....*....|....*....|....*....
gi 1233951479 793 AKEGAMKDKRRYQQEVdRIKEAVRYKSSGKRGHSAQIAK 831
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEK-KKAEELKKAEEENKIKAAEEAK 1668
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
324-795 |
3.76e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 324 ERQKYEEEIRRLYKQLDDKDDEINQqsqlieklkqqMLDQEELlvsTRGDNEKVQRELSHLQSENDAAKDEVKEV---LQ 400
Cdd:PRK02224 273 EREELAEEVRDLRERLEELEEERDD-----------LLAEAGL---DDADAEAVEARREELEDRDEELRDRLEECrvaAQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 401 ALEELAVNYDQKSQEVEEKSqqnqllvDELSQKVATmlsLESELQRLQEVSGHQRKRIAEvlngLMKDLSEFSVIVGNGE 480
Cdd:PRK02224 339 AHNEEAESLREDADDLEERA-------EELREEAAE---LESELEEAREAVEDRREEIEE----LEEEIEELRERFGDAP 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 481 IKL--PVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQV-----ECHRKMEVTGR--ELSSCQLLISQHEAKI 551
Cdd:PRK02224 405 VDLgnAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpECGQPVEGSPHveTIEEDRERVEELEAEL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 552 RSLTEYMQSVELKKRHLEE------SYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAhhrqL 625
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDlveaedRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREA----A 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 626 ARLRDEINEKQKTIDELKDLNQKLQLELEKLqadyEKLKSEEHEKSTKLQELTFLYERHEQskqdlkgleetvareLQTL 705
Cdd:PRK02224 561 AEAEEEAEEAREEVAELNSKLAELKERIESL----ERIRTLLAAIADAEDEIERLREKREA---------------LAEL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 706 HNLRKLFVQDVTTRVKksaEMEPE-DSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRC----------ELPKLEK 774
Cdd:PRK02224 622 NDERRERLAEKRERKR---ELEAEfDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAeigaveneleELEELRE 698
|
490 500
....*....|....*....|.
gi 1233951479 775 RLRATAERVKALEGALKEAKE 795
Cdd:PRK02224 699 RREALENRVEALEALYDEAEE 719
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
548-778 |
3.98e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.53 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 548 EAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMEshreahhRQLAR 627
Cdd:pfam12128 603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKN-------KALAE 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 628 LRDEINEKQKTID-ELKDLNQKLQLELEKLQADY--------EKLKSEEHEKSTKLQEL-TFLYERHEQSKQDLKGLEET 697
Cdd:pfam12128 676 RKDSANERLNSLEaQLKQLDKKHQAWLEEQKEQKreartekqAYWQVVEGALDAQLALLkAAIAARRSGAKAELKALETW 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 698 VARELQTL----HNLRKLF--VQDVTTRVKKSAEMEPE---------DSGGIHSQKQKISfLENNLEQLTKVHKQLVRDN 762
Cdd:pfam12128 756 YKRDLASLgvdpDVIAKLKreIRTLERKIERIAVRRQEvlryfdwyqETWLQRRPRLATQ-LSNIERAISELQQQLARLI 834
|
250
....*....|....*.
gi 1233951479 763 ADLRCELPKLEKRLRA 778
Cdd:pfam12128 835 ADTKLRRAKLEMERKA 850
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
293-676 |
4.12e-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: 47.51 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 293 LAGEEAALGAELCEETPVNDNSSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRG 372
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 373 DNEKVQRELSHLQS------ENDAAKDEVKEVLQalEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQR 446
Cdd:pfam10174 423 RVKSLQTDSSNTDTalttleEALSEKERIIERLK--EQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLID 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 447 LQEVSGHQRKRiaevlnGLMKDLSEFSVivgngEIKLPVEISGAIEEEFTVARLYISKIKSEVK-SVVKRCRQLENlqvE 525
Cdd:pfam10174 501 LKEHASSLASS------GLKKDSKLKSL-----EIAVEQKKEECSKLENQLKKAHNAEEAVRTNpEINDRIRLLEQ---E 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 526 CHRKMEvtgrELSSCQllisqheAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQ--DA 603
Cdd:pfam10174 567 VARYKE----ESGKAQ-------AEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKkkGA 635
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1233951479 604 DEVKKALELQMESHREAHHRQLARLrdeINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQE 676
Cdd:pfam10174 636 QLLEEARRREDNLADNSQQLQLEEL---MGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEE 705
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
318-823 |
6.34e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 318 VRIAPEERQKYEEeiRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEEllvSTRGDNEKVQRELSHLQSENDAAKDEVKE 397
Cdd:PTZ00121 1301 KKKADEAKKKAEE--AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE---AAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 398 VLQALEELAVNYDQ--KSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEvsghqrKRIAEVLNGLMKDLSEFSVI 475
Cdd:PTZ00121 1376 AKKKADAAKKKAEEkkKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEE------KKKADEAKKKAEEAKKADEA 1449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 476 VGNGEIKLPVEISGAIEEEftvarlyiSKIKSEVKSVVKRCRQLEnlqvECHRKMEVTGRELSSCQlliSQHEAKIRSlt 555
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEE--------AKKADEAKKKAEEAKKAD----EAKKKAEEAKKKADEAK---KAAEAKKKA-- 1512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 556 EYMQSVELKKRhleesydslSDELAKLQAQETVHEVAlkdKEPDTQDADEVKKALEL-QMESHREAHHRQlaRLRDEINE 634
Cdd:PTZ00121 1513 DEAKKAEEAKK---------ADEAKKAEEAKKADEAK---KAEEKKKADELKKAEELkKAEEKKKAEEAK--KAEEDKNM 1578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 635 KQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKlfvQ 714
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK---A 1655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 715 DVTTRVKKSAEMEPEDSggihsQKQKISFLENNLEQLTKVHKQLVRDNADLRcelpKLEKRLRATAERVKALEGALKEak 794
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEE-----DKKKAEEAKKAEEDEKKAAEALKKEAEEAK----KAEELKKKEAEEKKKAEELKKA-- 1724
|
490 500 510
....*....|....*....|....*....|.
