|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
15-350 |
6.09e-165 |
|
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: 496.47 E-value: 6.09e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 15 PVRVALRVRPLLPKELLHGHQSCLRVEPERGRITLGRDRHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNATVFAYG 94
Cdd:cd01372 2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 95 QTGSGKTYTMGEASVASLHEDEQGIIPRAMAEAFKLIDE-NDLLDCLVHVSYLELYKEEFRDLLEVGTASR-DIQLREDD 172
Cdd:cd01372 82 QTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKkKDTFEFQLKVSFLEIYNEEIRDLLDPETDKKpTISIREDS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 173 RGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSRLPRPAAGHL--LVSKFHF 250
Cdd:cd01372 162 KGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSADDKNstFTSKFHF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 251 VDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRGSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSS 330
Cdd:cd01372 242 VDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPAD 321
|
330 340
....*....|....*....|
gi 568947414 331 SDFDETLNTLNYASRAQNIR 350
Cdd:cd01372 322 SNFEETLNTLKYANRARNIK 341
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
15-356 |
3.05e-137 |
|
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: 423.14 E-value: 3.05e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 15 PVRVALRVRPLLPKELLHGHQSCLRVEPERGRIT-------LGRDRHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFN 87
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLtvrspknRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 88 ATVFAYGQTGSGKTYTMGEasvaslHEDEQGIIPRAMAEAFKLIDEN-DLLDCLVHVSYLELYKEEFRDLLevGTASRDI 166
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKReEGWQFSVKVSYLEIYNEKIRDLL--NPSSKKL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 167 QLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSRlprpaaGHLLVS 246
Cdd:smart00129 153 EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSS------GSGKAS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRgSHIPYRDSKITRILKDSLGGNAKTVMIACV 326
Cdd:smart00129 227 KLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHIPYRDSKLTRLLQDSLGGNSKTLMIANV 305
|
330 340 350
....*....|....*....|....*....|
gi 568947414 327 SPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:smart00129 306 SPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
21-349 |
7.73e-134 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 413.51 E-value: 7.73e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 21 RVRPLLPKELLHGHQSCLRVEPERGRITL-------GRDRHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNATVFAY 93
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 94 GQTGSGKTYTMGEAsvaslhEDEQGIIPRAMAEAFKLIDEN-DLLDCLVHVSYLELYKEEFRDLLEVGTAS-RDIQLRED 171
Cdd:pfam00225 81 GQTGSGKTYTMEGS------DEQPGIIPRALEDLFDRIQKTkERSEFSVKVSYLEIYNEKIRDLLSPSNKNkRKLRIRED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 172 DRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSRLPrpaagHLLVSKFHFV 251
Cdd:pfam00225 155 PKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEE-----SVKTGKLNLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 252 DLAGSERVLKTG-STGERLKESIQINSTLLALGNVISALGDPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSS 330
Cdd:pfam00225 230 DLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS--KHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSS 307
|
330
....*....|....*....
gi 568947414 331 SDFDETLNTLNYASRAQNI 349
Cdd:pfam00225 308 SNYEETLSTLRFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
15-347 |
5.03e-123 |
|
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: 384.68 E-value: 5.03e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 15 PVRVALRVRPLLPKELLHGHqSCLRVEPERG-RITLGRDRH-----FGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNA 88
Cdd:cd00106 1 NVRVAVRVRPLNGREARSAK-SVISVDGGKSvVLDPPKNRVappktFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 89 TVFAYGQTGSGKTYTMGEASvaslhEDEQGIIPRAMAEAFKLIDENDLLD--CLVHVSYLELYKEEFRDLLEvGTASRDI 166
Cdd:cd00106 80 TIFAYGQTGSGKTYTMLGPD-----PEQRGIIPRALEDIFERIDKRKETKssFSVSASYLEIYNEKIYDLLS-PVPKKPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 167 QLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSrlprpaAGHLLVS 246
Cdd:cd00106 154 SLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKS------GESVTSS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRgsHIPYRDSKITRILKDSLGGNAKTVMIACV 326
Cdd:cd00106 228 KLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNK--HIPYRDSKLTRLLQDSLGGNSKTIMIACI 305
|
330 340
....*....|....*....|.
gi 568947414 327 SPSSSDFDETLNTLNYASRAQ 347
Cdd:cd00106 306 SPSSENFEETLSTLRFASRAK 326
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
16-349 |
4.18e-106 |
|
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: 339.71 E-value: 4.18e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 16 VRVALRVRPLLPKELLHGHQSCLRV---------EPERGRITL-------------GRDRHFGFHVVLGEDTGQEAVYQA 73
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVmdnhmlvfdPKDEEDGFFhggsnnrdrrkrrNKELKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 74 CVQPLLEAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLHEDEQGIIPRAMAEAFKLIDE-NDLLDCLVHVSYLELYKEE 152
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTM------LGTPQEPGLMVLTMKELFKRIESlKDEKEFEVSMSYLEIYNET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 153 FRDLLEvgTASRDIQLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTP 232
Cdd:cd01370 156 IRDLLN--PSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 233 SRLPRPAAGHLLVskfhfVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRGSHIPYRDSKITRILKD 312
Cdd:cd01370 234 SINQQVRQGKLSL-----IDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKNKHIPYRDSKLTRLLKD 308
|
330 340 350
....*....|....*....|....*....|....*..
gi 568947414 313 SLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQNI 349
Cdd:cd01370 309 SLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
16-349 |
7.09e-105 |
|
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: 335.97 E-value: 7.09e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 16 VRVALRVRPLLPKELLHGHQSCLRVEPERGRITL--GRD------RHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFN 87
Cdd:cd01371 3 VKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVrnPKAtaneppKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEGYN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 88 ATVFAYGQTGSGKTYTMGEASVAslhEDEQGIIPRAMAEAFKLID-ENDLLDCLVHVSYLELYKEEFRDLLEVGTASRdI 166
Cdd:cd01371 83 GTIFAYGQTGTGKTYTMEGKRED---PELRGIIPNSFAHIFGHIArSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKR-L 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 167 QLRED-DRGNVV--LCGVKEVDVEGLDEVLSLlemGNAARHTGATHFNRLSSRSHTVFTVTLEQrgrtpSRLPRPAAGHL 243
Cdd:cd01371 159 ELKERpDTGVYVkdLSMFVVKNADEMEHVMNL---GNKNRSVGATNMNEDSSRSHAIFTITIEC-----SEKGEDGENHI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 244 LVSKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPqrRGSHIPYRDSKITRILKDSLGGNAKTVMI 323
Cdd:cd01371 231 RVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KSTHIPYRDSKLTRLLQDSLGGNSKTVMC 308
|
330 340
....*....|....*....|....*.
gi 568947414 324 ACVSPSSSDFDETLNTLNYASRAQNI 349
Cdd:cd01371 309 ANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
16-356 |
6.57e-102 |
|
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.
Pssm-ID: 276816 [Multi-domain] Cd Length: 361 Bit Score: 328.93 E-value: 6.57e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 16 VRVALRVRPLLPKELLHGHQSCLRVEPERGRITLGRDRH------------FGFHVVL----GED---TGQEAVYQACVQ 76
Cdd:cd01365 3 VKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADknnkatrevpksFSFDYSYwshdSEDpnyASQEQVYEDLGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 77 PLLEAFFEGFNATVFAYGQTGSGKTYTMGEAsvaslhEDEQGIIPRAMAEAFKLID--ENDLLDCLVHVSYLELYKEEFR 154
Cdd:cd01365 83 ELLQHAFEGYNVCLFAYGQTGSGKSYTMMGT------QEQPGIIPRLCEDLFSRIAdtTNQNMSYSVEVSYMEIYNEKVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 155 DLLEVGTASRDIQL--REDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRgRTP 232
Cdd:cd01365 157 DLLNPKPKKNKGNLkvREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQK-RHD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 233 SRLPRPAAghlLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQR-----RGSHIPYRDSKIT 307
Cdd:cd01365 236 AETNLTTE---KVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskkKSSFIPYRDSVLT 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 568947414 308 RILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:cd01365 313 WLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
16-349 |
1.26e-101 |
|
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: 326.60 E-value: 1.26e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 16 VRVALRVRPLLPKELLHG--------HQSCLRVEPERGRitlgrdrhFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFN 87
Cdd:cd01374 2 ITVTVRVRPLNSREIGINeqvaweidNDTIYLVEPPSTS--------FTFDHVFGGDSTNREVYELIAKPVVKSALEGYN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 88 ATVFAYGQTGSGKTYTMgeasvaSLHEDEQGIIPRAMAEAFKLIDENDLLDCLVHVSYLELYKEEFRDLLEVGtaSRDIQ 167
Cdd:cd01374 74 GTIFAYGQTSSGKTFTM------SGDEDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLLSPT--SQNLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 168 LREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPsrlprPAAGHLLVSK 247
Cdd:cd01374 146 IRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGE-----LEEGTVRVST 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 248 FHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRGsHIPYRDSKITRILKDSLGGNAKTVMIACVS 327
Cdd:cd01374 221 LNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKVGG-HIPYRDSKLTRILQPSLGGNSRTAIICTIT 299
|
330 340
....*....|....*....|..
gi 568947414 328 PSSSDFDETLNTLNYASRAQNI 349
Cdd:cd01374 300 PAESHVEETLNTLKFASRAKKI 321
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
16-358 |
1.67e-96 |
|
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276815 [Multi-domain] Cd Length: 353 Bit Score: 313.88 E-value: 1.67e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 16 VRVALRVRPLLPKELLHGHQSCLRVEPERGRITL--------GRDRHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFN 87
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 88 ATVFAYGQTGSGKTYTM-GEASVASLHEDEQ----GIIPRAMAEAFKLIDENDLlDCLVHVSYLELYKEEFRDLLEV-GT 161
Cdd:cd01364 84 CTIFAYGQTGTGKTYTMeGDRSPNEEYTWELdplaGIIPRTLHQLFEKLEDNGT-EYSVKVSYLEIYNEELFDLLSPsSD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 162 ASRDIQLREDDR--GNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSrlprpa 239
Cdd:cd01364 163 VSERLRMFDDPRnkRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTID------ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 240 aGHLLV--SKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDpqrRGSHIPYRDSKITRILKDSLGGN 317
Cdd:cd01364 237 -GEELVkiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE---RAPHVPYRESKLTRLLQDSLGGR 312
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 568947414 318 AKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVNWR 358
Cdd:cd01364 313 TKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
16-351 |
5.04e-95 |
|
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: 308.75 E-value: 5.04e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 16 VRVALRVRPLLPKELlHGHQSCLRVEPERG-RITL---GRDRH-FGFHVVLGEDTGQEAVYQAcVQPLLEAFFEGFNATV 90
Cdd:cd01366 4 IRVFCRVRPLLPSEE-NEDTSHITFPDEDGqTIELtsiGAKQKeFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 91 FAYGQTGSGKTYTMgeasvaSLHEDEQGIIPRAMAEAFKLIDENDLLDCLVH--VSYLELYKEEFRDLLEVGTASR---D 165
Cdd:cd01366 82 FAYGQTGSGKTYTM------EGPPESPGIIPRALQELFNTIKELKEKGWSYTikASMLEIYNETIRDLLAPGNAPQkklE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 166 IQlREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLeqRGRTPSRlprpaaGHLLV 245
Cdd:cd01366 156 IR-HDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI--SGRNLQT------GEISV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 246 SKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGdpqRRGSHIPYRDSKITRILKDSLGGNAKTVMIAC 325
Cdd:cd01366 227 GKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR---QKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVN 303
|
330 340
....*....|....*....|....*.
gi 568947414 326 VSPSSSDFDETLNTLNYASRAQNIRN 351
Cdd:cd01366 304 ISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
16-349 |
4.99e-93 |
|
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: 303.10 E-value: 4.99e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 16 VRVALRVRPLLPKELLHGHQSCLRVEPERgRITLGRD---RHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNATVFA 92
Cdd:cd01369 4 IKVVCRFRPLNELEVLQGSKSIVKFDPED-TVVIATSetgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTIFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 93 YGQTGSGKTYTMgeasVASLHEDE-QGIIPRAMAEAFKLIDEND-LLDCLVHVSYLELYKEEFRDLLEVgtaSRD-IQLR 169
Cdd:cd01369 83 YGQTSSGKTYTM----EGKLGDPEsMGIIPRIVQDIFETIYSMDeNLEFHVKVSYFEIYMEKIRDLLDV---SKTnLSVH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 170 EDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTpsrlprpaAGHLLVSKFH 249
Cdd:cd01369 156 EDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVE--------TEKKKSGKLY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 250 FVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSPS 329
Cdd:cd01369 228 LVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK--THIPYRDSKLTRILQDSLGGNSRTTLIICCSPS 305
|
330 340
....*....|....*....|
gi 568947414 330 SSDFDETLNTLNYASRAQNI 349
Cdd:cd01369 306 SYNESETLSTLRFGQRAKTI 325
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
15-356 |
8.08e-86 |
|
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: 283.63 E-value: 8.08e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 15 PVRVALRVRPLLPKELLHGHQSCLRVEPERGRITLG-RDRHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNATVFAY 93
Cdd:cd01373 2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSkPPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 94 GQTGSGKTYTM-GEAS--VASLHEDeQGIIPRAMAEAFKLID-----ENDLLDCLVHVSYLELYKEEFRDLLEvgTASRD 165
Cdd:cd01373 82 GQTGSGKTYTMwGPSEsdNESPHGL-RGVIPRIFEYLFSLIQrekekAGEGKSFLCKCSFLEIYNEQIYDLLD--PASRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 166 IQLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSrlprpaAGHLLV 245
Cdd:cd01373 159 LKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKAC------FVNIRT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 246 SKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGD-PQRRGSHIPYRDSKITRILKDSLGGNAKTVMIA 324
Cdd:cd01373 233 SRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvAHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIA 312
|
330 340 350
....*....|....*....|....*....|..
