|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
15-350 |
6.22e-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: 6.22e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 15 PVRVALRVRPLLPKELLHGHQSCLRVEPERGRITLGRDRHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNATVFAYG 94
Cdd:cd01372 2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 95 QTGSGKTYTMGEASVASLHEDEQGIIPRAMAEAFKLIDE-NDLLDCLVHVSYLELYKEEFRDLLEVGTASR-DIQLREDD 172
Cdd:cd01372 82 QTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKkKDTFEFQLKVSFLEIYNEEIRDLLDPETDKKpTISIREDS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 173 RGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSRLPRPAAGHL--LVSKFHF 250
Cdd:cd01372 162 KGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSADDKNstFTSKFHF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 251 VDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRGSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSS 330
Cdd:cd01372 242 VDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPAD 321
|
330 340
....*....|....*....|
gi 568947408 331 SDFDETLNTLNYASRAQNIR 350
Cdd:cd01372 322 SNFEETLNTLKYANRARNIK 341
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
15-356 |
3.16e-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: 3.16e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 15 PVRVALRVRPLLPKELLHGHQSCLRVEPERGRIT-------LGRDRHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFN 87
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLtvrspknRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 88 ATVFAYGQTGSGKTYTMGEasvaslHEDEQGIIPRAMAEAFKLIDEN-DLLDCLVHVSYLELYKEEFRDLLevGTASRDI 166
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKReEGWQFSVKVSYLEIYNEKIRDLL--NPSSKKL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 167 QLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSRlprpaaGHLLVS 246
Cdd:smart00129 153 EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSS------GSGKAS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRgSHIPYRDSKITRILKDSLGGNAKTVMIACV 326
Cdd:smart00129 227 KLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHIPYRDSKLTRLLQDSLGGNSKTLMIANV 305
|
330 340 350
....*....|....*....|....*....|
gi 568947408 327 SPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:smart00129 306 SPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
21-349 |
7.94e-134 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 413.51 E-value: 7.94e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 21 RVRPLLPKELLHGHQSCLRVEPERGRITL-------GRDRHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNATVFAY 93
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 94 GQTGSGKTYTMGEAsvaslhEDEQGIIPRAMAEAFKLIDEN-DLLDCLVHVSYLELYKEEFRDLLEVGTAS-RDIQLRED 171
Cdd:pfam00225 81 GQTGSGKTYTMEGS------DEQPGIIPRALEDLFDRIQKTkERSEFSVKVSYLEIYNEKIRDLLSPSNKNkRKLRIRED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 172 DRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSRLPrpaagHLLVSKFHFV 251
Cdd:pfam00225 155 PKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEE-----SVKTGKLNLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 252 DLAGSERVLKTG-STGERLKESIQINSTLLALGNVISALGDPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSS 330
Cdd:pfam00225 230 DLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS--KHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSS 307
|
330
....*....|....*....
gi 568947408 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 |
5.10e-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: 5.10e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 15 PVRVALRVRPLLPKELLHGHqSCLRVEPERG-RITLGRDRH-----FGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNA 88
Cdd:cd00106 1 NVRVAVRVRPLNGREARSAK-SVISVDGGKSvVLDPPKNRVappktFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 89 TVFAYGQTGSGKTYTMGEASvaslhEDEQGIIPRAMAEAFKLIDENDLLD--CLVHVSYLELYKEEFRDLLEvGTASRDI 166
Cdd:cd00106 80 TIFAYGQTGSGKTYTMLGPD-----PEQRGIIPRALEDIFERIDKRKETKssFSVSASYLEIYNEKIYDLLS-PVPKKPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 167 QLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSrlprpaAGHLLVS 246
Cdd:cd00106 154 SLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKS------GESVTSS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRgsHIPYRDSKITRILKDSLGGNAKTVMIACV 326
Cdd:cd00106 228 KLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNK--HIPYRDSKLTRLLQDSLGGNSKTIMIACI 305
|
330 340
....*....|....*....|.
gi 568947408 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 568947408 16 VRVALRVRPLLPKELLHGHQSCLRV---------EPERGRITL-------------GRDRHFGFHVVLGEDTGQEAVYQA 73
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVmdnhmlvfdPKDEEDGFFhggsnnrdrrkrrNKELKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 74 CVQPLLEAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLHEDEQGIIPRAMAEAFKLIDE-NDLLDCLVHVSYLELYKEE 152
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTM------LGTPQEPGLMVLTMKELFKRIESlKDEKEFEVSMSYLEIYNET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 153 FRDLLEvgTASRDIQLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTP 232
Cdd:cd01370 156 IRDLLN--PSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 233 SRLPRPAAGHLLVskfhfVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRGSHIPYRDSKITRILKD 312
Cdd:cd01370 234 SINQQVRQGKLSL-----IDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKNKHIPYRDSKLTRLLKD 308
|
330 340 350
....*....|....*....|....*....|....*..