gi 1233951479 795 egamkdkrryqQEVDRIK--EAVRYKSSGKR 823
Cdd:PTZ00121 1725 -----------EEENKIKaeEAKKEAEEDKK 1744
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
314-449 |
6.38e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 314 SSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKD 393
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1233951479 394 EVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQE 449
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
517-728 |
9.34e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 9.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 517 RQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDK 596
Cdd:pfam07888 55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 597 EPDTQDADEVKKALELQMESHREAHHRQLARLRDEINEKqktidelkdlnqklqlelEKLQADYEKLKSEEHEKSTKLQE 676
Cdd:pfam07888 135 EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAER------------------KQLQAKLQQTEEELRSLSKEFQE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1233951479 677 LTFLYERHEQSKQDLKgleETVARELQTLhnlrklfvqdvTTRVKKSAEMEP 728
Cdd:pfam07888 197 LRNSLAQRDTQVLQLQ---DTITTLTQKL-----------TTAHRKEAENEA 234
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
623-717 |
9.53e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 46.23 E-value: 9.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 623 RQLARLRDEINEKQKTIDEL-KDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVARE 701
Cdd:COG0542 418 RRLEQLEIEKEALKKEQDEAsFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAEL 497
|
90
....*....|....*.
gi 1233951479 702 LQTLHNLRKLFVQDVT 717
Cdd:COG0542 498 EEELAELAPLLREEVT 513
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
548-813 |
1.30e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 548 EAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEvALKDKEPDTQDADEVkkalelqmeshreahHRQLAR 627
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEIDVASA---------------EREIAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 628 LRDEINEKQKTIDELKdlnqKLQLELEKLQADYEKLKSEEHEKSTKL----QELTFLYERHEQSKQDLKGLEETVARELQ 703
Cdd:COG4913 673 LEAELERLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIgrleKELEQAEEELDELQDRLEAAEDLARLELR 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 704 TLHN--LRKLFVQDVTTRVKKSAEmepedsGGIHSQKQKISFLENNLEQLTKVHKQL-----------VRDNADLRCELP 770
Cdd:COG4913 749 ALLEerFAAALGDAVERELRENLE------ERIDALRARLNRAEEELERAMRAFNREwpaetadldadLESLPEYLALLD 822
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1233951479 771 KLEK-RLratAERVKALEGALKEAKEGAMKD-KRRYQQEVDRIKE 813
Cdd:COG4913 823 RLEEdGL---PEYEERFKELLNENSIEFVADlLSKLRRAIREIKE 864
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
582-725 |
1.46e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 45.47 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 582 LQAQETVHEVALKDKEPDTQDADEVKKALELQM-ESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADY 660
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAkELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLE 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1233951479 661 EKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVARELqTLHNLRKLFVQDVTTRVKKSAE 725
Cdd:PRK12705 105 NQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKL-LLKLLDAELEEEKAQRVKKIEE 168
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
597-852 |
1.91e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 597 EPDTQDADEVKKALELQMESHREahhrQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQE 676
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQA----ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 677 LTflyeRHEQSKQDLKGLEETV--ARELQTLHNlRKLFVQDVTTRVKKSAEmepedsgGIHSQKQKISFLENNLEQLTKV 754
Cdd:COG3883 91 RA----RALYRSGGSVSYLDVLlgSESFSDFLD-RLSALSKIADADADLLE-------ELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 755 HKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIKEAVRYKSSGKRGHSAQIAKPVR 834
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
250
....*....|....*...
gi 1233951479 835 PGHYPASSPTNPYGTRSP 852
Cdd:COG3883 239 AAAAAASAAGAGAAGAAG 256
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
318-696 |
1.94e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 318 VRIAPEERQKYEEeiRRLYKQLDDKDDEINQQSQLIEKLKQ-QMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVK 396
Cdd:PTZ00121 1430 KKKADEAKKKAEE--AKKADEAKKKAEEAKKAEEAKKKAEEaKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 397 EVLQALEELAVNYDQKSQEV---EEKSQQNQLLVDELSQKvATMLSLESELQRLQEVSGHQRK-----------RIAEVL 462
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAkkaEEAKKADEAKKAEEKKK-ADELKKAEELKKAEEKKKAEEAkkaeedknmalRKAEEA 1586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 463 NGLMKDLSEFSVIVGNGEIKLPVEISGAIEEEftvaRLYISKIKSEvKSVVKRCRQLENLQVECHRKMEvtgrelsscQL 542
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA----KIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAE---------EL 1652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 543 LISQHEAKIRSlTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMEshREAHH 622
Cdd:PTZ00121 1653 KKAEEENKIKA-AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA--EEENK 1729
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1233951479 623 RQLARLRDEINEKQKTIDELKdlnqKLQLELEKLQadyeKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEE 696
Cdd:PTZ00121 1730 IKAEEAKKEAEEDKKKAEEAK----KDEEEKKKIA----HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
549-779 |
2.18e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 549 AKIRSLTEYMQSVELKKRHLEE---SYDSLSDELAKLQAQEtvheVALKDKEPDtqdaDEVKKAlelqmeshrEAHHRQL 625
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQqikTYNKNIEEQRKKNGEN----IARKQNKYD----ELVEEA---------KTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 626 ARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEH------EKSTKLQELTFLYERHEQSKQDLKGLEETVA 699
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekggVCPTCTQQISEGPDRITKIKDKLKELQHSLE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 700 RELQTLHNLRKLFVQdVTTRVKKSAEMEPEdsggIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRAT 779
Cdd:PHA02562 317 KLDTAIDELEEIMDE-FNEQSKKLLELKNK----ISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
385-811 |
2.24e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 385 QSENDAAKDE----VKEVLQALEELAVNYDQKSQEV-EEKSQ-QNQLLVD-ELSQKVATM-LSLESELQRLQEVSGHQRK 456