gi 568947414 325 CVSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:cd01373 313 NVHPSSKCFGETLSTLRFAQRAKLIKNKAVVN 344
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
55-356 |
4.42e-85 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 289.33 E-value: 4.42e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 55 FGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLHEDEQGIIPRAMAEAFKLIDEN 134
Cdd:COG5059 58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTM------SGTEEEPGIIPLSLKELFSKLEDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 135 DLLDCL-VHVSYLELYKEEFRDLLEVGTASRDIqlREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRL 213
Cdd:COG5059 132 SMTKDFaVSISYLEIYNEKIYDLLSPNEESLNI--REDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 214 SSRSHTVFTVTLEQRGRTPSRLPRpaaghllvSKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQ 293
Cdd:COG5059 210 SSRSHSIFQIELASKNKVSGTSET--------SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKK 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568947414 294 RRGsHIPYRDSKITRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:COG5059 282 KSG-HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVN 343
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
15-347 |
3.60e-79 |
|
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: 265.03 E-value: 3.60e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 15 PVRVALRVRPLLPKELLHGHQSCLRVE--------PERGRITLGRDR-------HFGFHVVLGEDTGQEAVYQACVQPLL 79
Cdd:cd01368 2 PVKVYLRVRPLSKDELESEDEGCIEVInsttvvlhPPKGSAANKSERnggqketKFSFSKVFGPNTTQKEFFQGTALPLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 80 EAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLHEDEQGIIPRAMAEAFKLIDENDlldclVHVSYLELYKEEFRDLLEV 159
Cdd:cd01368 82 QDLLHGKNGLLFTYGVTNSGKTYTM------QGSPGDGGILPRSLDVIFNSIGGYS-----VFVSYIEIYNEYIYDLLEP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 160 GTASRD-----IQLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQrgrtpsr 234
Cdd:cd01368 151 SPSSPTkkrqsLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQ------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 235 LPRPAAGHLL-------VSKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRG--SHIPYRDSK 305
Cdd:cd01368 224 APGDSDGDVDqdkdqitVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGtnKMVPFRDSK 303
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 568947414 306 ITRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQ 347
Cdd:cd01368 304 LTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
15-345 |
3.44e-78 |
|
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: 261.46 E-value: 3.44e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 15 PVRVALRVRPLLPKELLHGHQ--------SCLRVEPERGRITLGR--DRH-FGFHVVLGEDTGQEAVYQACVQPLLEAFF 83
Cdd:cd01367 1 KIKVCVRKRPLNKKEVAKKEIdvvsvpskLTLIVHEPKLKVDLTKyiENHtFRFDYVFDESSSNETVYRSTVKPLVPHIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 84 EGFNATVFAYGQTGSGKTYTMGEASvaSLHEDEQGIIPRAMAEAFKLIDE-NDLLDCLVHVSYLELYKEEFRDLLEVGTa 162
Cdd:cd01367 81 EGGKATCFAYGQTGSGKTYTMGGDF--SGQEESKGIYALAARDVFRLLNKlPYKDNLGVTVSFFEIYGGKVFDLLNRKK- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 163 srDIQLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLeqrgrtpsrlpRPAAGH 242
Cdd:cd01367 158 --RVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL-----------RDRGTN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 243 LLVSKFHFVDLAGSER-VLKTGSTGERLKESIQINSTLLALGNVISALGDPQrrgSHIPYRDSKITRILKDSL-GGNAKT 320
Cdd:cd01367 225 KLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNK---AHIPFRGSKLTQVLKDSFiGENSKT 301
|
330 340
....*....|....*....|....*
gi 568947414 321 VMIACVSPSSSDFDETLNTLNYASR 345
Cdd:cd01367 302 CMIATISPGASSCEHTLNTLRYADR 326
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
15-347 |
7.77e-78 |
|
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: 260.13 E-value: 7.77e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 15 PVRVALRVRPLLPKELLHGHQSCLRVEPERgRITLGRDRHFG------FHVVLGEDTGQEAVYQACVQPLLEAFFEGFNA 88
Cdd:cd01376 1 NVRVAVRVRPFVDGTAGASDPSCVSGIDSC-SVELADPRNHGetlkyqFDAFYGEESTQEDIYAREVQPIVPHLLEGQNA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 89 TVFAYGQTGSGKTYTM-GeasvaslHEDEQGIIPRAMAEAFKLIDENDLLDClVHVSYLELYKEEFRDLLEVgtASRDIQ 167
Cdd:cd01376 80 TVFAYGSTGAGKTFTMlG-------SPEQPGLMPLTVMDLLQMTRKEAWALS-FTMSYLEIYQEKILDLLEP--ASKELV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 168 LREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRT-PSRLPRpaaghllvS 246
Cdd:cd01376 150 IREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLaPFRQRT--------G 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRgshIPYRDSKITRILKDSLGGNAKTVMIACV 326
Cdd:cd01376 222 KLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPR---IPYRDSKLTRLLQDSLGGGSRCIMVANI 298
|
330 340
....*....|....*....|.
gi 568947414 327 SPSSSDFDETLNTLNYASRAQ 347
Cdd:cd01376 299 APERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
55-345 |
1.87e-72 |
|
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: 245.57 E-value: 1.87e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 55 FGFHVVLgEDTGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMGEASVASLHedeQGIIPRAMAEAFKLIDEN 134
Cdd:cd01375 50 FKFDGVL-HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENYKH---RGIIPRALQQVFRMIEER 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 135 DLLDCLVHVSYLELYKEEFRDLL----EVGTASRDIQLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHF 210
Cdd:cd01375 126 PTKAYTVHVSYLEIYNEQLYDLLstlpYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTM 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 211 NRLSSRSHTVFTVTLEQRGRTPSrlprpaAGHLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALG 290
Cdd:cd01375 206 NKNSSRSHCIFTIHLEAHSRTLS------SEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALS 279
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568947414 291 DPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASR 345
Cdd:cd01375 280 DKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASR 332
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
10-356 |
8.60e-59 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 222.89 E-value: 8.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 10 GAEEAPVRVALRVRPLLPKEllhghQSCLRVEPERGRITLGRDRHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNAT 89
Cdd:PLN03188 94 GVSDSGVKVIVRMKPLNKGE-----EGEMIVQKMSNDSLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 90 VFAYGQTGSGKTYTM-GEASVAS---LHEDEQGIIPRAMAEAFKLIDENDL------LDCLVHVSYLELYKEEFRDLLEv 159
Cdd:PLN03188 169 VFAYGQTGSGKTYTMwGPANGLLeehLSGDQQGLTPRVFERLFARINEEQIkhadrqLKYQCRCSFLEIYNEQITDLLD- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 160 gTASRDIQLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSrlprPA 239
Cdd:PLN03188 248 -PSQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVA----DG 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 240 AGHLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRGS--HIPYRDSKITRILKDSLGGN 317
Cdd:PLN03188 323 LSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKqrHIPYRDSRLTFLLQESLGGN 402
|
330 340 350
....*....|....*....|....*....|....*....
gi 568947414 318 AKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:PLN03188 403 AKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVN 441
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
705-1202 |
1.99e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.99 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 705 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASE 784
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 785 RSRLQEfrKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELER-NVQLMRRQQGQLQRRLREETEQKRRLETEMNK 863
Cdd:COG1196 304 IARLEE--RRRELEERLEELEEELAELEEELEELEEELEELEEELEEaEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 864 RQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsvVSLEQQQIEEQKKwLDQEMEKVLQQRRALEELGEELRKR 943
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERL------ERLEEELEELEEA-LAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 944 EVILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQ----NQQQIRGEIDTLRQ--- 1016
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAlllaGLRGLAGAVAVLIGvea 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1017 -------------------EKDSLLKQRLEIDSKLRQG-----------SLLSPEEERTLFQLDEAIEALDAAIEYKNEA 1066
Cdd:COG1196 535 ayeaaleaalaaalqnivvEDDEVAAAAIEYLKAAKAGratflpldkirARAALAAALARGAIGAAVDLVASDLREADAR 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1067 ITCRQRVLRASASLLSQCEM--NLMAKLSYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEV 1144
Cdd:COG1196 615 YYVLGDTLLGRTLVAARLEAalRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE 694
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 568947414 1145 ALERQRLEMDRQLTLQQKEHEQNVQLLLQQGRDHLGEGLADSKRQYEARIHALEKELG 1202
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA 752
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
707-1217 |
8.03e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.06 E-value: 8.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 707 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREP----QDA 782
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAeleeELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 783 SERSRLQEFRKRVAAAQSQVQVLKEK-KQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEM 861
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAElAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 862 NKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsVVSLEQQQIEEQKKWLDQEMEKVLQQRRALEELGEELR 941
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE-----EAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 942 KREVILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEksgQLRQGSAQNQQQIRGEIDTLRQEKDSL 1021
Cdd:COG1196 489 AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA---ALEAALAAALQNIVVEDDEVAAAAIEY 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1022 LKQ----RLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEM--NLMAKLSY- 1094
Cdd:COG1196 566 LKAakagRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAalRRAVTLAGr 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1095 ------------LSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQK 1162
Cdd:COG1196 646 lrevtlegeggsAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1163 EHEQNVQLLLQQGRDHLGEGLADSKRQYE-----ARIHALEKELgrhmwinQELKQKLSA 1217
Cdd:COG1196 726 LEEQLEAEREELLEELLEEEELLEEEALEelpepPDLEELEREL-------ERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
730-1066 |
2.34e-14 |
|
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: 78.56 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 730 GELVRTG---------KAAQALNRQhsQRIRELEQEAERVRAELCEGQRQLRELEgrepqdaSERSRLQ-EFRKRVAAAQ 799
Cdd:TIGR02168 652 GDLVRPGgvitggsakTNSSILERR--REIEELEEKIEELEEKIAELEKALAELR-------KELEELEeELEQLRKELE 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 800 SQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQ 879
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 880 KILKIKTEEI------AAFQRKRRSGSNGSVVSLEQQ--QIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVILAKKE 951
Cdd:TIGR02168 803 EALDELRAELtllneeAANLRERLESLERRIAATERRleDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 952 ALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRqgsaQNQQQIRGEIDTLRQEKDSLLKQRLEIDSK 1031
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE----LRLEGLEVRIDNLQERLSEEYSLTLEEAEA 958
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 568947414 1032 LRQGSLLSPEE-ERTLFQLDEAIEA-----LDAAIEYKNEA 1066
Cdd:TIGR02168 959 LENKIEDDEEEaRRRLKRLENKIKElgpvnLAAIEEYEELK 999
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
712-1134 |
1.18e-11 |
|
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: 69.28 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 712 QQKIREL-AINIRMKEELIGELVRTGKAAQALNRQHSQrIRELEQEAERVRAELCEGQRQL-------RELEGREPQDAS 783
Cdd:TIGR04523 217 ESQISELkKQNNQLKDNIEKKQQEINEKTTEISNTQTQ-LNQLKDEQNKIKKQLSEKQKELeqnnkkiKELEKQLNQLKS 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 784 ERSRL-----QEFRKRVaaaQSQVQVLKEKKQATERLVSlsaQSETRLQELERNVQLMRrqqgqlqrrlreetEQKRRLE 858
Cdd:TIGR04523 296 EISDLnnqkeQDWNKEL---KSELKNQEKKLEEIQNQIS---QNNKIISQLNEQISQLK--------------KELTNSE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 859 TEMNKRQhrvKELElkhEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQIEEQKKWLDQEMEKVLQQRRALEELGE 938
Cdd:TIGR04523 356 SENSEKQ---RELE---EKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 939 ELRKrEVILAKKE--ALMQEKTGLES-----KRLRSSQ-----ALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQq 1006
Cdd:TIGR04523 430 RLKE-TIIKNNSEikDLTNQDSVKELiiknlDNTRESLetqlkVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE- 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1007 IRGEIDTLRQEKDSLL-------KQRLEIDSKLRQ--GSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITcrqrvlras 1077
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKekiekleSEKKEKESKISDleDELNKDDFELKKENLEKEIDEKNKEIEELKQTQK--------- 578
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 568947414 1078 aSLLSqcemnlmaklsylSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEE 1134
Cdd:TIGR04523 579 -SLKK-------------KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
18-288 |
2.01e-11 |
|
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: 63.90 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 18 VALRVRPLLpkellhghqsclRVEPERGRITLGRDRHFGFHvvlgedTGQEAVYqACVQPLLEAFFEGFN-ATVFAYGQT 96
Cdd:cd01363 1 VLVRVNPFK------------ELPIYRDSKIIVFYRGFRRS------ESQPHVF-AIADPAYQSMLDGYNnQSIFAYGES 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 97 GSGKTYTMgeasvaslhedeQGIIPRAMAEAFklidendlldclvhvSYLELYKEEFRDLLEvgtasrdiqlreddrgnv 176
Cdd:cd01363 62 GAGKTETM------------KGVIPYLASVAF---------------NGINKGETEGWVYLT------------------ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 177 vlcgvkEVDVEGLDEVLSLLEMGNAARhTGATHFNRLSSRSHTVFTVtleqrgrtpsrlprpaaghllvskfhFVDLAGS 256
Cdd:cd01363 97 ------EITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI--------------------------LLDIAGF 143
|
250 260 270
....*....|....*....|....*....|..
gi 568947414 257 ERvlktgstgerlkesiqINSTLLALGNVISA 288
Cdd:cd01363 144 EI----------------INESLNTLMNVLRA 159
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
705-1215 |
3.17e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.17 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 705 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQ------ALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGRE 778
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELKELKEKAEeyiklsEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 779 PQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETR-LQELERNVQLMRRQQGQLQRRLREETEQKRRL 857
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLtPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 858 ETEMNKRQHRVKEL------------ELKHEQQQKILKIKTEEIAafqrkrrsgsngsvvsleqqQIEEQKKWLDQEMEK 925
Cdd:PRK03918 418 KKEIKELKKAIEELkkakgkcpvcgrELTEEHRKELLEEYTAELK--------------------RIEKELKEIEEKERK 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 926 VlqqRRALEELGEELRKREVILAKKEALMQektgLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLR--QGSAQN 1003
Cdd:PRK03918 478 L---RKELRELEKVLKKESELIKLKELAEQ----LKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKslKKELEK 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1004 QQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEertlfqLDEAIEALDAAIEYKNEAITCRQRvLRASASLLSQ 1083
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE------LEERLKELEPFYNEYLELKDAEKE-LEREEKELKK 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1084 CEMNLMAKLSYLSSSETRallckyfdkVVTLREEQHQQQIAFSElemqlEEQQRlvywlevaLERQRLEMDRQLTLQQKE 1163
Cdd:PRK03918 624 LEEELDKAFEELAETEKR---------LEELRKELEELEKKYSE-----EEYEE--------LREEYLELSRELAGLRAE 681
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 568947414 1164 HEQnvqllLQQGRDHLGEGLADSKRQYEARIHALE--KELGRHMWINQELKQKL 1215
Cdd:PRK03918 682 LEE-----LEKRREEIKKTLEKLKEELEEREKAKKelEKLEKALERVEELREKV 730
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
708-1034 |
1.29e-10 |
|
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: 65.81 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 708 LAQAQQKIRELAINIRMKEELIGELvrtgkaaqalNRQHSQ---RIRELEQEAERVRAELCEGQRQLRELEgREPQdase 784
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQNNKIISQL----------NEQISQlkkELTNSESENSEKQRELEEKQNEIEKLK-KENQ---- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 785 rSRLQEFRKrvaaAQSQVQVLKEKKQATERLvslSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKR 864
Cdd:TIGR04523 381 -SYKQEIKN----LESQINDLESKIQNQEKL---NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 865 QHRVKELELKHEQQQKILKIKTEEIAAFQRKrrsgsngsvvsLEQQQIEEQKKwlDQEMEKVLQQRRALEELGEELRKR- 943
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQN-----------LEQKQKELKSK--EKELKKLNEEKKELEEKVKDLTKKi 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 944 EVILAKKEALMQEKTGLESKrLRSsqaLNEDIVRVSSRL--EHLEKELSEKsgqlrqgsaqNQqqirgEIDTLRQEKDSL 1021
Cdd:TIGR04523 520 SSLKEKIEKLESEKKEKESK-ISD---LEDELNKDDFELkkENLEKEIDEK----------NK-----EIEELKQTQKSL 580
|
330
....*....|...
gi 568947414 1022 LKQRLEIDSKLRQ 1034
Cdd:TIGR04523 581 KKKQEEKQELIDQ 593
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
708-1034 |
1.48e-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: 66.23 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 708 LAQAQQKIRELAINIRMKEELI-------GELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQ 780
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLeelrlevSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 781 DASERSRLQEfrkrvaaaqsqvqvlkekkqaterlvsLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETE 860
Cdd:TIGR02168 328 LESKLDELAE---------------------------ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 861 MNKRQHRVKELELKHEQQQKILKIkteeiaafQRKRRSGSNGSVVSLEQQQIEEQKKWLDQEMEKVLQQRRALEELGEEL 940
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIER--------LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 941 RKR-EVILAKKEALMQEKTGLESKRlrssQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSA--QNQQQIRGEIDtlrqe 1017
Cdd:TIGR02168 453 QEElERLEEALEELREELEEAEQAL----DAAERELAQLQARLDSLERLQENLEGFSEGVKAllKNQSGLSGILG----- 523
|
330
....*....|....*..
gi 568947414 1018 kdsLLKQRLEIDSKLRQ 1034
Cdd:TIGR02168 524 ---VLSELISVDEGYEA 537
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
748-1083 |
1.60e-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: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 748 QRIRELEQEAERVRAELCEGQRQLRELEgrepQDASERSRLQEFRKRVAAAQSQVQVLkekkqateRLVSLSAQSETRLQ 827
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSLE----RQAEKAERYKELKAELRELELALLVL--------RLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 828 ELERNVQLMRrqqgqlqrrlrEETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAfqrkrrsgsngsvvsl 907
Cdd:TIGR02168 247 ELKEAEEELE-----------ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR---------------- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 908 eqqqIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEK 987
Cdd:TIGR02168 300 ----LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 988 ELSEKSGQLRQGSAQNQQQIR-----------------GEIDTLRQEKDSLLKQRLEIDSKLRQGSLlsPEEERTLFQLD 1050
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIAslnneierlearlerleDRRERLQQEIEELLKKLEEAELKELQAEL--EELEEELEELQ 453
|
330 340 350
....*....|....*....|....*....|...