Cdd:pfam01576 3 QEEEMQAKEEelqkVKERQQKAESELKELEKKHQQLcEEKNAlQEQLQAEtELCAEAEEMrARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 457 RIAE---VLNGLMKDLSEFSVIVGNGEIKLPveisgaiEEEFTVARLYISKIKSEVK----------------SVVKRCR 517
Cdd:pfam01576 83 RLEEeeeRSQQLQNEKKKMQQHIQDLEEQLD-------EEEAARQKLQLEKVTTEAKikkleedillledqnsKLSKERK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 518 QLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYM-------QSVELKKRHLEESYDSLSDELAKLQAQETVHE 590
Cdd:pfam01576 156 LLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLkkeekgrQELEKAKRKLEGESTDLQEQIAELQAQIAELR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 591 VALKDKEPDTQDAdevkkalelqmeshreahhrqLARLRDEINEK---QKTIDELKDLNQKLQLELEKLQADYEKlksEE 667
Cdd:pfam01576 236 AQLAKKEEELQAA---------------------LARLEEETAQKnnaLKKIRELEAQISELQEDLESERAARNK---AE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 668 HEKSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENN 747
Cdd:pfam01576 292 KQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRN 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1233951479 748 LEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRI 811
Cdd:pfam01576 372 KANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKL 435
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
377-808 |
2.50e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.10 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 377 VQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSG---H 453
Cdd:pfam05483 97 IEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKkyeY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 454 QRKRIAEVLNGLMKDLSEfsVIVGNGEIKLPVEiSGAIEEEFTVARLYiskiksevksvvkrcRQLENLQVECHRKMEVT 533
Cdd:pfam05483 177 EREETRQVYMDLNNNIEK--MILAFEELRVQAE-NARLEMHFKLKEDH---------------EKIQHLEEEYKKEINDK 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 534 GRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALE-- 611
Cdd:pfam05483 239 EKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEed 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 612 --------LQMESHREAHHRQLAR------------------LRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKS 665
Cdd:pfam05483 319 lqiatktiCQLTEEKEAQMEELNKakaahsfvvtefeattcsLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTK 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 666 EEHEKSTKLQEL--------TFLYERHEQSK--QDLKGLEETVARELQT----LHNLRKLFVQDVTTRVKKSAEMEpEDS 731
Cdd:pfam05483 399 FKNNKEVELEELkkilaedeKLLDEKKQFEKiaEELKGKEQELIFLLQArekeIHDLEIQLTAIKTSEEHYLKEVE-DLK 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 732 GGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCEL----------PKLEKRLRATAERVKALEGALKEAKEGAMKDK 801
Cdd:pfam05483 478 TELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELkkhqediincKKQEERMLKQIENLEEKEMNLRDELESVREEF 557
|
....*..
gi 1233951479 802 RRYQQEV 808
Cdd:pfam05483 558 IQKGDEV 564
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
323-833 |
3.10e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 323 EERQKYEEEIRRLYKQLDDKDDEINQQSQLIE---------------------KLKQQMLDQEELLVSTRGDNEK---VQ 378
Cdd:PRK01156 249 DMKNRYESEIKTAESDLSMELEKNNYYKELEErhmkiindpvyknrnyindyfKYKNDIENKKQILSNIDAEINKyhaII 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 379 RELSHLQSEND------AAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQnqllVDELSQKVATMLSLESELQRLQEVSG 452
Cdd:PRK01156 329 KKLSVLQKDYNdyikkkSRYDDLNNQILELEGYEMDYNSYLKSIESLKKK----IEEYSKNIERMSAFISEILKIQEIDP 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 453 HQRKRIAEVLNglmKDLSEFSVIVGNGEIKLPVEISGAIEEEFTVARLyiskiksEVKSVVKRC---------RQLENLQ 523
Cdd:PRK01156 405 DAIKKELNEIN---VKLQDISSKVSSLNQRIRALRENLDELSRNMEML-------NGQSVCPVCgttlgeeksNHIINHY 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 524 VECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKrhLEESYDSLSDELAKLQAQEtVHEVALKDKEPDTQDA 603
Cdd:PRK01156 475 NEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINK--SINEYNKIESARADLEDIK-IKINELKDKHDKYEEI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 604 DEVKKALELQ-MESHREAHHRQLARLRD-EINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLY 681
Cdd:PRK01156 552 KNRYKSLKLEdLDSKRTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNL 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 682 ERHEQSKQDLKGLEETVARElqtlhnlrklfVQDVTTRVKKSAEMEPEDSggihSQKQKISFLENNLEQLTKVHKQLVRD 761
Cdd:PRK01156 632 NNKYNEIQENKILIEKLRGK-----------IDNYKKQIAEIDSIIPDLK----EITSRINDIEDNLKKSRKALDDAKAN 696
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1233951479 762 NADLRCELPKLEKRLRATAERVKALEGALKEakegaMKDKRRYQQEVDRIKEAVrykssGKRGHSAQIAKPV 833
Cdd:PRK01156 697 RARLESTIEILRTRINELSDRINDINETLES-----MKKIKKAIGDLKRLREAF-----DKSGVPAMIRKSA 758
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
329-801 |
3.50e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 329 EEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKD-------EVKEVLQA 401
Cdd:TIGR04523 53 EKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEqknklevELNKLEKQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 402 LEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLMKDLSEFSVIVG---- 477
Cdd:TIGR04523 133 KKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKkiqk 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 478 ----NGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVEchrkmevTGRELSSCQLLISQHEAKIRS 553
Cdd:TIGR04523 213 nkslESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNK-------IKKQLSEKQKELEQNNKKIKE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 554 LTEYMQSVE-----LKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQM---ESHREAHHRQL 625
Cdd:TIGR04523 286 LEKQLNQLKseisdLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELtnsESENSEKQREL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 626 A----RLRDEINEKQKTIDELK-------DLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGL 694
Cdd:TIGR04523 366 EekqnEIEKLKKENQSYKQEIKnlesqinDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 695 EETVARELQTLHNLRKLfvqdvttrvKKSAEMEPED-SGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLE 773
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNT---------RESLETQLKVlSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLT 516
|
490 500
....*....|....*....|....*...