gi 568947414 1051 EAIEALDAAIEYKNEAITCRQRVLRASASLLSQ 1083
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
849-1227 |
3.02e-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: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 849 EETEQKRRlETEMN-----------KRQhrVKELELKHEQQQKILKIKTEEiaafQRKRRSGSNGSVVSLEQQ--QIEEQ 915
Cdd:TIGR02168 175 KETERKLE-RTRENldrledilnelERQ--LKSLERQAEKAERYKELKAEL----RELELALLVLRLEELREEleELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 916 KKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLrssQALNEDIVRVSSRLEHLEKELSEKSGQ 995
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI---SRLEQQKQILRERLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 996 LRQGSAQNQQQIRgEIDTLRQEKDSLLKQRLEIDSKLrqgsllsPEEERTLFQLDEAIEALDAAIEYKNEAItcrqrvlr 1075
Cdd:TIGR02168 325 LEELESKLDELAE-ELAELEEKLEELKEELESLEAEL-------EELEAELEELESRLEELEEQLETLRSKV-------- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1076 asASLLSQcEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERqrleMDR 1155
Cdd:TIGR02168 389 --AQLELQ-IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELER----LEE 461
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568947414 1156 QLTLQQKEHEQNVQLLLQQGRDHlgegladskRQYEARIHALEKELGRHMWINQELKQKLSAGSTAGQSRGC 1227
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAEREL---------AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV 524
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
716-1061 |
4.52e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.32 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 716 RELAINIRMKEeLIGELVRTGKAAQALNRQHSQRI---RELEQEAERVRAELCEGQRQLrelegrepqdASERSRLQEFR 792
Cdd:TIGR02169 633 RRLMGKYRMVT-LEGELFEKSGAMTGGSRAPRGGIlfsRSEPAELQRLRERLEGLKREL----------SSLQSELRRIE 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 793 KRVAAAQSQVQVlkekkqATERLVSLSAQSETRLQELERNVQLMRRQQgqlqRRLREETEQKRRLETEMNKRQHRVKELE 872
Cdd:TIGR02169 702 NRLDELSQELSD------ASRKIGEIEKEIEQLEQEEEKLKERLEELE----EDLSSLEQEIENVKSELKELEARIEELE 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 873 LK-HEQQQKILKIKT-------EEIAA---FQRKRRSGSNGSVVSLEQ--QQIEEQKKWLDQEMEKVLQQRRALEELGEE 939
Cdd:TIGR02169 772 EDlHKLEEALNDLEArlshsriPEIQAelsKLEEEVSRIEARLREIEQklNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 940 LRKR-EVILAKKEALMQEktgLESKRLRSSQalnedivrVSSRLEHLEKELSEKSGQLRQgSAQNQQQIRGEIDTLR--- 1015
Cdd:TIGR02169 852 IEKEiENLNGKKEELEEE---LEELEAALRD--------LESRLGDLKKERDELEAQLRE-LERKIEELEAQIEKKRkrl 919
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 568947414 1016 ---QEKDSLLKQRL-EIDSKLRQGSlLSPEEERTLFQLDEAIEALDAAIE 1061
Cdd:TIGR02169 920 selKAKLEALEEELsEIEDPKGEDE-EIPEEELSLEDVQAELQRVEEEIR 968
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
709-1067 |
1.09e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 709 AQAQQKIREL---AINIRMKEELigelvrTGKAAQALNRQHSQRIRELEQEAERVRAElCEGQRQLRELEGRepqdASER 785
Cdd:PTZ00121 1414 AAAKKKADEAkkkAEEKKKADEA------KKKAEEAKKADEAKKKAEEAKKAEEAKKK-AEEAKKADEAKKK----AEEA 1482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 786 SRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLEtEMNKRQ 865
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAE 1561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 866 HRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQIEEQKKWLDQEMEKVLQQRRALEEL--------- 936
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKkkveqlkkk 1641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 937 -------GEELRKREVILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKElSEKSGQLRQGSAQNQ---QQ 1006
Cdd:PTZ00121 1642 eaeekkkAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE-AKKAEELKKKEAEEKkkaEE 1720
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568947414 1007 IRGEiDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAI 1067
Cdd:PTZ00121 1721 LKKA-EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
16-157 |
1.90e-09 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 57.62 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 16 VRVALRVRPLLPKELlhghqsclRVEPERGRITLGRDRH----FGFHVVLGEDTGQEAVYQACVQpLLEAFFEGFNATVF 91
Cdd:pfam16796 22 IRVFARVRPELLSEA--------QIDYPDETSSDGKIGSknksFSFDRVFPPESEQEDVFQEISQ-LVQSCLDGYNVCIF 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568947414 92 AYGQTGSGKTYTMgeasvaslhedeqgiIPRAMAEAFKLIDENDLLDCL-VHVSYLELYKEEFRDLL 157
Cdd:pfam16796 93 AYGQTGSGSNDGM---------------IPRAREQIFRFISSLKKGWKYtIELQFVEIYNESSQDLL 144
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
707-1083 |
3.53e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 707 RLAQAQQKIRELAINIRMKEELIGELVRTGK---AAQALNRQHSQRIRELEQ--EAERVRAELCEGQRQLRELEGREPQD 781
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEeleELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 782 ASERSRLQEFRKRVAAAQSQVQVLKEkkQATERLVSLSAQSETRLQELERNVQlmrrqqgQLQRRLREETEQKRRLETEM 861
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQE--ELEELLEQLSLATEEELQDLAEELE-------ELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 862 NKRQHRVKELELKHEQQQKILKIKTEEIAAF------------------------------------------------Q 893
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsliltiagvlflvlgllallflllarekaslgK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 894 RKRRSGSNGSVVSLEQQQIEEQKK--------------WLDQEMEKVLQQRRALEELGEELRkREVILAKKEALMQEKTG 959
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAalglppdlspeellELLDRIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 960 LESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQ--------QQIRGEIDTLRQEKDSLLKQRLEIDSK 1031
Cdd:COG4717 382 EDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeeleeelEELEEELEELEEELEELREELAELEAE 461
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 568947414 1032 LRQgsllsPEEERTLFQLDEAIEALDAAIEYKNEAItcrqRVLRASASLLSQ 1083
Cdd:COG4717 462 LEQ-----LEEDGELAELLQELEELKAELRELAEEW----AALKLALELLEE 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
750-1134 |
3.81e-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: 61.62 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 750 IRELEQEAERVRAELCEGQRQLRELEGREPQDASERSRLQefrkrvaaaqsqvqvlKEKKQATERLVSLSAQSETRLQEL 829
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLR----------------REREKAERYQALLKEKREYEGYEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 830 ERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQ-QQKILKIKTEEIAAFQRKRRSgsngsvVSLE 908
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGE------LEAE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 909 QQQIEEQKKWLDQEMEKVLQQRRALEELgeelrkREVILAKKEALMQEktgLESKRLRSSQalnedivrVSSRLEHLEKE 988
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEAE------IDKLLAEIEELERE---IEEERKRRDK--------LTEEYAELKEE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 989 LSEKSGQLRQGSAQNqQQIRGEIDTLRQEKDSLLKqrlEIDSKLRQGSLLSPEEERtlfqLDEAIEALDAAIEYKNEAIT 1068
Cdd:TIGR02169 366 LEDLRAELEEVDKEF-AETRDELKDYREKLEKLKR---EINELKRELDRLQEELQR----LSEELADLNAAIAGIEAKIN 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568947414 1069 CRQRVLRASASLLSQCEMNLMaklsylsssETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEE 1134
Cdd:TIGR02169 438 ELEEEKEDKALEIKKQEWKLE---------QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
796-1040 |
5.28e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 796 AAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKH 875
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 876 EQQQKILKIKTEEIAAFQRKR-RSGSNGSVVSLEQQQIEEQKKWLDQEMEKVLQQRRA-LEELGEELRKREVILAKKEAL 953
Cdd:COG4942 93 AELRAELEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREqAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 954 MQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQgSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLR 1033
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE-LQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
....*..
gi 568947414 1034 QGSLLSP 1040
Cdd:COG4942 252 KGKLPWP 258
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
705-1202 |
7.28e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 7.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 705 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQ---RIRELEQEAERVRAELCEGQRQLRELEGREPQD 781
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEElekELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 782 ASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLEtem 861
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE--- 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 862 nkrqhrvkELELKHEQQQKILKIKTEeiAAFQRKRRSGSNGSVVSLEQQQIEEQKKWLDQEMEKVLQQRRALEELGEELR 941
Cdd:PRK03918 356 --------ELEERHELYEEAKAKKEE--LERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 942 K----------------REVILAKKEALMQEKTgLESKRLRSSQALNEDIVR-VSSRLEHLEKELSEKSGQLRqgsaqnQ 1004
Cdd:PRK03918 426 KaieelkkakgkcpvcgRELTEEHRKELLEEYT-AELKRIEKELKEIEEKERkLRKELRELEKVLKKESELIK------L 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1005 QQIRGEIDTLRQEKDSLLKQRLEIDSKLRQ----------GSLLSPEEErtLFQLDEAIEALDAAIEYKNEAITCRQRVL 1074
Cdd:PRK03918 499 KELAEQLKELEEKLKKYNLEELEKKAEEYEklkekliklkGEIKSLKKE--LEKLEELKKKLAELEKKLDELEEELAELL 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1075 RASASLLSQCEMNLMAKLSYLSSSETRALLCKyfDKVVTLREEQHQQQIAFSELEMQLEEQQRlvywLEVALERQRLEMD 1154
Cdd:PRK03918 577 KELEELGFESVEELEERLKELEPFYNEYLELK--DAEKELEREEKELKKLEEELDKAFEELAE----TEKRLEELRKELE 650
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 568947414 1155 R-QLTLQQKEHEQNVQLLLQQGRDHLG-----EGLADSKRQYEARIHALEKELG 1202
Cdd:PRK03918 651 ElEKKYSEEEYEELREEYLELSRELAGlraelEELEKRREEIKKTLEKLKEELE 704
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
703-1033 |
7.41e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 7.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 703 ASEWRLAQAQQKIRELAiniRMKEELIGELVRTGKAAQALNR--QHSQRIRELEQEAERVRAELCEGQRQLRELEgrEPQ 780
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEA---KKADEAKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKKADEAKKAEEAKKAD--EAK 1540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 781 DASERSRLQEFRK--RVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRrlreETEQKRRLE 858
Cdd:PTZ00121 1541 KAEEKKKADELKKaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM----KAEEAKKAE 1616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 859 TEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQIEEQKKWLDQEMEKVLQQRRALEELG- 937
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKk 1696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 938 --EELRKREViLAKKEALMQEKtgleSKRLRSSQALNEDIVRVSSRLEHLEKELSE---KSGQLRQGSAQNQQQIRGEID 1012
Cdd:PTZ00121 1697 eaEEAKKAEE-LKKKEAEEKKK----AEELKKAEEENKIKAEEAKKEAEEDKKKAEeakKDEEEKKKIAHLKKEEEKKAE 1771
|
330 340
....*....|....*....|..
gi 568947414 1013 TLRQEKDSLLKQRL-EIDSKLR 1033
Cdd:PTZ00121 1772 EIRKEKEAVIEEELdEEDEKRR 1793
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
697-894 |
3.04e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 697 QAPAAMASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEg 776
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 777 repqdASERSRLQEFRKRVAAAQ-----SQVQVL---KEKKQATERLVSLSAQSETR----------LQELERNVQLMRR 838
Cdd:COG4942 97 -----AELEAQKEELAELLRALYrlgrqPPLALLlspEDFLDAVRRLQYLKYLAPARreqaeelradLAELAALRAELEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568947414 839 QQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQR 894
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
708-1018 |
3.11e-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: 58.54 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 708 LAQAQQKIRELAINIRMKEELIGEL-VRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERS 786
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELnKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEID 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 787 RLQEFRKRVAAAQSQVQVLKEkkQATERLVSLSAQSETRLQELErnvqlmrrqqgqlqrrlrEETEQKRRLETEMNKRQH 866
Cdd:TIGR02169 333 KLLAEIEELEREIEEERKRRD--KLTEEYAELKEELEDLRAELE------------------EVDKEFAETRDELKDYRE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 867 RVKELELKHEQqqkilkIKTEEIAAFQRKRRSGSNGSVVSLEQQQIEEQKKWLDQEMEkvlqqrraleELGEELRKREvi 946
Cdd:TIGR02169 393 KLEKLKREINE------LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE----------DKALEIKKQE-- 454
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568947414 947 lakkEALMQEKTGLESKRlrssqalnEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEK 1018
Cdd:TIGR02169 455 ----WKLEQLAADLSKYE--------QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
813-1191 |
7.76e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 57.29 E-value: 7.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 813 ERLVSLSAQSETRLQEL--ERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQhrvkelELKHEQQQKILKIKTEEIA 890
Cdd:pfam02463 154 RRLEIEEEAAGSRLKRKkkEALKKLIEETENLAELIIDLEELKLQELKLKEQAKK------ALEYYQLKEKLELEEEYLL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 891 A----FQRKRRSGSNGSVVSLEQQQIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLR 966
Cdd:pfam02463 228 YldylKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 967 SSQALNEDIVRVSSRLEHLEKELSEKSGQLRQgsAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTL 1046
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEE--LEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1047 FQLDEAIEALDAAIEYK-----NEAITCRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQHQQ 1121
Cdd:pfam02463 386 LSSAAKLKEEELELKSEeekeaQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL 465
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1122 QIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNVQLLLQQGRDHLGEGLADSKRQYE 1191
Cdd:pfam02463 466 ELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG 535
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
931-1235 |
8.22e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 8.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 931 RALEELGEELRKREvilaKKEALMQEKTGLESKRLRSSQALNEdivrVSSRLEHLEKELSEKSGQLRQgSAQNQQQIRGE 1010
Cdd:TIGR02169 668 FSRSEPAELQRLRE----RLEGLKRELSSLQSELRRIENRLDE----LSQELSDASRKIGEIEKEIEQ-LEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1011 IDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAA--------IEYKNEAITCRQRVLRASASLLS 1082
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsripeIQAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1083 QCEMNLMAKLSYLSSS----ETRALLCKyfDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLE---VALERQRLEMDR 1155
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEiqelQEQRIDLK--EQIKSIEKEIENLNGKKEELEEELEELEAALRDLEsrlGDLKKERDELEA 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1156 QLT-LQQKEHEQNVQllLQQGRDHLGEgLADSKRQYEARIHALEKELGRHMWINQELkqkLSAGSTAGQSRGCERRSLCL 1234
Cdd:TIGR02169 897 QLReLERKIEELEAQ--IEKKRKRLSE-LKAKLEALEEELSEIEDPKGEDEEIPEEE---LSLEDVQAELQRVEEEIRAL 970
|
.
gi 568947414 1235 E 1235
Cdd:TIGR02169 971 E 971
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
740-1200 |
1.44e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 740 QALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLS 819
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 820 AQSEtRLQELERNVQlmrrqqgqlqrRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSG 899
Cdd:COG4717 129 PLYQ-ELEALEAELA-----------ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 900 SNGSVVSLEQQ--QIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGL----ESKRLRSSQALNE 973
Cdd:COG4717 197 LAEELEELQQRlaELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLallgLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 974 DIVRVSSRLEHLEKELSEKSGQLRQgSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLrqgsllSPEEERTLFQLDEAI 1053
Cdd:COG4717 277 GVLFLVLGLLALLFLLLAREKASLG-KEAEELQALPALEELEEEELEELLAALGLPPDL------SPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1054 EALDAAIEYKNEAITcRQRVLRASASLLSQCEMnlmaklsylSSSETRALLCKYFDKVVTLREEqhqqqiaFSELEMQLE 1133
Cdd:COG4717 350 QELLREAEELEEELQ-LEELEQEIAALLAEAGV---------EDEEELRAALEQAEEYQELKEE-------LEELEEQLE 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568947414 1134 E-----QQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNV-------QLLLQQGRDHLGEGLADSKRQYEARIHALEKE 1200
Cdd:COG4717 413 EllgelEELLEALDEEELEEELEELEEELEELEEELEELReelaeleAELEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
695-1180 |
2.02e-07 |
|
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: 55.75 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 695 TRQAPAAMASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKA-AQALNRQHSQRI----RELEQEAERVRAELCEG-Q 768
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVvLARLLELQEEPCplcgSCIHPNPARQDIDNPGPlT 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 769 RQLRELEGREPQDASE----RSRLQEFRKRVAAAQSQVQVLKEKKQA-TERLVSLSAQSETRLQELERNVQLMRRQQGQL 843
Cdd:TIGR00618 528 RRMQRGEQTYAQLETSeedvYHQLTSERKQRASLKEQMQEIQQSFSIlTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 844 QRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIaafqrkrrsgsngsvvSLEQQQIEEQKKWLDQEM 923
Cdd:TIGR00618 608 DMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQL----------------TLTQERVREHALSIRVLP 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 924 EKVLQQRRALEElgEELRKREVILAKKEALMQEKTGLESkrlrssqalnedivrvssrLEHLEKELSEKSGQLRQGSAQN 1003
Cdd:TIGR00618 672 KELLASRQLALQ--KMQSEKEQLTYWKEMLAQCQTLLRE-------------------LETHIEEYDREFNEIENASSSL 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1004 QQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLrasASLLSQ 1083
Cdd:TIGR00618 731 GSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLL---KTLEAE 807
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1084 CEMNLMAKLSYLSSSETraLLCKYFDKVVTLREEQHQQQIAFSELEMQLEE-----QQRLVYWLEVALERQRLEMDRQLT 1158
Cdd:TIGR00618 808 IGQEIPSDEDILNLQCE--TLVQEEEQFLSRLEEKSATLGEITHQLLKYEEcskqlAQLTQEQAKIIQLSDKLNGINQIK 885
|
490 500
....*....|....*....|....*....
gi 568947414 1159 -------LQQKEHEQNVQLLLQQGRDHLG 1180
Cdd:TIGR00618 886 iqfdgdaLIKFLHEITLYANVRLANQSEG 914
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
705-1201 |
2.31e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 705 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGR--EPQDA 782
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRleELEEQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 783 SE--RSRLQEFRKRVAAAQSQVQVLKEKKQATE-RLVSLSAQSETRLQELERN-VQLMRRQQGQLQRRLREETEQKRRLE 858
Cdd:TIGR02168 381 LEtlRSKVAQLELQIASLNNEIERLEARLERLEdRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 859 TEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSN---------------GSVVSLEQQQIEEQKKWlDQEM 923
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegvkallknqsglSGILGVLSELISVDEGY-EAAI 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 924 EKVL-------------QQRRALEELGEELRKREVILA---KKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLE---- 983
Cdd:TIGR02168 540 EAALggrlqavvvenlnAAKKAIAFLKQNELGRVTFLPldsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkals 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 984 ----------------HLEKELSE-------------KSGQLRQGSAQNQQQI---RGEIDTLRQEK------------- 1018
Cdd:TIGR02168 620 yllggvlvvddldnalELAKKLRPgyrivtldgdlvrPGGVITGGSAKTNSSIlerRREIEELEEKIeeleekiaeleka 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1019 -DSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEykneaiTCRQRVLRASASLLSQcEMNLMAKLSYLSS 1097
Cdd:TIGR02168 700 lAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE------QLEERIAQLSKELTEL-EAEIEELEERLEE 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1098 SETRALLCKyfDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDrQLTLQQKEHEQNVQLLLQQGRD 1177
Cdd:TIGR02168 773 AEEELAEAE--AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE-SLERRIAATERRLEDLEEQIEE 849
|
570 580
....*....|....*....|....*.
gi 568947414 1178 --HLGEGLADSKRQYEARIHALEKEL 1201
Cdd:TIGR02168 850 lsEDIESLAAEIEELEELIEELESEL 875
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
742-1204 |
3.62e-07 |
|
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: 54.97 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 742 LNRQHS--QRIRELEQEAERVRAE---LCEGQRQLRELEGR-EPQDASERSrlqeFRKRVAAAQSQVQVLKekkqatERL 815
Cdd:TIGR00618 371 SCQQHTltQHIHTLQQQKTTLTQKlqsLCKELDILQREQATiDTRTSAFRD----LQGQLAHAKKQQELQQ------RYA 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 816 VSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRK 895
Cdd:TIGR00618 441 ELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDI 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 896 RRSGSNGSVVsleqQQIEEQKKWLDQEMEKVLQQrraleelGEELRKREVILAKKEALMQEKTGLESKRLRSSQALNEDI 975
Cdd:TIGR00618 521 DNPGPLTRRM----QRGEQTYAQLETSEEDVYHQ-------LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 976 VRVSSRLEHLEKELSEKSGQLRQgsAQNQQQIRGEIDTLRQEKDSLLKQrleIDSKLRQGSLLSPEEERTLFQLDEAIEA 1055
Cdd:TIGR00618 590 QNITVRLQDLTEKLSEAEDMLAC--EQHALLRKLQPEQDLQDVRLHLQQ---CSQELALKLTALHALQLTLTQERVREHA 664
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1056 LdAAIEYKNEAITCRQRVLRASASLLSQCEMN---LMAKLSYLSSSETrallckyfdKVVTLREEQHQQQIAFSELEMQL 1132
Cdd:TIGR00618 665 L-SIRVLPKELLASRQLALQKMQSEKEQLTYWkemLAQCQTLLRELET---------HIEEYDREFNEIENASSSLGSDL 734
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568947414 1133 EEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNVQLLLQQGRD--HLGEGLADSKRQYEARIHALEKELGRH 1204
Cdd:TIGR00618 735 AAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAElsHLAAEIQFFNRLREEDTHLLKTLEAEI 808
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
694-1083 |
3.91e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 694 QTRQAPAAMASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRE 773
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 774 LEgrEPQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLsaQSETRLQELERNVQLMRRQQGQLQRRLREETEQ 853
Cdd:COG1196 426 LE--EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL--LEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 854 KRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQ---QQIEEQKKWLDQEMEKVLQQR 930
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEvaaAAIEYLKAAKAGRATFLPLDK 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 931 RALEELGEELRKREVILAKKEALMQEKTGLESKRLRSSQAL------NEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQ 1004
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLlgrtlvAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568947414 1005 QQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQ 1083
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
705-1034 |
4.10e-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: 54.69 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 705 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELcegQRQLRELEGREPQDASE 784
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL---KELEARIEELEEDLHKL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 785 RSRLQEFRKRVaaAQSQVQVLKEKKQATERLVSlsaQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKR 864
Cdd:TIGR02169 778 EEALNDLEARL--SHSRIPEIQAELSKLEEEVS---RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 865 QHRVKELELKHEQQQKILkiktEEIAAFQRKRRSgsngsvvslEQQQIEEQKKWLDQEMEKVLQQRRALEELGEELRKR- 943
Cdd:TIGR02169 853 EKEIENLNGKKEELEEEL----EELEAALRDLES---------RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRl 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 944 EVILAKKEALMQEKTGLE--SKRLRSSQALNEDIVRVSSRLEHLEKELSE------------KSGQLRQGSAQNQQQirg 1009
Cdd:TIGR02169 920 SELKAKLEALEEELSEIEdpKGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnmlaiqeyEEVLKRLDELKEKRA--- 996
|
330 340
....*....|....*....|....*
gi 568947414 1010 eidTLRQEKDSLLKQRLEIDSKLRQ 1034
Cdd:TIGR02169 997 ---KLEEERKAILERIEEYEKKKRE 1018
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
708-1177 |
5.75e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 54.35 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 708 LAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQR---IRELEQEAERVRAElCEGQ--RQLRELEGREPQDA 782
Cdd:pfam15921 383 LADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRnmeVQRLEALLKAMKSE-CQGQmeRQMAAIQGKNESLE 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 783 SERSRLQEFRKRVAAAQSQVQVLKEKK---QATERLVSlsaQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLET 859
Cdd:pfam15921 462 KVSSLTAQLESTKEMLRKVVEELTAKKmtlESSERTVS---DLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKN 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 860 EMNKRQHRVKE---LELKHEQQQKILKIKTEEIAAF-QRKRRSGSNGSVVSLEQQQIEEQKKwlDQEMEkvLQQRRALEE 935
Cdd:pfam15921 539 EGDHLRNVQTEceaLKLQMAEKDKVIEILRQQIENMtQLVGQHGRTAGAMQVEKAQLEKEIN--DRRLE--LQEFKILKD 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 936 lGEELRKREvILAKKEALMQEKTGL---ESKRLRS--------SQALNE------DIVRVSSRLEHLEKELSEKSGQLRQ 998
Cdd:pfam15921 615 -KKDAKIRE-LEARVSDLELEKVKLvnaGSERLRAvkdikqerDQLLNEvktsrnELNSLSEDYEVLKRNFRNKSEEMET 692
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 999 GSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDeaieALDAAIEYKNEAITC---RQRVLR 1075
Cdd:pfam15921 693 TTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQID----ALQSKIQFLEEAMTNankEKHFLK 768
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1076 ASASLLSQcemnlmaKLSYLSSSETRALlckyfdkvvtlreeqhqqqiafSELEMQLEEQQRL---VYWLEVALERQRLE 1152
Cdd:pfam15921 769 EEKNKLSQ-------ELSTVATEKNKMA----------------------GELEVLRSQERRLkekVANMEVALDKASLQ 819
|
490 500
....*....|....*....|....*
gi 568947414 1153 MDRQLTLQQKEHEQNVQLLLQQGRD 1177
Cdd:pfam15921 820 FAECQDIIQRQEQESVRLKLQHTLD 844
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
749-1217 |
8.95e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 8.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 749 RIRELEQEAERVraelcegQRQLRELEGREPQDASERSRLQEFRKRVAAaqsqvqvLKEKKQATERLVSLSAQSETRLQE 828
Cdd:PRK03918 194 LIKEKEKELEEV-------LREINEISSELPELREELEKLEKEVKELEE-------LKEEIEELEKELESLEGSKRKLEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 829 LERNVQlmrrqqgqlqrrlrEETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEeiaafqrkrrsgsngsvvsle 908
Cdd:PRK03918 260 KIRELE--------------ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEE--------------------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 909 qqqIEEQKKWLDQEMEKVLQQRRALEELGEELRKREvilAKKEALMQEKTGLESK--RLRSSQALNEDIVRVSSRLEHLE 986
Cdd:PRK03918 305 ---YLDELREIEKRLSRLEEEINGIEERIKELEEKE---ERLEELKKKLKELEKRleELEERHELYEEAKAKKEELERLK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 987 KELSEKSgqlrqgsaqnQQQIRGEIDTLRQEKDSLLKQRLEIDSKLrqGSLLSPEEERtlfqlDEAIEALDAAieyKNEA 1066
Cdd:PRK03918 379 KRLTGLT----------PEKLEKELEELEKAKEEIEEEISKITARI--GELKKEIKEL-----KKAIEELKKA---KGKC 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1067 ITCRqrvlrasASLLSQCEMNLMAKLSyLSSSETRALLCKYFDKVVTLREEqhqqqiaFSELEMQLEEQQRLVYWLEVAL 1146
Cdd:PRK03918 439 PVCG-------RELTEEHRKELLEEYT-AELKRIEKELKEIEEKERKLRKE-------LRELEKVLKKESELIKLKELAE 503
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568947414 1147 ERQRLEmdrqltlqQKEHEQNVQLLLQQGRDHlgEGLADSKRQYEARIHALEKELGRhmwiNQELKQKLSA 1217
Cdd:PRK03918 504 QLKELE--------EKLKKYNLEELEKKAEEY--EKLKEKLIKLKGEIKSLKKELEK----LEELKKKLAE 560
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
602-1191 |
1.11e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 602 KAEVLAQADKLRSASST----TSEEEGEEEEEEEEEEEEPPRRTLYLRR----NGISNWSQRAGLSPGSPPDRKGPEVCP 673
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDArkaeAARKAEEERKAEEARKAEDAKKAEAVKKaeeaKKDAEEAKKAEEERNNEEIRKFEEARM 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 674 EEPAAAIPAPQAVGSGKVPVQTRQAPAAMASEWRLAQAQQKIREL---AINIRMKEELIGELVRTGKAAQALNRQHSQR- 749
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAkkkAEEAKKADEAKKKAEEAKKKADAAKKKAEEAk 1342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 750 ----IRELEQEAERVRAELCEGQRQLRELEGREP--------QDASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVS 817
Cdd:PTZ00121 1343 kaaeAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkkadaakKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE 1422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 818 LSAQSE--TRLQELERNVQlmrrqQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKI----LKIKTEEIAA 891
Cdd:PTZ00121 1423 AKKKAEekKKADEAKKKAE-----EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkadeAKKKAEEAKK 1497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 892 FQRKRRSGSNGSVVSLEQQQIEEQKKWLD----------QEMEKVLQQRRAlEEL--GEELRKREVILAKKEALMQEKTG 959
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKKAEEAKKADEakkaeeakkaDEAKKAEEKKKA-DELkkAEELKKAEEKKKAEEAKKAEEDK 1576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 960 LESKRlRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQgsAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLS 1039
Cdd:PTZ00121 1577 NMALR-KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK--AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1040 PEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNLMAKlsylsssETRALLCKYFDKVVTLREEQH 1119
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE-------ELKKKEAEEKKKAEELKKAEE 1726
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568947414 1120 QQQIAFSELEMQLEEQQRlvywlevALERQRLEMDRQLTLQQ--KEHEQNVQLLLQQGRDHLGEGL--ADSKRQYE 1191
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKK-------KAEEAKKDEEEKKKIAHlkKEEEKKAEEIRKEKEAVIEEELdeEDEKRRME 1795
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
696-955 |
2.21e-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: 52.05 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 696 RQAPAAMASEWRLAQAQQKIRELAINIRMKEELIGELVRTgkaAQALNRQHSQRIR--ELEQEAERVRA-ELCEGQRQLR 772
Cdd:pfam17380 314 RRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI---RQEERKRELERIRqeEIAMEISRMRElERLQMERQQK 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 773 ELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATE-RLVSLSAQSETRLQELERnVQLMRRQQGQLQRRLREET 851
Cdd:pfam17380 391 NERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEaRQREVRRLEEERAREMER-VRLEEQERQQQVERLRQQE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 852 EQKRRLETEMNKRQHRVKELElkhEQQQKILKIKTEE----IAAFQRKRR------SGSNGSVVSLEQQQIEEQKKWLDQ 921
Cdd:pfam17380 470 EERKRKKLELEKEKRDRKRAE---EQRRKILEKELEErkqaMIEEERKRKllekemEERQKAIYEEERRREAEEERRKQQ 546
|
250 260 270
....*....|....*....|....*....|....