gi 1233951479 774 KRLRATAERVKALEGALKEaKEGAMKDK 801
Cdd:TIGR04523 517 KKISSLKEKIEKLESEKKE-KESKISDL 543
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
272-696 |
4.86e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 272 AKLEAELSRWRNGENVPETERLAGEEAALGAELCEETPVNDNSSIVVRIAPEERQKYEEEIRRLYKQlDDKDDEINQQSQ 351
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA-KKKADEAKKKAE 1428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 352 LIEKLKQQMLDQEEllvsTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAvNYDQKSQEVEEKSQQNQLLVDELS 431
Cdd:PTZ00121 1429 EKKKADEAKKKAEE----AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKA-EEAKKADEAKKKAEEAKKKADEAK 1503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 432 QKvatmlslESELQRLQEVSGHQRKRIAEVLNGlMKDLSEFSVIVGNGEIKLPVEISGAIEEEftvarlyiskiKSEVKS 511
Cdd:PTZ00121 1504 KA-------AEAKKKADEAKKAEEAKKADEAKK-AEEAKKADEAKKAEEKKKADELKKAEELK-----------KAEEKK 1564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 512 VVKRCRQLENLQVECHRKMEvtgrELSSCQLLISQHEAKIRSLTEYMQSVELKKrhlEESYDSLSDELAKLQAQETVHEV 591
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAE----EAKKAEEARIEEVMKLYEEEKKMKAEEAKK---AEEAKIKAEELKKAEEEKKKVEQ 1637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 592 ALKDKEPDTQDADEVKKALEL------QMESHREAHHRQLARLRDEINEKQKTIDEL--KDLNQKLQLELEKLQAD---- 659
Cdd:PTZ00121 1638 LKKKEAEEKKKAEELKKAEEEnkikaaEEAKKAEEDKKKAEEAKKAEEDEKKAAEALkkEAEEAKKAEELKKKEAEekkk 1717
|
410 420 430
....*....|....*....|....*....|....*..
gi 1233951479 660 YEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEE 696
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
285-661 |
5.09e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.19 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 285 ENVPETERLAGEEAALGAELCEETPVNDNSSIVVRIAPEERQKYEEEIRRLYKQLddKDDEINQQSQLIEKLKQQMLDQE 364
Cdd:pfam02463 148 AMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKL--KEQAKKALEYYQLKEKLELEEEY 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 365 ELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAvNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESEL 444
Cdd:pfam02463 226 LLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKL-AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 445 QRLQEVSGHQRKRIAE--------VLNGLMKDLSEFSVIVGNGEIKLpvEISGAIEEEFTVARLYISKIKSEVKSVVKRC 516
Cdd:pfam02463 305 LERRKVDDEEKLKESEkekkkaekELKKEKEEIEELEKELKELEIKR--EAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 517 RQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRhLEESYDSLSDELAKLQAQETVHEVALKDK 596
Cdd:pfam02463 383 SERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEIL-EEEEESIELKQGKLTEEKEELEKQELKLL 461
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1233951479 597 EPDTQDADEVKKALELQMESHREAHHRQLAR-LRDEINEKQKTIDELKDLNQKLQLELEKLQADYE 661
Cdd:pfam02463 462 KDELELKKSEDLLKETQLVKLQEQLELLLSRqKLEERSQKESKARSGLKVLLALIKDGVGGRIISA 527
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
535-814 |
5.28e-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: 44.17 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 535 RELSSCQ-LLISQHEAKIRsLTEYMQSVELKKRHLEESYDSLSDELAKLQ----AQETVhevalkdkEPDTQDADEVKKA 609
Cdd:COG3096 292 RELFGARrQLAEEQYRLVE-MARELEELSARESDLEQDYQAASDHLNLVQtalrQQEKI--------ERYQEDLEELTER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 610 LELQMEShREAHHRQLARLRDEINEKQKTIDELKDlnqklQLeleklqADYEklkseehekstklQELTFLYERHEQSKQ 689
Cdd:COG3096 363 LEEQEEV-VEEAAEQLAEAEARLEAAEEEVDSLKS-----QL------ADYQ-------------QALDVQQTRAIQYQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 690 DLKGLEETvarelQTLHNLRKLFVQDVTTRVKKSAEMEPEDSGGIHSQKQKISF-------LENNLEQLTKVHKQLVRDN 762
Cdd:COG3096 418 AVQALEKA-----RALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVadaarrqFEKAYELVCKIAGEVERSQ 492
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1233951479 763 ADLRC-ELPKLEKRLRATAERVKALEGALKEAKEGAmkdkrRYQQEVDRIKEA 814
Cdd:COG3096 493 AWQTArELLRRYRSQQALAQRLQQLRAQLAELEQRL-----RQQQNAERLLEE 540
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
338-449 |
5.63e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.53 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 338 QLDDKDDEINQQSQLIEKLKQQMLDQEELLVST-----------------RG-DNEKVQRELSHLQSENDAAKDEVKEVL 399
Cdd:PRK11637 97 TLNQLNKQIDELNASIAKLEQQQAAQERLLAAQldaafrqgehtglqlilSGeESQRGERILAYFGYLNQARQETIAELK 176
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 400 QALEELAVnydQKSQEVEEKSQQNQLLVDELSQKVA----------TMLSLESELQRLQE 449
Cdd:PRK11637 177 QTREELAA---QKAELEEKQSQQKTLLYEQQAQQQKleqarnerkkTLTGLESSLQKDQQ 233
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
323-802 |
6.21e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.56 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 323 EERQKYEEEIrrlYKQLDDKDDEINQQSQLIEKLKQQMLD-----QEELLVSTRG------DNEKVQRELSHLQSENDAA 391
Cdd:pfam05483 274 EEKTKLQDEN---LKELIEKKDHLTKELEDIKMSLQRSMStqkalEEDLQIATKTicqlteEKEAQMEELNKAKAAHSFV 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 392 KDEVKEVLQALEELavnYDQKSQEVEEKSQQNQLLVDELSQKVATMLSL-------ESELQRLQEVSGHQRK-------- 456
Cdd:pfam05483 351 VTEFEATTCSLEEL---LRTEQQRLEKNEDQLKIITMELQKKSSELEEMtkfknnkEVELEELKKILAEDEKlldekkqf 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 457 -RIAEVLNGLMKDLSeFSVIVGNGEI-KLPVEISGAieeefTVARLYISKIKSEVKSVVKRcRQLENLQVECHRKM---- 530
Cdd:pfam05483 428 eKIAEELKGKEQELI-FLLQAREKEIhDLEIQLTAI-----KTSEEHYLKEVEDLKTELEK-EKLKNIELTAHCDKllle 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 531 -EVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKA 609
Cdd:pfam05483 501 nKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEY 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 610 LELQMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQ-------LELEKLQADYEKLKSEEHEKSTKLQELTFLYE 682
Cdd:pfam05483 581 EVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKkkgsaenKQLNAYEIKVNKLELELASAKQKFEEIIDNYQ 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 683 RH-EQSKQDLKGLEETVARELQTLHNLRKLfVQDVTTRVK-KSAEM-------EPEDSGGIHSQKQKISFLENNLEQLTK 753
Cdd:pfam05483 661 KEiEDKKISEEKLLEEVEKAKAIADEAVKL-QKEIDKRCQhKIAEMvalmekhKHQYDKIIEERDSELGLYKNKEQEQSS 739
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1233951479 754 VHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEaKEGAMKDKR 802
Cdd:pfam05483 740 AKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE-NTAILKDKK 787
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
325-711 |
6.26e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 43.30 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 325 RQKYEEEIRRLYKQLDD-----KDDEINQ--------QSQ-LIEKLKQ--------QMLDQEELLVSTRGDNE-----KV 377
Cdd:pfam06160 5 RKKIYKEIDELEERKNElmnlpVQEELSKvkklnltgETQeKFEEWRKkwddivtkSLPDIEELLFEAEELNDkyrfkKA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 378 QRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQrlqevsghqrkr 457
Cdd:pfam06160 85 KKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDELE------------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 458 iaEVLNGLMKDLSEFSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRC-RQLENLQvECHRKMEVTGRE 536
Cdd:pfam06160 153 --KQLAEIEEEFSQFEELTESGDYLEAREVLEKLEEETDALEELMEDIPPLYEELKTELpDQLEELK-EGYREMEEEGYA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 537 LSSCQLL--ISQHEAKIRSLTEYMQSVELKK-----RHLEESYDSLSDELAK-LQAQETVHEvALKDKEPDTQDADEVKK 608
Cdd:pfam06160 230 LEHLNVDkeIQQLEEQLEENLALLENLELDEaeealEEIEERIDQLYDLLEKeVDAKKYVEK-NLPEIEDYLEHAEEQNK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 609 ALELQMESHREA---HHRQLARLRDeineKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTflyERHE 685
Cdd:pfam06160 309 ELKEELERVQQSytlNENELERVRG----LEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIE---EEQE 381
|
410 420 430
....*....|....*....|....*....|...
gi 1233951479 686 QSKQDLKGL--EETVAREL-----QTLHNLRKL 711
Cdd:pfam06160 382 EFKESLQSLrkDELEAREKldefkLELREIKRL 414
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
349-663 |
7.05e-04 |
|
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: 43.35 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 349 QSQLIEKLKQQmldqEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEV---LQALEELAVNYDQKSQEVEEKSQQNQL 425
Cdd:pfam07888 33 QNRLEECLQER----AELLQAQEAANRQREKEKERYKRDREQWERQRRELesrVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 426 LVDELSQ-KVATMLSLESELQRLQEVSGH-----QRKRIAEVLNGLMKDLSEFSVIVG----------NGEIKLPVEISG 489
Cdd:pfam07888 109 SSEELSEeKDALLAQRAAHEARIRELEEDiktltQRVLERETELERMKERAKKAGAQRkeeeaerkqlQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 490 AIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRK---MEVTGRELSSCQLLISQHEAKIRSLTEYMQSV----- 561
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKeaeNEALLEELRSLQERLNASERKVEGLGEELSSMaaqrd 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 562 ----ELKKRHLEESydSLSDELAKL------------QAQETVHEVALKDKEPDTQDADEVKKALE-LQME-SHREAHHR 623
Cdd:pfam07888 269 rtqaELHQARLQAA--QLTLQLADAslalregrarwaQERETLQQSAEADKDRIEKLSAELQRLEErLQEErMEREKLEV 346
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1233951479 624 QLARLRD----EINEKQKTIDELKDLNQKLQLELEKLQADYEKL 663
Cdd:pfam07888 347 ELGREKDcnrvQLSESRRELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
549-700 |
9.99e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.81 E-value: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 549 AKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQLARL 628
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELEL 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1233951479 629 RDEINEKQKTIDELKDLNQKLQlELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVAR 700
Cdd:pfam05557 128 QSTNSELEELQERLDLLKAKAS-EAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELAR 198
|
|
| BAR_Rvs167p |
cd07599 |
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon ... |
605-720 |
1.07e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon starvation protein 167 and similar proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of fungal proteins with similarity to Saccharomyces cerevisiae Reduced viability upon starvation protein 167 (Rvs167p) and Schizosaccharomyces pombe Hob1 (homolog of Bin1). S. cerevisiae Rvs167p plays a role in regulation of the actin cytoskeleton, endocytosis, and sporulation. It forms a heterodimer with another BAR domain protein Rvs161p. Rvs161p and Rvs167p share common functions but are not interchangeable. Their BAR domains cannot be replaced with each other and the overexpression of one cannot suppress the mutant phenotypes of the other. Rvs167p also interacts with the GTPase activating protein (GAP) Gyp5p, which is involved in ER to Golgi vesicle trafficking. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153283 [Multi-domain] Cd Length: 216 Bit Score: 41.47 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 605 EVKKALELQMESHREAHHRQLARLRDEINEKQKTIDElkdlNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERH 684
Cdd:cd07599 82 ELKKELLEELEFFEERVILPAKELKKYIKKIRKTIKK----RDHKKLDYDKLQNKLNKLLQKKKELSLKDEKQLAKLERK 157
|
90 100 110
....*....|....*....|....*....|....*..