gi 568947414 922 EMEKVLQQRRALEELGEELRKREVILAKKEALMQ 955
Cdd:pfam17380 547 EMEERRRIQEQMRKATEERSRLEAMEREREMMRQ 580
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
708-1034 |
3.23e-06 |
|
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: 51.90 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 708 LAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQE----AERVRAELCEGQRQLRELE---GREPQ 780
Cdd:pfam02463 671 LTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAeellADRVQEAQDKINEELKLLKqkiDEEEE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 781 DASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETE 860
Cdd:pfam02463 751 EEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKI 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 861 MNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKR--RSGSNGSVVSLEQQ---QIEEQKKWLDQEMEKVLQQRRALEE 935
Cdd:pfam02463 831 KEEELEELALELKEEQKLEKLAEEELERLEEEITKEelLQELLLKEEELEEQklkDELESKEEKEKEEKKELEEESQKLN 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 936 LGEELRKREVILAKKEALMQEKTGLESKRLRSSQALNED---------IVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQ 1006
Cdd:pfam02463 911 LLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEkeennkeeeEERNKRLLLAKEELGKVNLMAIEEFEEKEERY 990
|
330 340 350
....*....|....*....|....*....|
gi 568947414 1007 --IRGEIDTLRQEKDSLLKQRLEIDSKLRQ 1034
Cdd:pfam02463 991 nkDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
700-1220 |
4.43e-06 |
|
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: 51.28 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 700 AAMASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQR---IRELEQEAERVRAELCEGQRQL----- 771
Cdd:pfam05557 35 KASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYleaLNKKLNEKESQLADAREVISCLknels 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 772 ---RELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLmRRQQGQLQRRLR 848
Cdd:pfam05557 115 elrRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQS-QEQDSEIVKNSK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 849 EETEQKRRLETEMNKRQHRVKELelkHEQQQKILKIKtEEIAAFQRK--RRSGSNGSVVSLE------QQQIEEQKKwLD 920
Cdd:pfam05557 194 SELARIPELEKELERLREHNKHL---NENIENKLLLK-EEVEDLKRKleREEKYREEAATLElekeklEQELQSWVK-LA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 921 QEMEKVLQQRRALEELGEELRKREVilakkeALMQEKTGLES--KRLRSSQALNEDIVRV-SSRLEHLEKELSEKSGQLR 997
Cdd:pfam05557 269 QDTGLNLRSPEDLSRRIEQLQQREI------VLKEENSSLTSsaRQLEKARRELEQELAQyLKKIEDLNKKLKRHKALVR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 998 QgsaqNQQQIRgeidTLRQEKDsLLKQRLE-IDSKLRqgsllspEEERTLFQLDEAIEALDAAIEYKNEAITCRQRV--- 1073
Cdd:pfam05557 343 R----LQRRVL----LLTKERD-GYRAILEsYDKELT-------MSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLsva 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1074 LRASASLLSQCEMnLMAKLSYLSSSETRALLCKYFDKVVTLREEqhqqqiaFSELEMQLEEQQRLVYWLEVALERQrlem 1153
Cdd:pfam05557 407 EEELGGYKQQAQT-LERELQALRQQESLADPSYSKEEVDSLRRK-------LETLELERQRLREQKNELEMELERR---- 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568947414 1154 drqlTLQQKEHEQNVQLLlqqgrdHLGEG-LADSKRQYEARIHALEKELGRHMWINQELKQKLSAGST 1220
Cdd:pfam05557 475 ----CLQGDYDPKKTKVL------HLSMNpAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLR 532
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
708-1027 |
4.49e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.27 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 708 LAQAQQKIRELAINIRMKEELIGELVRTGkaaqalNRQHSQRIRELEQEAERVRAELCEGQRQLRElegrepqdasersR 787
Cdd:pfam15921 283 LTEKASSARSQANSIQSQLEIIQEQARNQ------NSMYMRQLSDLESTVSQLRSELREAKRMYED-------------K 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 788 LQEFRKRVAAAQSQvqvLKEKKQATERLVSLSAQSETRLQELERNVQlmrrqqgqlqrrlreETEQKRRLETEMNKR--- 864
Cdd:pfam15921 344 IEELEKQLVLANSE---LTEARTERDQFSQESGNLDDQLQKLLADLH---------------KREKELSLEKEQNKRlwd 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 865 ---------QHRVKELELKHEQQQKilkikteeIAAFQRKRRSGSNGsvvSLEQQQIEEQKKwlDQEMEKVLQQRRALEE 935
Cdd:pfam15921 406 rdtgnsitiDHLRRELDDRNMEVQR--------LEALLKAMKSECQG---QMERQMAAIQGK--NESLEKVSSLTAQLES 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 936 LGEELRK-------REVILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELseksgQLRQGSAQNQQQIR 1008
Cdd:pfam15921 473 TKEMLRKvveeltaKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQEL-----QHLKNEGDHLRNVQ 547
|
330 340
....*....|....*....|....*
gi 568947414 1009 GEIDTLR---QEKD---SLLKQRLE 1027
Cdd:pfam15921 548 TECEALKlqmAEKDkviEILRQQIE 572
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
778-1034 |
4.83e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 778 EPQDASER-SRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQK-R 855
Cdd:COG4913 219 EEPDTFEAaDALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAElE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 856 RLETEMNKRQHRVKELELKHEQQQkilkikTEEIAAFQRKRRSGSNgsvvslEQQQIEEQKKWLDQEMEKVLQQRRALEE 935
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALR------EELDELEAQIRGNGGD------RLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 936 LGEELrkrevilakKEALMQEKTGLESKRLRSSQALNEdivrVSSRLEHLEKELSEKSGQLRQGsaqnqqqiRGEIDTLR 1015
Cdd:COG4913 367 LLAAL---------GLPLPASAEEFAALRAEAAALLEA----LEEELEALEEALAEAEAALRDL--------RRELRELE 425
|
250
....*....|....*....
gi 568947414 1016 QEKDSLLKQRLEIDSKLRQ 1034
Cdd:COG4913 426 AEIASLERRKSNIPARLLA 444
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
728-1166 |
9.46e-06 |
|
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: 50.11 E-value: 9.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 728 LIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELcegQRQLRELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKE 807
Cdd:pfam05483 350 VVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMEL---QKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQ 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 808 KKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQ---QQKILKI 884
Cdd:pfam05483 427 FEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKlllENKELTQ 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 885 KTEEIAAFQRKRRSGSNGSvvsleQQQIEEQKKWLDQEMEKVLQQRRALEELGEEL-RKREVILAKKEALMQEKTGLESK 963
Cdd:pfam05483 507 EASDMTLELKKHQEDIINC-----KKQEERMLKQIENLEEKEMNLRDELESVREEFiQKGDEVKCKLDKSEENARSIEYE 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 964 RLRSSQAL-------NEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKD-SLLKQRLE--IDSKLR 1033
Cdd:pfam05483 582 VLKKEKQMkilenkcNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELElASAKQKFEeiIDNYQK 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1034 QGSLLSPEEERTLFQLDEAIEALDAAIEYKNEA-ITCRQRVLRASAsllsqcemnLMAKLSYlsssetrallckYFDKVV 1112
Cdd:pfam05483 662 EIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIdKRCQHKIAEMVA---------LMEKHKH------------QYDKII 720
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 568947414 1113 tlrEEQHQQQIAFSELEmqlEEQQRLVYWLEVALERQRLEM---DRQLTLQQKEHEQ 1166
Cdd:pfam05483 721 ---EERDSELGLYKNKE---QEQSSAKAALEIELSNIKAELlslKKQLEIEKEEKEK 771
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
921-1061 |
1.04e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 921 QEMEKVLQQRRALE---ELGEELRKREVILAKKEALM--------QEKTGLESKRLRSSQA----LNEDIVRVSSRLEHL 985
Cdd:COG4913 242 EALEDAREQIELLEpirELAERYAAARERLAELEYLRaalrlwfaQRRLELLEAELEELRAelarLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568947414 986 EKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIE 1061
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE 397
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
908-1191 |
1.17e-05 |
|
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: 50.06 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 908 EQQQIEEQKKWLDQEMEKVLQQRRALEELGEELRKREvilakkealmqektgleskrlrssQALNEDIVRVSSRLEHLEK 987
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKEL------------------------EELSRQISALRKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 988 ElseksgqlRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAI 1067
Cdd:TIGR02168 741 E--------VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1068 TCRQRVLRASASLLSQCEMNLMAKLSYLssSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALE 1147
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRL--EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 568947414 1148 RQRLEMDrQLTLQQKEHEQNVQlLLQQGRDHLGEGLADSKRQYE 1191
Cdd:TIGR02168 891 LLRSELE-ELSEELRELESKRS-ELRRELEELREKLAQLELRLE 932
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
745-1080 |
1.34e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.91 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 745 QHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERSR---LQEFRKRVAAAQSQVQ-VLKEKKQATERLVSLSA 820
Cdd:PRK11281 77 RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLStlsLRQLESRLAQTLDQLQnAQNDLAEYNSQLVSLQT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 821 QSE----------TRLQELerNVQLMRRQQGQLQRRLreetEQKRRLETEMnkrqhrvKELELKHEQQQKILKIKTEEIA 890
Cdd:PRK11281 157 QPEraqaalyansQRLQQI--RNLLKGGKVGGKALRP----SQRVLLQAEQ-------ALLNAQNDLQRKSLEGNTQLQD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 891 AFQRKRrsgsngSVVSLEQQQIEEQKKWLdQEMekVLQQRRAL-EELGEELRKREVI-------LAKKEalMQEKTGLES 962
Cdd:PRK11281 224 LLQKQR------DYLTARIQRLEHQLQLL-QEA--INSKRLTLsEKTVQEAQSQDEAariqanpLVAQE--LEINLQLSQ 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 963 KRLRSSQALNE---DIVRVSSRLEHL---EKELSEKSGQLrQGSAQ-----NQQQ------------------IRGEIDT 1013
Cdd:PRK11281 293 RLLKATEKLNTltqQNLRVKNWLDRLtqsERNIKEQISVL-KGSLLlsrilYQQQqalpsadliegladriadLRLEQFE 371
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568947414 1014 LRQEKDSLLKQRLEIDSKLR-QGSLLSPEEERTLFQ--------LDEAIEALDAAIeykNEAITC---RQRVLRASASL 1080
Cdd:PRK11281 372 INQQRDALFQPDAYIDKLEAgHKSEVTDEVRDALLQllderrelLDQLNKQLNNQL---NLAINLqlnQQQLLSVSDSL 447
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
835-1066 |
1.45e-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: 48.99 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 835 LMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGsngsvvsleQQQIEE 914
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL---------EQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 915 QKKWLDQEMEKVLQQRRALEELGEELRKREVILAK-------KEALMQEKTGLESKRLRSSQALN-------EDIVRVSS 980
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRlgrqpplALLLSPEDFLDAVRRLQYLKYLAparreqaEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 981 RLEHLEKELSEKSGQLRQGSAQNQQQiRGEIDTLRQEKDSLLKQrLEIDSKLRQGSLLSPEEERTlfQLDEAIEALDAAI 1060
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEE-RAALEALKAERQKLLAR-LEKELAELAAELAELQQEAE--ELEALIARLEAEA 236
|
....*.
gi 568947414 1061 EYKNEA 1066
Cdd:COG4942 237 AAAAER 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
703-943 |
1.47e-05 |
|
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: 49.67 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 703 ASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELE------- 775
Cdd:TIGR02168 800 ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELEseleall 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 776 ----GREPQDASERSRLQEFRKRVAAAQSQVQvlkEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREET 851
Cdd:TIGR02168 880 neraSLEEALALLRSELEELSEELRELESKRS---ELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEA 956
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 852 EQK-RRLETEMNKRQHRVKELElkheqqQKILKIKTEEIAAFQrkrrsgsngsvvslEQQQIEEQKKWLDQEMEKVLQQR 930
Cdd:TIGR02168 957 EALeNKIEDDEEEARRRLKRLE------NKIKELGPVNLAAIE--------------EYEELKERYDFLTAQKEDLTEAK 1016
|
250
....*....|...
gi 568947414 931 RALEELGEELRKR 943
Cdd:TIGR02168 1017 ETLEEAIEEIDRE 1029
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
900-1065 |
1.66e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.37 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 900 SNGSVVSLEQQQIEEQKKWLDQEMEKVLQQRRALEELGEELR-KREVILAKKEALMQEKTGLESKRlrssQALNEDIVRV 978
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAeKRDELNAQVKELREEAQELREKR----DELNEKVKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 979 SSRLEHLEKELSEKSGQLRQGSAQNQQQI--RGEIDTLRQEKDSLLKQrleidsklRQGSLLSPEEERTLF----QLDEA 1052
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELNkaGGSIDKLRKEIERLEWR--------QQTEVLSPEEEKELVekikELEKE 148
|
170
....*....|...
gi 568947414 1053 IEALDAAIEYKNE 1065
Cdd:COG1340 149 LEKAKKALEKNEK 161
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
709-1181 |
1.76e-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: 49.66 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 709 AQAQQKIRElaINIRMKEELIGELVRTGKAAQALNRQHSQRiRELEQEAERVR------AELCEGQRQLR-ELEGREPQD 781
Cdd:TIGR00606 545 MDKDEQIRK--IKSRHSDELTSLLGYFPNKKQLEDWLHSKS-KEINQTRDRLAklnkelASLEQNKNHINnELESKEEQL 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 782 AS-------------ERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSA--------------QSETRLQELERNVQ 834
Cdd:TIGR00606 622 SSyedklfdvcgsqdEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTdenqsccpvcqrvfQTEAELQEFISDLQ 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 835 LMRRQQgqlqrrlreETEQKRrLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGsvVSLEQQQIEE 914
Cdd:TIGR00606 702 SKLRLA---------PDKLKS-TESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRD--IQRLKNDIEE 769
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 915 QKKWL-----DQEMEKVLQQR-RALEELGEELRKREVILAKKEALMQEKTGleskrLRSSQALNEdivRVSSRLEHLEKE 988
Cdd:TIGR00606 770 QETLLgtimpEEESAKVCLTDvTIMERFQMELKDVERKIAQQAAKLQGSDL-----DRTVQQVNQ---EKQEKQHELDTV 841
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 989 LSEksGQLRQGSAQNQQQirgEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAIT 1068
Cdd:TIGR00606 842 VSK--IELNRKLIQDQQE---QIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLET 916
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1069 CRQRVLRASASLLSQCEM-NLMAKLSYLSSSETRALLCKY----FDKVVTLREEQ-HQQQIAFSELEMQLEEQQRLVYWL 1142
Cdd:TIGR00606 917 FLEKDQQEKEELISSKETsNKKAQDKVNDIKEKVKNIHGYmkdiENKIQDGKDDYlKQKETELNTVNAQLEECEKHQEKI 996
|
490 500 510
....*....|....*....|....*....|....*....
gi 568947414 1143 EVALERQRLEMDRQltlQQKEHEQNVQLLLQQGRDHLGE 1181
Cdd:TIGR00606 997 NEDMRLMRQDIDTQ---KIQERWLQDNLTLRKRENELKE 1032
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
721-1047 |
2.20e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 721 NIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELegrepqdaseRSRLQEFRKRVAAAQS 800
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKEL----------REEAQELREKRDELNE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 801 QVQVLKEKKQAterlvsLSAQSETRLQELERnvqlmrrqqgqlqrrLREETEQKRRLETEMNKRQHRVKELELKheQQQK 880
Cdd:COG1340 72 KVKELKEERDE------LNEKLNELREELDE---------------LRKELAELNKAGGSIDKLRKEIERLEWR--QQTE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 881 ILKIKTE-----EIAAFQRKRRsgsngsvvslEQQQIEEQKKWLDQEMEKVLQQRRALEELGEELRK-REVILAKKEALM 954
Cdd:COG1340 129 VLSPEEEkelveKIKELEKELE----------KAKKALEKNEKLKELRAELKELRKEAEEIHKKIKElAEEAQELHEEMI 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 955 QEKTGLESKRlRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRqgsaQNQQQIRGEIDTLR-----QEKDSLLKQRLEID 1029
Cdd:COG1340 199 ELYKEADELR-KEADELHKEIVEAQEKADELHEEIIELQKELR----ELRKELKKLRKKQRalkreKEKEELEEKAEEIF 273
|
330
....*....|....*...
gi 568947414 1030 SKLRQGSLLSPEEERTLF 1047
Cdd:COG1340 274 EKLKKGEKLTTEELKLLQ 291
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
725-1058 |
3.26e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 725 KEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERSR-----------LQEFRK 793
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDElrereaeleatLRTARE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 794 RVAAAQ------------------SQVQVLKEKKQATERLVSLSAQSETRLQELERNVqlmrrqqgqlqrrlrEETEQKR 855
Cdd:PRK02224 441 RVEEAEalleagkcpecgqpvegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERL---------------ERAEDLV 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 856 RLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAafqrkrRSGSNGSVVSLEQQQIEEQKKWLDQEMEKVL-------Q 928
Cdd:PRK02224 506 EAEDRIERLEERREDLEELIAERRETIEEKRERAE------ELRERAAELEAEAEEKREAAAEAEEEAEEAReevaelnS 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 929 QRRALEELGEELRKREVILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLE---HLEKELS----EKSGQLRQGSA 1001
Cdd:PRK02224 580 KLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRErkrELEAEFDeariEEAREDKERAE 659
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 568947414 1002 QNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQgsLLSPEEERTlfQLDEAIEALDA 1058
Cdd:PRK02224 660 EYLEQVEEKLDELREERDDLQAEIGAVENELEE--LEELRERRE--ALENRVEALEA 712
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
734-1033 |
3.44e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.68 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 734 RTGKAAQALNRQHSqRIRELEQEAERVRAELCEGQRQLrELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATE 813
Cdd:pfam12128 605 RLDKAEEALQSARE-KQAAAEEQLVQANGELEKASREE-TFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANE 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 814 RLVSLSAQsetrLQELERNVQLMrrqqgqlqrrLREETEQKRRLETEMNKrqhrvKELELKHEQQQKILKIKtEEIAAfq 893
Cdd:pfam12128 683 RLNSLEAQ----LKQLDKKHQAW----------LEEQKEQKREARTEKQA-----YWQVVEGALDAQLALLK-AAIAA-- 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 894 rkRRSGSNGSVVSLEQQQIEEQKKwLDQEMEKVL---QQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLrssqa 970
Cdd:pfam12128 741 --RRSGAKAELKALETWYKRDLAS-LGVDPDVIAklkREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRL----- 812
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568947414 971 lnedivrvSSRLEHLEKELSEKSGQLrqgsAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLR 1033
Cdd:pfam12128 813 --------ATQLSNIERAISELQQQL----ARLIADTKLRRAKLEMERKASEKQQVRLSENLR 863
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
707-834 |
3.46e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 707 RLAQAQQKIRELAINIRMKEELIGELVRTGkAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERS 786
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQSP-VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ 312
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568947414 787 R-LQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQ 834
Cdd:COG3206 313 RiLASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
852-1217 |
1.05e-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: 46.94 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 852 EQKRRLETEMNKRQhrvKELELKHEQQQKILK-IKTEEiaafqrKRRSGSNGSVVSLEqQQIEEQKKWLDQEMEKVLQQR 930
Cdd:TIGR04523 117 EQKNKLEVELNKLE---KQKKENKKNIDKFLTeIKKKE------KELEKLNNKYNDLK-KQKEELENELNLLEKEKLNIQ 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 931 RALEELGEELRKREVILAKKEALMQEKTGLESKRL---RSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQ--- 1004
Cdd:TIGR04523 187 KNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISelkKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNkik 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1005 ------------------------QQIRGEIDTLRQEK----DSLLKQRLE-IDSKLRQGSLLSPEEERTLFQLDEAIEA 1055
Cdd:TIGR04523 267 kqlsekqkeleqnnkkikelekqlNQLKSEISDLNNQKeqdwNKELKSELKnQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1056 LDAAIEYKNEAITCRQRVLRASASLLSQCEMNlmaKLSYLSSSetrallckyfdkvvtlreEQHQQQIafSELEMQLEEQ 1135
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKE---NQSYKQEI------------------KNLESQI--NDLESKIQNQ 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1136 qrlvywlevalERQRLEMDRQLTLQQKEH---EQNVQLLLQQGRDhlgegLADSKRQYEARIHALEKELGRHMWINQELK 1212
Cdd:TIGR04523 404 -----------EKLNQQKDEQIKKLQQEKellEKEIERLKETIIK-----NNSEIKDLTNQDSVKELIIKNLDNTRESLE 467
|
....*
gi 568947414 1213 QKLSA 1217
Cdd:TIGR04523 468 TQLKV 472
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
703-955 |
2.16e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.88 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 703 ASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDA 782
Cdd:pfam15921 552 ALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 783 SERSRLqefrkrVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGqlqrrlreetEQKRRLETEMN 862
Cdd:pfam15921 632 LEKVKL------VNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFR----------NKSEEMETTTN 695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 863 KRQHRVKELELKHEQQQKILKI------KTEEIAAFQRKRRSGSNGSVVSL----------------EQQQIEEQKKWLD 920
Cdd:pfam15921 696 KLKMQLKSAQSELEQTRNTLKSmegsdgHAMKVAMGMQKQITAKRGQIDALqskiqfleeamtnankEKHFLKEEKNKLS 775
|
250 260 270
....*....|....*....|....*....|....*
gi 568947414 921 QEMEKVLQQRRALEELGEELRKREVILAKKEALMQ 955
Cdd:pfam15921 776 QELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
602-1167 |
2.28e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 602 KAEVLAQADKLRSASSTTSEEEGEEEEEEEE----EEEEPPRRTLYLRRNGIsnwSQRAGLSPGSPPDRKGPEVCPEEPA 677
Cdd:PTZ00121 1117 AEEAKKKAEDARKAEEARKAEDARKAEEARKaedaKRVEIARKAEDARKAEE---ARKAEDAKKAEAARKAEEVRKAEEL 1193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 678 AAIPAPQAVGSGKVPVQTRQAPAA-MASEWRLAQAQQKIRElainIRMKEEligelvrtgKAAQALNRQHSQRIRELEQE 756
Cdd:PTZ00121 1194 RKAEDARKAEAARKAEEERKAEEArKAEDAKKAEAVKKAEE----AKKDAE---------EAKKAEEERNNEEIRKFEEA 1260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 757 -----AERVRAELCEGQRQLRELEGREPQDASERSRLQEFRKRVAAAQSQVQvlkEKKQATErlvsLSAQSETRLQELER 831
Cdd:PTZ00121 1261 rmahfARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAE---EAKKADE----AKKKAEEAKKKADA 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 832 NVQLMRRQQGQLQRRLREETEQKRRLEtemnKRQHRVKELELKHEQQQK---ILKIKTEEIAAFQRKRRSGSNGSVVSLE 908
Cdd:PTZ00121 1334 AKKKAEEAKKAAEAAKAEAEAAADEAE----AAEEKAEAAEKKKEEAKKkadAAKKKAEEKKKADEAKKKAEEDKKKADE 1409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 909 QQQIEEQKKWLDQEMEKVLQQRRA--LEELGEELRKREVilAKKEAlmQEKTGLESKRLRSSQALNEDIVRVSSRLEHLE 986
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKKAdeAKKKAEEAKKADE--AKKKA--EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA 1485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 987 KELSEKSGQLRQGS--AQNQQQIRGEIDTLRQEKDSLLKQRL-EIDSKLRQGSLLSPEEERTLFQLDEAIEALDA----A 1059
Cdd:PTZ00121 1486 DEAKKKAEEAKKKAdeAKKAAEAKKKADEAKKAEEAKKADEAkKAEEAKKADEAKKAEEKKKADELKKAEELKKAeekkK 1565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1060 IEYKNEAITCRQRVLRaSASLLSQCEMNLMAKLSYLSSSETRAllckyfdKVVTLREEQhQQQIAFSELEMQLEEQQRLv 1139
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKLYEEEKKM-------KAEEAKKAE-EAKIKAEELKKAEEEKKKV- 1635
|
570 580
....*....|....*....|....*...
gi 568947414 1140 ywleVALERQRLEMDRQLTLQQKEHEQN 1167
Cdd:PTZ00121 1636 ----EQLKKKEAEEKKKAEELKKAEEEN 1659
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
795-956 |
2.64e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 795 VAAAQSQVQVLKEK-KQATERLVSLSAQSETRLQELERnvqlmrrqqgqlqrrLREETEQ-KRRLETEMNKRQHRVKELE 872
Cdd:PRK00409 504 IEEAKKLIGEDKEKlNELIASLEELERELEQKAEEAEA---------------LLKEAEKlKEELEEKKEKLQEEEDKLL 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 873 LKHEQQ-QKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQIEEQKKWLDQEMEKV----LQQRRALEEL--GEELR---- 941
Cdd:PRK00409 569 EEAEKEaQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKekkkKKQKEKQEELkvGDEVKylsl 648
|
170
....*....|....*....
gi 568947414 942 --KREV--ILAKKEALMQE 956
Cdd:PRK00409 649 gqKGEVlsIPDDKEAIVQA 667
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
708-1055 |
2.96e-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: 45.55 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 708 LAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGR------EPQD 781
Cdd:pfam01576 168 LAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQlakkeeELQA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 782 A-----SERSRLQEFRKRVAAAQSQVQVLKE--------KKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLR 848
Cdd:pfam01576 248 AlarleEETAQKNNALKKIRELEAQISELQEdleseraaRNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQ 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 849 EETEQKRRLETEMNKRQHRVKELELKHEQQQKILkikTEEIAAFQRKRrsgsngsvVSLE--QQQIEEQKKWLDQEMeKV 926
Cdd:pfam01576 328 EVTELKKALEEETRSHEAQLQEMRQKHTQALEEL---TEQLEQAKRNK--------ANLEkaKQALESENAELQAEL-RT 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 927 LQQRRALEElgeelRKREvilaKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSE---KSGQLRQGSAQN 1003
Cdd:pfam01576 396 LQQAKQDSE-----HKRK----KLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEaegKNIKLSKDVSSL 466
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 568947414 1004 QQQIRGEIDTLRQEKdsllKQRLEIDSKLRQgsllsPEEERT--LFQLDEAIEA 1055
Cdd:pfam01576 467 ESQLQDTQELLQEET----RQKLNLSTRLRQ-----LEDERNslQEQLEEEEEA 511
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
740-1024 |
3.24e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 740 QALNRQHSQRIRELEQEAERVRAELCEGQRQL----RELEGREP-------QDASERSRLQEFRKRVAAAQSQVQVLKE- 807
Cdd:pfam10174 453 ERLKEQREREDRERLEELESLKKENKDLKEKVsalqPELTEKESslidlkeHASSLASSGLKKDSKLKSLEIAVEQKKEe 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 808 ---------KKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQ 878
Cdd:pfam10174 533 csklenqlkKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 879 QKILKIKTEEIAAFQRKRRSGSngsvvsleQQQIEEQKKWLDQEMEKVLQQRraLEELGEELRK-REVILAKKEAL---- 953
Cdd:pfam10174 613 MKEQNKKVANIKHGQQEMKKKG--------AQLLEEARRREDNLADNSQQLQ--LEELMGALEKtRQELDATKARLsstq 682
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568947414 954 --MQEKTG-LESKRLRSSQALNEdivRVSSRLEHLEKELSEKSGQ--LRQGSAQNQQQIRGEIDTLRQEKDSLLKQ 1024
Cdd:pfam10174 683 qsLAEKDGhLTNLRAERRKQLEE---ILEMKQEALLAAISEKDANiaLLELSSSKKKKTQEEVMALKREKDRLVHQ 755
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
849-1066 |
4.03e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 849 EETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKR--RSGSNGSVVSLeQQQIEE-----QKKWLDQ 921
Cdd:COG1340 54 ELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELaeLNKAGGSIDKL-RKEIERlewrqQTEVLSP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 922 EMEKVLQQRraLEELGEELRKREVILAKKEALMQEKTGLESKRLRSSQaLNEDIvrvssrlehleKELSEKSGQLRqgsa 1001
Cdd:COG1340 133 EEEKELVEK--IKELEKELEKAKKALEKNEKLKELRAELKELRKEAEE-IHKKI-----------KELAEEAQELH---- 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568947414 1002 QNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQgslLSPEEERTLFQLDEAIEALDAAIEYKNEA 1066
Cdd:COG1340 195 EEMIELYKEADELRKEADELHKEIVEAQEKADE---LHEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
707-1240 |
6.29e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 707 RLAQAQQKIRELAINIRMKEELIGELVRTgkaaqalnrqhsqrIRELEQEAERVRAELC----EGQRQLRELEGREPQDA 782
Cdd:pfam10174 220 QLQPDPAKTKALQTVIEMKDTKISSLERN--------------IRDLEDEVQMLKTNGLlhteDREEEIKQMEVYKSHSK 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 783 SERSRLQEFRKRVAAAQSQVQVLKEKkqaterLVSLSAQSETRLQELErnvqlmrrqqgqlqrRLREETEQKrrlETEMN 862
Cdd:pfam10174 286 FMKNKIDQLKQELSKKESELLALQTK------LETLTNQNSDCKQHIE---------------VLKESLTAK---EQRAA 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 863 KRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRrsgsngsvvSLEQQQIEEQKKWLDQEMEKVLQQRRALEELGEELRK 942
Cdd:pfam10174 342 ILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEK---------STLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRD 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 943 REVILA-KKEALmqektgleskrlrssQALNEDIVRVSSRLEHLEKELSEKSG---QLRQGSAQNQQQIRGEIDTLRQE- 1017
Cdd:pfam10174 413 KDKQLAgLKERV---------------KSLQTDSSNTDTALTTLEEALSEKERiieRLKEQREREDRERLEELESLKKEn 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1018 KDslLKQRLEI--DSKLRQGSLLSPEEERT------LFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMN-- 1087
Cdd:pfam10174 478 KD--LKEKVSAlqPELTEKESSLIDLKEHAsslassGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNpe 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1088 LMAKLSYLSSSETRallckYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQL----TLQQKE 1163
Cdd:pfam10174 556 INDRIRLLEQEVAR-----YKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVanikHGQQEM 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1164 HEQNVQLLLQQGRDHLGEGLADSKRQYEARIHALEKelgrhmwINQEL---KQKLSAGSTAGQSRGCERRSLCLENRQCL 1240
Cdd:pfam10174 631 KKKGAQLLEEARRREDNLADNSQQLQLEELMGALEK-------TRQELdatKARLSSTQQSLAEKDGHLTNLRAERRKQL 703
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
948-1201 |
6.41e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 948 AKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELseksgqlrQGSAQNQQQIRGEIDTLRQEKDSLLKQRLE 1027
Cdd:PRK11281 48 LNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQL--------AQAPAKLRQAQAELEALKDDNDEETRETLS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1028 IDSkLRQgslLSPEEERTLFQLDEAIEALDaaiEYKNEAITCRQRVLRASASllsqcemnlmaklsyLSSSETRAllcky 1107
Cdd:PRK11281 120 TLS-LRQ---LESRLAQTLDQLQNAQNDLA---EYNSQLVSLQTQPERAQAA---------------LYANSQRL----- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1108 fdkvvtlreeqhqQQIAfSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNVQL--LLQQGRDHLgeglad 1185
Cdd:PRK11281 173 -------------QQIR-NLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLqdLLQKQRDYL------ 232
|
250
....*....|....*.