gi 1233951479 685 -EQSKQDLKGLEETVARELQTLHNLRKLFVQDVTTRV 720
Cdd:cd07599 158 lEEAKEEYEALNELLKSELPKLLALADEFLPPLFKSF 194
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
593-813 |
1.17e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 593 LKDKEPDTQDADEVKKALELQMESHR------EAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSE 666
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEkfikrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 667 EhekstklQELTFLYERHEQSKQDLKGLEETVaRELQTLHNLRKLFVQDVTTRVKKSAEMEP---------EDSGGIHSQ 737
Cdd:PRK03918 237 K-------EEIEELEKELESLEGSKRKLEEKI-RELEERIEELKKEIEELEEKVKELKELKEkaeeyiklsEFYEEYLDE 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1233951479 738 KQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEakegaMKDKRRYQQEVDRIKE 813
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHEL-----YEEAKAKKEELERLKK 379
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
385-609 |
1.25e-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: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 385 QSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNG 464
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 465 LMK---DLSEFSVIVGNGeiklpvEISGAIEEEFTVARLY------ISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGR 535
Cdd:COG3883 95 LYRsggSVSYLDVLLGSE------SFSDFLDRLSALSKIAdadadlLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1233951479 536 ELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKA 609
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
327-801 |
1.40e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 327 KYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELa 406
Cdd:TIGR04523 100 KLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLL- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 407 vnydqkSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEvsghqrkriaevlngLMKDLSEFSvivgngeiklpvE 486
Cdd:TIGR04523 179 ------EKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKS---------------LESQISELK------------K 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 487 ISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVEchrkmevTGRELSSCQLLISQHEAKIRSLTEYMQSVE---- 562
Cdd:TIGR04523 226 QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNK-------IKKQLSEKQKELEQNNKKIKELEKQLNQLKseis 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 563 -LKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQM---ESHREAHHRQLA----RLRDEINE 634
Cdd:TIGR04523 299 dLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELtnsESENSEKQRELEekqnEIEKLKKE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 635 KQKTIDELK-------DLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVA---RELQT 704
Cdd:TIGR04523 379 NQSYKQEIKnlesqinDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSvkeLIIKN 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 705 LHNLRKLFVQ--DVTTRVKKSAEMEPEDsggihsQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAER 782
Cdd:TIGR04523 459 LDNTRESLETqlKVLSRSINKIKQNLEQ------KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
490
....*....|....*....
gi 1233951479 783 VKALEGALKEAKEGAMKDK 801
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDD 551
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
613-666 |
1.41e-03 |
|
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.
Pssm-ID: 439196 [Multi-domain] Cd Length: 91 Bit Score: 38.70 E-value: 1.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1233951479 613 QMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSE 666
Cdd:cd22887 15 ELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEE 68
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
558-709 |
1.49e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.93 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 558 MQSVELKKRHLEESYDSLSDELAKLQAQET-VHEV--ALKDKEPDTQDADEVKKALELQMESHREAhhrQLARLRDEINE 634
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLMKELElLNSIkpKLRDRKDALEEELRQLKQLEDELEDCDPT---ELDRAKEKLKK 215
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1233951479 635 KQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELT-FLYERHEQSKQDLKGLEETVaRELQTLHNLR 709
Cdd:smart00787 216 LLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEkKLEQCRGFTFKEIEKLKEQL-KLLQSLTGWK 290
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
548-705 |
1.65e-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: 41.06 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 548 EAKIRSLTEyMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREahhrqlar 627
Cdd:COG1579 3 PEDLRALLD-LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA-------- 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1233951479 628 LRDEINEKQKTIDELKDLNQkLQLELEKLQADYEKLKSEEHEKSTKLQELTflyERHEQSKQDLKGLEETVARELQTL 705
Cdd:COG1579 74 RIKKYEEQLGNVRNNKEYEA-LQKEIESLKRRISDLEDEILELMERIEELE---EELAELEAELAELEAELEEKKAEL 147
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
327-469 |
1.96e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 327 KYEEEIRRLykqldDKDDEINqqSQLIEKLKQQMLDQEELLVSTRGD----NEKVQReLSHLQSENDAAKDEVKEVLQAL 402
Cdd:PRK04863 972 SYEDAAEML-----AKNSDLN--EKLRQRLEQAEQERTRAREQLRQAqaqlAQYNQV-LASLKSSYDAKRQMLQELKQEL 1043
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1233951479 403 EELAVNYDqksQEVEEKSQQNQllvDELSQKVATMLSLESELQRlqevsghQRKRIAEVLNGLMKDL 469
Cdd:PRK04863 1044 QDLGVPAD---SGAEERARARR---DELHARLSANRSRRNQLEK-------QLTFCEAEMDNLTKKL 1097
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
597-832 |
2.10e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 41.92 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 597 EPDTQDADEVKKAL-----ELQMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLEL-----EKLQADYEKLKSE 666
Cdd:NF033838 54 ESQKEHAKEVESHLekilsEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELtsktkKELDAAFEQFKKD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 667 EHEKSTKLQELTFLYERHEQSKQDLKglEETVARELQTLHNLRKLFVQDVTTRVKKsAEMEpedsggihsqkqkisflen 746
Cdd:NF033838 134 TLEPGKKVAEATKKVEEAEKKAKDQK--EEDRRNYPTNTYKTLELEIAESDVEVKK-AELE------------------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 747 nleqLTKVHKQLVRDNADLRCELPKLEKRlRATAERVKAL----EGALKEAKEGAMKDKRRYQQEVDRIKEAVRYKSSGK 822
Cdd:NF033838 192 ----LVKEEAKEPRDEEKIKQAKAKVESK-KAEATRLEKIktdrEKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAK 266
|
250
....*....|
gi 1233951479 823 RGHSAQIAKP 832
Cdd:NF033838 267 RGVLGEPATP 276
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
339-450 |
2.42e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 339 LDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHL-QSENDAAKDEVKEVLQALEElavnydqKSQEVE 417
Cdd:smart00787 156 LKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCdPTELDRAKEKLKKLLQEIMI-------KVKKLE 228
|
90 100 110
....*....|....*....|....*....|...