gi 568947414 1186 skrqyEARIHALEKEL 1201
Cdd:PRK11281 233 -----TARIQRLEHQL 243
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
850-991 |
6.79e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 850 ETEQKRRLETEMNKRQHRVKELELkhEQQQKILKIKTEEIAAFQRKRRSgsngsVVSLEQ--QQIEEQkkwLDQEMEKVL 927
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEALL--EAKEEIHKLRNEFEKELRERRNE-----LQKLEKrlLQKEEN---LDRKLELLE 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568947414 928 QQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLRSSQALNEDIVRvSSRLEHLEKELSE 991
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAK-EILLEKVEEEARH 169
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
732-1181 |
1.09e-03 |
|
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: 43.42 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 732 LVRTGKAAQALNRQHSQRIRELEQ--EAERVRAELCEGQRQLRELEGrEPQDASERSRLQEFrkrvaAAQSQVQVLKEKK 809
Cdd:TIGR00618 148 LLPQGEFAQFLKAKSKEKKELLMNlfPLDQYTQLALMEFAKKKSLHG-KAELLTLRSQLLTL-----CTPCMPDTYHERK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 810 QATERLVslsAQSETRLQELERNvqlmrrqqGQLQRRLREETEQKRRLETEMNKRQHRVKELElkheqqqkilkikTEEi 889
Cdd:TIGR00618 222 QVLEKEL---KHLREALQQTQQS--------HAYLTQKREAQEEQLKKQQLLKQLRARIEELR-------------AQE- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 890 aafqrkrrsgsngSVVSLEQQQIEEQKKWL-----DQEMEKVLQQR-RALEELGEELRKREVILAKKEALMQEKTGLESK 963
Cdd:TIGR00618 277 -------------AVLEETQERINRARKAAplaahIKAVTQIEQQAqRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 964 RLRSSQALN-EDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEE 1042
Cdd:TIGR00618 344 RRLLQTLHSqEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQ 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1043 ERtLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQHQ-Q 1121
Cdd:TIGR00618 424 GQ-LAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQeE 502
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1122 QIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKehEQNVQLLLQQGRDHLGE 1181
Cdd:TIGR00618 503 PCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETS--EEDVYHQLTSERKQRAS 560
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
754-1165 |
1.11e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 754 EQEAERVRAELCEGQRQLRELEGREPQDASERSRLQEfrkrvaAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNV 833
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQE------QLQAETELCAEAEEMRARLAARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 834 QlmrrqqgqlqrrlrEETEQKRRLETEMNKRQHRVKELELKHEqqqkilkiktEEIAAFQRKRRSGsngsvVSLEQ--QQ 911
Cdd:pfam01576 85 E--------------EEEERSQQLQNEKKKMQQHIQDLEEQLD----------EEEAARQKLQLEK-----VTTEAkiKK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 912 IEEQKKWLDQEMEKVLQQRRALEE--------LGEELRKR-----------------EVILAKKEALMQEKTGLESKRLR 966
Cdd:pfam01576 136 LEEDILLLEDQNSKLSKERKLLEEriseftsnLAEEEEKAkslsklknkheamisdlEERLKKEEKGRQELEKAKRKLEG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 967 SSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDsLLKQRLEIDSKLRQGSLLSPEEERTL 1046
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE-LEAQISELQEDLESERAARNKAEKQR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1047 FQLDEAIEALDAAIEYKNEAiTCRQRVLRasasllSQCEMNLmAKLSYLSSSETRAllckyFDKVVTLREEQHQQqiAFS 1126
Cdd:pfam01576 295 RDLGEELEALKTELEDTLDT-TAAQQELR------SKREQEV-TELKKALEEETRS-----HEAQLQEMRQKHTQ--ALE 359
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 568947414 1127 ELEMQLEEQQRLVYWLE---VALERQRLEMDRQL-TLQQKEHE 1165
Cdd:pfam01576 360 ELTEQLEQAKRNKANLEkakQALESENAELQAELrTLQQAKQD 402
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
748-943 |
1.12e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 748 QRIRELEQEAERVRAELCEGQRQLRELEGREpqdASERSRLQEFRKRVAAAQSQVQVLKEK-KQATERLVSLSAQSEtrL 826
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARL---EAAKTELEDLEKEIKRLELEIEEVEARiKKYEEQLGNVRNNKE--Y 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 827 QELERnvqlmrrqqgqlqrrlrEETEQKRRLEtemnKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsvvs 906
Cdd:COG1579 92 EALQK-----------------EIESLKRRIS----DLEDEILELMERIEELEEELAELEAELAELEAELEE-------- 142
|
170 180 190
....*....|....*....|....*....|....*...
gi 568947414 907 lEQQQIEEQKKWLDQEMEKVLQQRRALEE-LGEELRKR 943
Cdd:COG1579 143 -KKAELDEELAELEAELEELEAEREELAAkIPPELLAL 179
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
707-1205 |
1.12e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 707 RLAQAQQKIRELAINIRMKEELIgELVRTGKAAQALNRQHsQRIRELEQEAERVRAELCEGQRQLRELEGREpqDASERS 786
Cdd:COG4913 256 PIRELAERYAAARERLAELEYLR-AALRLWFAQRRLELLE-AELEELRAELARLEAELERLEARLDALREEL--DELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 787 RLQEFRKRVAAAQSQVQVLKEKKQATERLvslSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQH 866
Cdd:COG4913 332 IRGNGGDRLEQLEREIERLERELEERERR---RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 867 rvkELELKHEQQQKILKIKTEEIAAFQRkrrsgsNGSVVSLEQQQI-------------------------EEQKKWLDQ 921
Cdd:COG4913 409 ---EAEAALRDLRRELRELEAEIASLER------RKSNIPARLLALrdalaealgldeaelpfvgelievrPEEERWRGA 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 922 eMEKVL---------------QQRRALEE--LGEELRKREVILAKKEALMQ--------EKtgLESKR------LRSSQA 970
Cdd:COG4913 480 -IERVLggfaltllvppehyaAALRWVNRlhLRGRLVYERVRTGLPDPERPrldpdslaGK--LDFKPhpfrawLEAELG 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 971 LNEDIVRVSS--RLEHLEKELSeKSGQLRQGSAqnqqqiRGEIDTLRQEKDSLL-----KQRLEIDSKLRQgsllspEEE 1043
Cdd:COG4913 557 RRFDYVCVDSpeELRRHPRAIT-RAGQVKGNGT------RHEKDDRRRIRSRYVlgfdnRAKLAALEAELA------ELE 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1044 RTLFQLDEAIEALDAAIEYKNEAITCRQRVLRAS------ASLLSQCEmNLMAKLSYLSSSEtrallckyfDKVVTLREE 1117
Cdd:COG4913 624 EELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIA-ELEAELERLDASS---------DDLAALEEQ 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1118 QHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDR-QLTLQQKEHEQNV-----------QLLLQQGRDHLGEGLAD 1185
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElQDRLEAAEDLARLelralleerfaAALGDAVERELRENLEE 773
|
570 580
....*....|....*....|
gi 568947414 1186 SKRQYEARIHALEKELGRHM 1205
Cdd:COG4913 774 RIDALRARLNRAEEELERAM 793
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
705-991 |
1.24e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 705 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALnRQHSQRIREL---EQEAERVRAELCEGQRQLRELEgrepqd 781
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYswdEIDVASAEREIAELEAELERLD------ 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 782 aSERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEM 861
Cdd:COG4913 682 -ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 862 NKRQHRVKElELKHEQQQKILKIKTEE------IAAFQRKRRSGSNGSVVSLEqqQIEEQKKWLDQemekvlQQRRALEE 935
Cdd:COG4913 761 DAVERELRE-NLEERIDALRARLNRAEeeleraMRAFNREWPAETADLDADLE--SLPEYLALLDR------LEEDGLPE 831
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 568947414 936 LGEELRKrevilAKKEALMQEKTGLeskrlrsSQALNEDIVRVSSRLEHLEKELSE 991
Cdd:COG4913 832 YEERFKE-----LLNENSIEFVADL-------LSKLRRAIREIKERIDPLNDSLKR 875
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
749-1199 |
1.28e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 749 RIRELEQEAERVRAELCEGQRQLRELEGREPQDASERSRLQ-----------EFRKRVAAAQSQVQVL-KEKKQATERLV 816
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQlekvtteakikKLEEDILLLEDQNSKLsKERKLLEERIS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 817 SLS---AQSETRLQELE--RNVQLMRRQQGQLQRRLREETEQ-----KRRLETEMNKRQHRVKELELKHEQQQKILKIKT 886
Cdd:pfam01576 163 EFTsnlAEEEEKAKSLSklKNKHEAMISDLEERLKKEEKGRQelekaKRKLEGESTDLQEQIAELQAQIAELRAQLAKKE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 887 EEIAAFQRK------RRSGSNGSVVSLeQQQIEEQKKWLDQE---MEKVLQQRRALEELGEELR---------------- 941
Cdd:pfam01576 243 EELQAALARleeetaQKNNALKKIREL-EAQISELQEDLESEraaRNKAEKQRRDLGEELEALKteledtldttaaqqel 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 942 --KREVILAK-KEALMQEKTGLESK----RLRSSQALNEdivrVSSRLEHLE--KELSEKSgqlRQGSAQNQQQIRGEID 1012
Cdd:pfam01576 322 rsKREQEVTElKKALEEETRSHEAQlqemRQKHTQALEE----LTEQLEQAKrnKANLEKA---KQALESENAELQAELR 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1013 TLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNLMAKL 1092
Cdd:pfam01576 395 TLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1093 SYLsSSETRALLcKYFDKVVTLREEQhqqqiafSELEMQLEEQQRlvywLEVALERQRLEMDRQLTLQQKEHEQNVQLL- 1171
Cdd:pfam01576 475 ELL-QEETRQKL-NLSTRLRQLEDER-------NSLQEQLEEEEE----AKRNVERQLSTLQAQLSDMKKKLEEDAGTLe 541
|
490 500
....*....|....*....|....*....
gi 568947414 1172 -LQQGRDHLGEGLADSKRQYEARIHALEK 1199
Cdd:pfam01576 542 aLEEGKKRLQRELEALTQQLEEKAAAYDK 570
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
797-1201 |
1.57e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.79 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 797 AAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVkelelkhe 876
Cdd:pfam05483 322 ATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL-------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 877 qqqkilkiktEEIAAFQRKRrsgsngsvvsleQQQIEEQKKWLdQEMEKVLQQRRALEELGEELRKREvilakkealmQE 956
Cdd:pfam05483 394 ----------EEMTKFKNNK------------EVELEELKKIL-AEDEKLLDEKKQFEKIAEELKGKE----------QE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 957 KTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLrqgsaqnqqqirgeidtlrqEKDSLlkQRLEIDSKLRQGS 1036
Cdd:pfam05483 441 LIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL--------------------EKEKL--KNIELTAHCDKLL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1037 LlspeEERTLFQldeaiEALDAAIEYKNEA---ITCRQRVLRASASL--LSQCEMNLMAKLSYlsssetrallckyfdkv 1111
Cdd:pfam05483 499 L----ENKELTQ-----EASDMTLELKKHQediINCKKQEERMLKQIenLEEKEMNLRDELES----------------- 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1112 vtLREEQHQQQiafSELEMQL---EEQQRLVYWLEVALERQRLEMDRQ---LTLQQKEHEQNVQLLLQQGRDHLGEGLAD 1185
Cdd:pfam05483 553 --VREEFIQKG---DEVKCKLdksEENARSIEYEVLKKEKQMKILENKcnnLKKQIENKNKNIEELHQENKALKKKGSAE 627
|
410
....*....|....*...
gi 568947414 1186 SKR--QYEARIHALEKEL 1201
Cdd:pfam05483 628 NKQlnAYEIKVNKLELEL 645
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
700-1016 |
1.60e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 700 AAMASEWRLAQAQQKIRELaiNIRMKEELIgelVRTGKAAQALNRQhsQRIRELEQEAERVRAELCEGQRQLRELEGREP 779
Cdd:PRK04863 342 TALRQQEKIERYQADLEEL--EERLEEQNE---VVEEADEQQEENE--ARAEAAEEEVDELKSQLADYQQALDVQQTRAI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 780 QDASERSRLQEFR----------KRVAAAQSQVQVlkEKKQATERLVSLSAQ---SETRLQELERNVQLMR--------R 838
Cdd:PRK04863 415 QYQQAVQALERAKqlcglpdltaDNAEDWLEEFQA--KEQEATEELLSLEQKlsvAQAAHSQFEQAYQLVRkiagevsrS 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 839 QQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEeiaAFQRKRRSGSNGSVVSLEQQQIEEQKKW 918
Cdd:PRK04863 493 EAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAE---FCKRLGKNLDDEDELEQLQEELEARLES 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 919 LDQEMEKVLQQRRALEELGEELRKREVILAKKE----------ALMQEKTGLEskrLRSSQALNEDIVRVssrLEHlEKE 988
Cdd:PRK04863 570 LSESVSEARERRMALRQQLEQLQARIQRLAARApawlaaqdalARLREQSGEE---FEDSQDVTEYMQQL---LER-ERE 642
|
330 340
....*....|....*....|....*...
gi 568947414 989 LSeksgQLRQGSAQNQQQIRGEIDTLRQ 1016
Cdd:PRK04863 643 LT----VERDELAARKQALDEEIERLSQ 666
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
707-935 |
1.64e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 707 RLAQAQQKIRELAINI-RMKEELigelvrTGKAAQALNrqhSQRIRELEQEAERVRAELCEGQRQLRELEGR--EPQDAS 783
Cdd:PRK11281 88 QLAQAPAKLRQAQAELeALKDDN------DEETRETLS---TLSLRQLESRLAQTLDQLQNAQNDLAEYNSQlvSLQTQP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 784 ERS---------RLQEFRKRVAAAQ-SQVQVLKEKKQATE-RLVSLSAQSETRLQELERNVQLmrrqQGQLQRRLREETE 852
Cdd:PRK11281 159 ERAqaalyansqRLQQIRNLLKGGKvGGKALRPSQRVLLQaEQALLNAQNDLQRKSLEGNTQL----QDLLQKQRDYLTA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 853 QKRRLETEM--------NKR----QHRVKELelkhEQQQKILKIKT-----EEIAA----FQRKRRSGSNGSvvSLEQQQ 911
Cdd:PRK11281 235 RIQRLEHQLqllqeainSKRltlsEKTVQEA----QSQDEAARIQAnplvaQELEInlqlSQRLLKATEKLN--TLTQQN 308
|
250 260
....*....|....*....|....
gi 568947414 912 IeEQKKWLDqemeKVLQQRRALEE 935
Cdd:PRK11281 309 L-RVKNWLD----RLTQSERNIKE 327
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
693-1134 |
1.99e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 693 VQTRQAPAAMASEWRlaQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAEL----CEGQ 768
Cdd:PRK02224 233 RETRDEADEVLEEHE--ERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAglddADAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 769 RQLRELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKEKkqaTERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLR 848
Cdd:PRK02224 311 AVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRED---ADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 849 EETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNgsVVSLEQQQIEEQK------------ 916
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARE--RVEEAEALLEAGKcpecgqpvegsp 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 917 --KWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLRSSqalnedivRVSSRLEHLEKELSEKSG 994
Cdd:PRK02224 466 hvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERRE--------DLEELIAERRETIEEKRE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 995 QLRQGSAQNQqqirgEIDTLRQEK-DSLLKQRLEIDSKLRQGSLLspeeERTLFQLDEAIEALDAAIEYKNEAITCRQRV 1073
Cdd:PRK02224 538 RAEELRERAA-----ELEAEAEEKrEAAAEAEEEAEEAREEVAEL----NSKLAELKERIESLERIRTLLAAIADAEDEI 608
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568947414 1074 LRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFD--KVVTLREEQHQQQIAFSELEMQLEE 1134
Cdd:PRK02224 609 ERLREKREALAELNDERRERLAEKRERKRELEAEFDeaRIEEAREDKERAEEYLEQVEEKLDE 671
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
862-1054 |
2.46e-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: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 862 NKRQHRVKELELKHEQQQKILKIKTEEIAAFQR------KRRSGSNGSVVSLEqQQIEEQKKWLDQEMEKVLQQRRALEE 935
Cdd:TIGR04523 29 NKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKnlnkdeEKINNSNNKIKILE-QQIKDLNDKLKKNKDKINKLNSDLSK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 936 LGEELR-KREVILAKKEalmqektglESKRL-RSSQALNEDIVRVSSRLEHLEKELSEKSGQLRqgsaqnqqQIRGEIDT 1013
Cdd:TIGR04523 108 INSEIKnDKEQKNKLEV---------ELNKLeKQKKENKKNIDKFLTEIKKKEKELEKLNNKYN--------DLKKQKEE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568947414 1014 LRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIE 1054
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQ 211
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
789-1080 |
2.58e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.52 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 789 QEFRKRVAAAQSQVQVLKEK-KQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHR 867
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKqAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 868 VKELELKHEQQQKILKIKteeiaafqrkrrsgsngsvvslEQQQIEEQKKWLDQEMEKVLQQRRALEEL--GEELRKREV 945
Cdd:pfam12128 680 ANERLNSLEAQLKQLDKK----------------------HQAWLEEQKEQKREARTEKQAYWQVVEGAldAQLALLKAA 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 946 ILAKKEALMQEKTGLESKRLRSSQALNEDIVRVsSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQR 1025
Cdd:pfam12128 738 IAARRSGAKAELKALETWYKRDLASLGVDPDVI-AKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQL 816
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 568947414 1026 LEIDSKLR--QGSL--LSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASL 1080
Cdd:pfam12128 817 SNIERAISelQQQLarLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATL 875
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
705-940 |
2.69e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 705 EWRLAQAQQKIRELAINIRMKEELIGELVRT--GKAAQALNRQHsqriRELEQEAERVRAElcegQRQLRELEGREPQDA 782
Cdd:COG3096 461 EQKLSVADAARRQFEKAYELVCKIAGEVERSqaWQTARELLRRY----RSQQALAQRLQQL----RAQLAELEQRLRQQQ 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 783 SERSRLQEFRKRvaaaqsqvqvLKEKKQATERLVSLSAQSETRLQELErnvqlmrrqqgqlqRRLREETEQKRRLETEMN 862
Cdd:COG3096 533 NAERLLEEFCQR----------IGQQLDAAEELEELLAELEAQLEELE--------------EQAAEAVEQRSELRQQLE 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 863 KRQHRVKELELK----HEQQQKILKIKTEEIAAFQrkrrsgsNGSVVSLEQQQIEEQKKWLDQEMEKVLQQRRALEELGE 938
Cdd:COG3096 589 QLRARIKELAARapawLAAQDALERLREQSGEALA-------DSQEVTAAMQQLLEREREATVERDELAARKQALESQIE 661
|
..