gi 1233951479 418 EKSQQNQLLVDELSQKVATMLSLESELQRLQEV 450
Cdd:smart00787 229 ELEEELQELESKIEDLTNKKSELNTEIAEAEKK 261
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
502-683 |
2.78e-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: 40.29 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 502 ISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHL--EESYDSLSDEL 579
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 580 AKLQAQETVHEvalkdkepdtqdadevKKALELQMEshREAHHRQLARLRDEINEKQKTIDELKdlnQKLQLELEKLQAD 659
Cdd:COG1579 99 ESLKRRISDLE----------------DEILELMER--IEELEEELAELEAELAELEAELEEKK---AELDEELAELEAE 157
|
170 180
....*....|....*....|....*
gi 1233951479 660 YEKLKSEEHEKSTKL-QELTFLYER 683
Cdd:COG1579 158 LEELEAEREELAAKIpPELLALYER 182
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
324-428 |
3.49e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 324 ERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALE 403
Cdd:PHA02562 310 ELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELD 389
|
90 100
....*....|....*....|....*
gi 1233951479 404 ELAVNYDQKSQEVEEKSQQNQLLVD 428
Cdd:PHA02562 390 KIVKTKSELVKEKYHRGIVTDLLKD 414
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
570-680 |
4.29e-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: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 570 ESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKL 649
Cdd:pfam06785 83 EGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEEQLAEKQLLINEYQQTIEEQ 162
|
90 100 110
....*....|....*....|....*....|.
gi 1233951479 650 QLELEKLQADYEKLKSEEHEKSTKLQELTFL 680
Cdd:pfam06785 163 RSVLEKRQDQIENLESKVRDLNYEIKTLLQL 193
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
86-180 |
4.31e-03 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 40.88 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 86 SSPEEILDVIDEGK--SNRHVAVTNMNEHSSRSHSIFLINIKQENMETEQKLsgkLYLVDLAGSEKVSKTgAEGAVLDEA 163
Cdd:COG5059 473 SIPEETSDRVESEKasKLRSSASTKLNLRSSRSHSKFRDHLNGSNSSTKELS---LNQVDLAGSERKVSQ-SVGELLRET 548
|
90
....*....|....*..
gi 1233951479 164 KNINKSLSALGNVISAL 180
Cdd:COG5059 549 QSLNKSLSSLGDVIHAL 565
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
324-450 |
4.56e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 324 ERQKYEEEIRRLYKQLDDKDDEINQ--QSQLIEKLKQQMLDQE----ELLVSTRGDNEKVQRELSHLQSENDAAKDEVKE 397
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEaelaELSARYTPNHPDVIALRAQIAALRAQLQQEAQR 313
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1233951479 398 VLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEV 450
Cdd:COG3206 314 ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVAREL 366
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
325-462 |
5.23e-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: 40.49 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 325 RQKYEEEIRRLYKQLDDKDDEINQ-QSQL---IEKLKQQMLDQEELLVSTRGDNEKVQRELShLQSENDAAKDEVKEVLQ 400
Cdd:pfam05557 81 KKKYLEALNKKLNEKESQLADAREvISCLkneLSELRRQIQRAELELQSTNSELEELQERLD-LLKAKASEAEQLRQNLE 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1233951479 401 ALEELAVNYDQKSQEVE-EKSQQNQ--LLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVL 462
Cdd:pfam05557 160 KQQSSLAEAEQRIKELEfEIQSQEQdsEIVKNSKSELARIPELEKELERLREHNKHLNENIENKL 224
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
625-828 |
5.69e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 625 LARLRDEINEKQKTIDELKDLNQKlqlELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEEtvarELQT 704
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLK---ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE----ELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 705 LHNLRKLFvQDVTTRVKKSAEMEPEDSG--GIHSQKQKISFLENNLEQLTKVHKQLVRD-NADLRCELPKLEKRLRATAE 781
Cdd:COG4717 121 LEKLLQLL-PLYQELEALEAELAELPERleELEERLEELRELEEELEELEAELAELQEElEELLEQLSLATEEELQDLAE 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1233951479 782 RVKALEGALKEAKEgamkDKRRYQQEVDRIKEAVRYKSSGKRGHSAQ 828
Cdd:COG4717 200 ELEELQQRLAELEE----ELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
392-670 |
6.12e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.30 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 392 KDEVKEVLQALeelavnydQKSQEVEeksqqnqllVDELSQKVATmLSLESELQRLQEVSGHQRK--RIAEVLNGLMKDL 469
Cdd:PRK05771 15 KSYKDEVLEAL--------HELGVVH---------IEDLKEELSN-ERLRKLRSLLTKLSEALDKlrSYLPKLNPLREEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 470 SEFSVivgngeiKLPVEISGAIEEEFtvarlyiSKIKSEVKSVVKRCRQLENLqvechrkmevtgrelsscqllISQHEA 549
Cdd:PRK05771 77 KKVSV-------KSLEELIKDVEEEL-------EKIEKEIKELEEEISELENE---------------------IKELEQ 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 550 KIRSLtEYMQSVELK-KRHLEESY--------DSLSDELAKLQAQETVHEVALKDKEPDT-------QDADEVKKalELQ 613
Cdd:PRK05771 122 EIERL-EPWGNFDLDlSLLLGFKYvsvfvgtvPEDKLEELKLESDVENVEYISTDKGYVYvvvvvlkELSDEVEE--ELK 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1233951479 614 MESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEK 670
Cdd:PRK05771 199 KLGFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEY 255
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
535-796 |
6.80e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 535 RELSSCQLLISQHEAKIRSLTEYMQSVE--------LKKRHLEESYDSLSDELAKLQ-AQETV--HEVALKDKEP----- 598
Cdd:COG3096 850 RELAQHRAQEQQLRQQLDQLKEQLQLLNkllpqanlLADETLADRLEELREELDAAQeAQAFIqqHGKALAQLEPlvavl 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 599 --DTQDADEVKKALElQMESHREAHHRQLARLRDEIN--------EKQKTIDELKDLNqklqlelEKLQADYEKLKSEEH 668
Cdd:COG3096 930 qsDPEQFEQLQADYL-QAKEQQRRLKQQIFALSEVVQrrphfsyeDAVGLLGENSDLN-------EKLRARLEQAEEARR 1001
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 669 EKSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHN-LRKLFVQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLEnn 747
Cdd:COG3096 1002 EAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQeLEELGVQADAEAEERARIRRDELHEELSQNRSRRSQLE-- 1079
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1233951479 748 leqltkvhKQLVRDNAdlrcELPKLEKRLRATAERVKALEGALKEAKEG 796
Cdd:COG3096 1080 --------KQLTRCEA----EMDSLQKRLRKAERDYKQEREQVVQAKAG 1116
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
602-809 |
7.15e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 602 DADEVKKALELQmeshreAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLY 681
Cdd:COG1579 2 MPEDLRALLDLQ------ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 682 ERHEQSKQDLKGleetvARELQTLhnlrklfvqdvttrvkkSAEMEpedsggihSQKQKISFLENNLEQLTKVHKQLVRD 761
Cdd:COG1579 76 KKYEEQLGNVRN-----NKEYEAL-----------------QKEIE--------SLKRRISDLEDEILELMERIEELEEE 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1233951479 762 NADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVD 809
Cdd:COG1579 126 LAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
271-468 |
7.48e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 271 IAKLEAELSRWRNgenvpETERLAGEEAALGAELCEETPVNDNSSIVVRIAPEERQkyEEEIRRLYKQLDDKDDEINQQS 350
Cdd:COG4913 619 LAELEEELAEAEE-----RLEALEAELDALQERREALQRLAEYSWDEIDVASAERE--IAELEAELERLDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 351 QLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSEndaaKDEVKEVLQALEELAVNYDQksQEVEEKSQqnQLLVDEL 430
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE----LDELQDRLEAAEDLARLELR--ALLEERFA--AALGDAV 763
|
170 180 190
....*....|....*....|....*....|....*...
gi 1233951479 431 SQKVATmlSLESELQRLQEvsghQRKRIAEVLNGLMKD 468
Cdd:COG4913 764 ERELRE--NLEERIDALRA----RLNRAEEELERAMRA 795
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
321-465 |
7.62e-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: 39.75 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 321 APEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQ 400
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1233951479 401 ALEELAVNYDQKSQEVEEK---SQQN-----------QLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGL 465
Cdd:COG4942 105 ELAELLRALYRLGRQPPLAlllSPEDfldavrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
602-708 |
8.64e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 602 DADEVKKALELQMeshREAHHRQLARLRDEINEKQKtidELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLY 681
Cdd:PRK12704 50 EAEAIKKEALLEA---KEEIHKLRNEFEKELRERRN---ELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQ 123
|
90 100
....*....|....*....|....*..
gi 1233951479 682 ERHEQSKQDLKGLEETVARELQTLHNL 708
Cdd:PRK12704 124 QELEKKEEELEELIEEQLQELERISGL 150
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
572-712 |
9.55e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 39.28 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 572 YDSLSDELAKLQAQETVHEV--ALKDKEPDTQD-ADEVKKAL---ELQMESHREAHHRQLARLRDEINEKQKTI--DELK 643
Cdd:cd22656 103 LADATDDEELEEAKKTIKALldDLLKEAKKYQDkAAKVVDKLtdfENQTEKDQTALETLEKALKDLLTDEGGAIarKEIK 182
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1233951479 644 DLNQKLQLELE----KLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLF 712
Cdd:cd22656 183 DLQKELEKLNEeyaaKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEKLQGAW 255
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
576-834 |
9.93e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 9.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 576 SDELAKLQAQETVHEvaLKDKEPDTQDADEVKKALELQMESHREAHHR-QLARLRDEINEKQ--KTIDELKDLNQK---- 648
Cdd:PTZ00121 1292 ADEAKKAEEKKKADE--AKKKAEEAKKADEAKKKAEEAKKKADAAKKKaEEAKKAAEAAKAEaeAAADEAEAAEEKaeaa 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 649 -LQLELEKLQADYEKLKSEEHEKSTKLQeltflyERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVTTRVKKSAEme 727
Cdd:PTZ00121 1370 eKKKEEAKKKADAAKKKAEEKKKADEAK------KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE-- 1441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233951479 728 pedsggihsQKQKISFLENNLEQLTKVhkqlvrDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMK-DKRRYQQ 806
Cdd:PTZ00121 1442 ---------EAKKADEAKKKAEEAKKA------EEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKaDEAKKAA 1506
|
250 260
....*....|....*....|....*...
gi 1233951479 807 EVDRIKEAVRYKSSGKRGHSAQIAKPVR 834
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEAK 1534
|
|
| |