gi 568947414 939 EL 940
Cdd:COG3096 662 RL 663
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
687-1201 |
3.03e-03 |
|
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227569 [Multi-domain] Cd Length: 669 Bit Score: 41.98 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 687 GSGKVPVQTRQAPAAMAsewrlaqaQQKIRELAINI----RMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRA 762
Cdd:COG5244 94 KDGEIKQENHEDRIHFE--------ESKIRRLEETIealkSTEKEEIVELRRENEELDKINLSLRERISSEEPELNKDGS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 763 ELCEGQ-RQLRELEGREPQDASER-SRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQ 840
Cdd:COG5244 166 KLSYDElKEFVEESRVQVYDMVELvSDISETLNRNGSIQRSSVRECERSNIHDVLFLVNGILDGVIDELNGELERLRRQL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 841 GQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTeeiaaFQRKRRsgsngsvvSLEQQQIEEQKKWLD 920
Cdd:COG5244 246 VSLMSSHGIEVEENSRLKATLEKFQSLELKVNTLQEELYQNKLLKK-----FYQIYE--------PFAQAALSSQLQYLA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 921 QEMEKVLqqrRALEELGEELRKREVILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRL-EHLEKELSEKsgqlrqg 999
Cdd:COG5244 313 EVIESEN---FGKLENIEIHIILKVLSSISYALHIYTIKNTPDHLETTLQCFVNIAPISMWLsEFLQRKFSSK------- 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1000 saqnQQQIRGEIDTLRQEKDS-----LLKQRLEIDSKLRQGSLLSPEE---ERTLFQLDEAIEAldAAIEYKNEAITCRQ 1071
Cdd:COG5244 383 ----QETAFSICQFLEDNKDVtlilkILHPILETTVPKLLAFLRTNSNfndNDTLCLIGSLYEI--ARIDKLIGKEEISK 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 1072 RVLRasASLLSQCEMNLMAKLSYLSSSETRALL--CKYFDKVVTLREEQHQQQIAFSElemQLEEqqrlvywlEVALERQ 1149
Cdd:COG5244 457 QDNR--LFLYPSCDITLSSILTILFSDKLEVFFqgIESLLENITIFPEQPSQQTSDSE---NIKE--------NSLLSDR 523
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 568947414 1150 RLEMDRQL--TLQQKEHEQNVQLLLQ--QGRDHLgegladsKRQYEARIHALEKEL 1201
Cdd:COG5244 524 LNEENIRLkeVLVQKENMLTEETKIKiiIGRDLE-------RKTLEENIKTLKVEL 572
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
768-1008 |
3.31e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 768 QRQLRELEGREPQDASE--RSRLQEFRKRVAAAQSQVQVLKEKKQaterLVSLSAQSETRLQELER-NVQLmrrqqGQLQ 844
Cdd:COG3206 162 LEQNLELRREEARKALEflEEQLPELRKELEEAEAALEEFRQKNG----LVDLSEEAKLLLQQLSElESQL-----AEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 845 RRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQIEEQKKWLDQEME 924
Cdd:COG3206 233 AELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 925 KVLQQRRAleelgeelrKREVILAKKEALMQEKTGLESKRLRSSQALNE--DIVRVSSRLEHLEKELSEKSGQLRQGSAQ 1002
Cdd:COG3206 313 RILASLEA---------ELEALQAREASLQAQLAQLEARLAELPELEAElrRLEREVEVARELYESLLQRLEEARLAEAL 383
|
....*.
gi 568947414 1003 NQQQIR 1008
Cdd:COG3206 384 TVGNVR 389
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
709-907 |
3.43e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 709 AQAQQKIRELAINIrmkEELIGELvrtgkaaQALNRQHSQRIRELE---QEAERVRAELcegQRQLRELEGREpqdASER 785
Cdd:PRK00409 505 EEAKKLIGEDKEKL---NELIASL-------EELERELEQKAEEAEallKEAEKLKEEL---EEKKEKLQEEE---DKLL 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 786 SRL-QEFRKRVAAAqsqvqvlkekKQATERLVSlsaqsetRLQELERnvqlmrrqqgqlqrrlREETEQKRRLETEMNKR 864
Cdd:PRK00409 569 EEAeKEAQQAIKEA----------KKEADEIIK-------ELRQLQK----------------GGYASVKAHELIEARKR 615
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568947414 865 qhrvkeLELKHEQQQKILKIKTEEIAAFQ-----RKRRSGSNGSVVSL 907
Cdd:PRK00409 616 ------LNKANEKKEKKKKKQKEKQEELKvgdevKYLSLGQKGEVLSI 657
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
744-1027 |
4.02e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 41.20 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 744 RQHSQRIRELEQEAERVRAELCEGQRQLRELE---GREPQDASERSRLQE----FRKRVAAAQSQVQVLKEK-KQAteRL 815
Cdd:pfam15742 65 KQAQQKLLDSTKMCSSLTAEWKHCQQKIRELElevLKQAQSIKSQNSLQEklaqEKSRVADAEEKILELQQKlEHA--HK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 816 VSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMN---------------------KRQHRVKELELK 874
Cdd:pfam15742 143 VCLTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNelqqqvrslqdkeaqlemtnsQQQLRIQQQEAQ 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 875 HEQQQKILKIKTEEIAAfqrkrrsgsngsvvsleQQQIEEQKKWLDQEMEKVLQQ-RRALEELGEELRKRevilakKEAL 953
Cdd:pfam15742 223 LKQLENEKRKSDEHLKS-----------------NQELSEKLSSLQQEKEALQEElQQVLKQLDVHVRKY------NEKH 279
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568947414 954 MQEKTGLEskrlRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQnQQQIRGEIDTLRQEKDSLLKQRLE 1027
Cdd:pfam15742 280 HHHKAKLR----RAKDRLVHEVEQRDERIKQLENEIGILQQQSEKEKAF-QKQVTAQNEILLLEKRKLLEQLTE 348
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
719-1044 |
4.07e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 719 AINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQdasERSRLQEFRKRVAAA 798
Cdd:COG4372 23 GILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE---LNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 799 QSQVQVLKEKKQATERLVslsAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELElkHEQQ 878
Cdd:COG4372 100 QEELESLQEEAEELQEEL---EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALE--QELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 879 QKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQIEEQkkwldQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKT 958
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIES-----LPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 959 GLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLL 1038
Cdd:COG4372 250 ELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLE 329
|
....*.
gi 568947414 1039 SPEEER 1044
Cdd:COG4372 330 LALAIL 335
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
709-957 |
4.49e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 709 AQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERSRL 788
Cdd:pfam17380 400 AARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 789 QEFRKRVAAAQSQVQVLKEKkqaterlvslsaqsetrlqELERNVQLMrrqqgqlqrrlREETEQKRRLETEMNKRQHRV 868
Cdd:pfam17380 480 EKEKRDRKRAEEQRRKILEK-------------------ELEERKQAM-----------IEEERKRKLLEKEMEERQKAI 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 869 KElelkhEQQQKILkikteeiaafQRKRRSgsngsvvsleQQQIEEQKKwLDQEMEKVLQQRRALEELGeelRKREVILA 948
Cdd:pfam17380 530 YE-----EERRREA----------EEERRK----------QQEMEERRR-IQEQMRKATEERSRLEAME---REREMMRQ 580
|
....*....
gi 568947414 949 KKEALMQEK 957
Cdd:pfam17380 581 IVESEKARA 589
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
787-1061 |
5.19e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 787 RLQEFRKRVAAAQSQVQVLKEKKQatERLVSLSAQSEtrlqelernvqlmrrqqgqlqrrLREETEQKRRL---ETEMNK 863
Cdd:PRK02224 163 KLEEYRERASDARLGVERVLSDQR--GSLDQLKAQIE-----------------------EKEEKDLHERLnglESELAE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 864 RQHRVKELELKHEQQQKILKIKTEEIAAFQRKRrsgsngsvvsleqQQIEEQKKWLDQEMEKVLQQRRALEELGEELR-K 942
Cdd:PRK02224 218 LDEEIERYEEQREQARETRDEADEVLEEHEERR-------------EELETLEAEIEDLRETIAETEREREELAEEVRdL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 943 REVILAKKEAL--MQEKTGLESKrlrSSQALNEDIVRVSSRLEHLEKELSEKSgqLRQGSAQNQ-QQIRGEIDTLRQEKD 1019
Cdd:PRK02224 285 RERLEELEEERddLLAEAGLDDA---DAEAVEARREELEDRDEELRDRLEECR--VAAQAHNEEaESLREDADDLEERAE 359
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568947414 1020 SLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIE 1061
Cdd:PRK02224 360 ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
709-1028 |
6.62e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.65 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 709 AQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEG--REPQDASErS 786
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEkyKELSASSE-E 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 787 RLQEFRKRVAAAQSQVQVLKEKKqatERLVSLSAQSETRLQELERnvqlMRRQQGQLQRRLREETEQKRRLETEMnkrQH 866
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELE---EDIKTLTQRVLERETELER----MKERAKKAGAQRKEEEAERKQLQAKL---QQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 867 RVKELELKHEQQQKILKIKTEEIAAFQRKRRsgsngSVVSLEQQQIEEQKKWLdqEMEKVLQQRRALEELGEELRKrevi 946
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAQRDTQVLQLQD-----TITTLTQKLTTAHRKEA--ENEALLEELRSLQERLNASER---- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 947 laKKEALMQEKTGLESKRLRSSQALNEdivrvsSRLE--HLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQ 1024
Cdd:pfam07888 252 --KVEGLGEELSSMAAQRDRTQAELHQ------ARLQaaQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKL 323
|
....
gi 568947414 1025 RLEI 1028
Cdd:pfam07888 324 SAEL 327
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
705-967 |
7.92e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 705 EWRLAQAQQKIRELAINIRMKEEL------IGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEgqrqlRELEGRE 778
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAEDLveaedrIERLEERREDLEELIAERRETIEEKRERAEELRERAAE-----LEAEAEE 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 779 PQDASE--RSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERnvqlmrrQQGQLQRRLREETEQKRR 856
Cdd:PRK02224 556 KREAAAeaEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIER-------LREKREALAELNDERRER 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 857 LETemnkRQHRVKELELKHEQQqkilkiKTEEiaAFQRKRRSGSNGSVVSLEQQQIEEQKKWLDQEMEKVLQQRRALEEL 936
Cdd:PRK02224 629 LAE----KRERKRELEAEFDEA------RIEE--AREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL 696
|
250 260 270
....*....|....*....|....*....|...
gi 568947414 937 GEELRKREVILAKKEALMQEKTGLES--KRLRS 967
Cdd:PRK02224 697 RERREALENRVEALEALYDEAEELESmyGDLRA 729
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
909-1080 |
8.11e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 40.51 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 909 QQQIEEQKKWLDQEMEKVL-QQRRALEELGEELRKR-EVILAKKEALMQEKTGLESKRLRSS--QALNEDIVRVSSRL-E 983
Cdd:pfam09731 300 SKKLAELKKREEKHIERALeKQKEELDKLAEELSARlEEVRAADEAQLRLEFEREREEIRESyeEKLRTELERQAEAHeE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 984 HLEKELSEKSGQLrqgsaqNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQ-----GSLLSPEEE-RTLFQLDEAIEALD 1057
Cdd:pfam09731 380 HLKDVLVEQEIEL------QREFLQDIKEKVEEERAGRLLKLNELLANLKGlekatSSHSEVEDEnRKAQQLWLAVEALR 453
|
170 180
....*....|....*....|....*
gi 568947414 1058 AAIEYKNEAITCR--QRVLRASASL 1080
Cdd:pfam09731 454 STLEDGSADSRPRplVRELKALKEL 478
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
700-1052 |
8.32e-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: 40.71 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 700 AAMASEWRLAQAQQKIRELAINIRMKEELIGELvrtgKAAQALNRQHSQRIrelEQEAERVRAELCEGQRQLRELEGREP 779
Cdd:COG3096 341 TALRQQEKIERYQEDLEELTERLEEQEEVVEEA----AEQLAEAEARLEAA---EEEVDSLKSQLADYQQALDVQQTRAI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 780 QDASERSRLQEFRKR-------VAAAQSQVQVLKEK-KQATERLVSLsaqsETRL-------QELERNVQLMRRQQGQLQ 844
Cdd:COG3096 414 QYQQAVQALEKARALcglpdltPENAEDYLAAFRAKeQQATEEVLEL----EQKLsvadaarRQFEKAYELVCKIAGEVE 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 845 RRLREET---------EQKRRLETEMNKRQHrVKELELKHEQQQKILKIKTEEIaafQRKRRSGSNGSVVSLEQQQIEEQ 915
Cdd:COG3096 490 RSQAWQTarellrryrSQQALAQRLQQLRAQ-LAELEQRLRQQQNAERLLEEFC---QRIGQQLDAAEELEELLAELEAQ 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 916 KKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEAlmqektgleskRLRSSQAlnedivrvssRLEHLEKELSEKSGQ 995
Cdd:COG3096 566 LEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAP-----------AWLAAQD----------ALERLREQSGEALAD 624
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 568947414 996 LRQGSAQNQQQIRGEIDtLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEA 1052
Cdd:COG3096 625 SQEVTAAMQQLLERERE-ATVERDELAARKQALESQIERLSQPGGAEDPRLLALAER 680
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
699-818 |
9.67e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947414 699 PAAMASEWRLAQAQQKIRELAINIRMKEELIGELvrtgkaaQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGRE 778
Cdd:COG2433 399 REKEHEERELTEEEEEIRRLEEQVERLEAEVEEL-------EAELEEKDERIERLERELSEARSEERREIRKDREISRLD 471
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 568947414 779 PQDASERSRLQEFRKRVAAAQSQVQVLKE--KKQATERLVSL 818
Cdd:COG2433 472 REIERLERELEEERERIEELKRKLERLKElwKLEHSGELVPV 513
|
|
| |