gi 568947408 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 |
7.16e-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: 7.16e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 16 VRVALRVRPLLPKELLHGHQSCLRVEPERGRITL--GRD------RHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFN 87
Cdd:cd01371 3 VKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVrnPKAtaneppKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEGYN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 88 ATVFAYGQTGSGKTYTMGEASVAslhEDEQGIIPRAMAEAFKLID-ENDLLDCLVHVSYLELYKEEFRDLLEVGTASRdI 166
Cdd:cd01371 83 GTIFAYGQTGTGKTYTMEGKRED---PELRGIIPNSFAHIFGHIArSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKR-L 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 167 QLRED-DRGNVV--LCGVKEVDVEGLDEVLSLlemGNAARHTGATHFNRLSSRSHTVFTVTLEQrgrtpSRLPRPAAGHL 243
Cdd:cd01371 159 ELKERpDTGVYVkdLSMFVVKNADEMEHVMNL---GNKNRSVGATNMNEDSSRSHAIFTITIEC-----SEKGEDGENHI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 244 LVSKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPqrRGSHIPYRDSKITRILKDSLGGNAKTVMI 323
Cdd:cd01371 231 RVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KSTHIPYRDSKLTRLLQDSLGGNSKTVMC 308
|
330 340
....*....|....*....|....*.
gi 568947408 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 |
7.71e-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: 7.71e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 16 VRVALRVRPLLPKELLHGHQSCLRVEPERGRITLGRDRH------------FGFHVVL----GED---TGQEAVYQACVQ 76
Cdd:cd01365 3 VKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADknnkatrevpksFSFDYSYwshdSEDpnyASQEQVYEDLGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 77 PLLEAFFEGFNATVFAYGQTGSGKTYTMGEAsvaslhEDEQGIIPRAMAEAFKLID--ENDLLDCLVHVSYLELYKEEFR 154
Cdd:cd01365 83 ELLQHAFEGYNVCLFAYGQTGSGKSYTMMGT------QEQPGIIPRLCEDLFSRIAdtTNQNMSYSVEVSYMEIYNEKVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 155 DLLEVGTASRDIQL--REDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRgRTP 232
Cdd:cd01365 157 DLLNPKPKKNKGNLkvREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQK-RHD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 233 SRLPRPAAghlLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQR-----RGSHIPYRDSKIT 307
Cdd:cd01365 236 AETNLTTE---KVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskkKSSFIPYRDSVLT 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 568947408 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 |
1.27e-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: 1.27e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 16 VRVALRVRPLLPKELLHG--------HQSCLRVEPERGRitlgrdrhFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFN 87
Cdd:cd01374 2 ITVTVRVRPLNSREIGINeqvaweidNDTIYLVEPPSTS--------FTFDHVFGGDSTNREVYELIAKPVVKSALEGYN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 88 ATVFAYGQTGSGKTYTMgeasvaSLHEDEQGIIPRAMAEAFKLIDENDLLDCLVHVSYLELYKEEFRDLLEVGtaSRDIQ 167
Cdd:cd01374 74 GTIFAYGQTSSGKTFTM------SGDEDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLLSPT--SQNLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 168 LREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPsrlprPAAGHLLVSK 247
Cdd:cd01374 146 IRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGE-----LEEGTVRVST 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 248 FHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRGsHIPYRDSKITRILKDSLGGNAKTVMIACVS 327
Cdd:cd01374 221 LNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKVGG-HIPYRDSKLTRILQPSLGGNSRTAIICTIT 299
|
330 340
....*....|....*....|..
gi 568947408 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 |
1.65e-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: 1.65e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 16 VRVALRVRPLLPKELLHGHQSCLRVEPERGRITL--------GRDRHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFN 87
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 88 ATVFAYGQTGSGKTYTM-GEASVASLHEDEQ----GIIPRAMAEAFKLIDENDLlDCLVHVSYLELYKEEFRDLLEV-GT 161
Cdd:cd01364 84 CTIFAYGQTGTGKTYTMeGDRSPNEEYTWELdplaGIIPRTLHQLFEKLEDNGT-EYSVKVSYLEIYNEELFDLLSPsSD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 162 ASRDIQLREDDR--GNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSrlprpa 239
Cdd:cd01364 163 VSERLRMFDDPRnkRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTID------ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 240 aGHLLV--SKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDpqrRGSHIPYRDSKITRILKDSLGGN 317
Cdd:cd01364 237 -GEELVkiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE---RAPHVPYRESKLTRLLQDSLGGR 312
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 568947408 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 |
5.07e-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: 5.07e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 16 VRVALRVRPLLPKELlHGHQSCLRVEPERG-RITL---GRDRH-FGFHVVLGEDTGQEAVYQAcVQPLLEAFFEGFNATV 90
Cdd:cd01366 4 IRVFCRVRPLLPSEE-NEDTSHITFPDEDGqTIELtsiGAKQKeFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 91 FAYGQTGSGKTYTMgeasvaSLHEDEQGIIPRAMAEAFKLIDENDLLDCLVH--VSYLELYKEEFRDLLEVGTASR---D 165
Cdd:cd01366 82 FAYGQTGSGKTYTM------EGPPESPGIIPRALQELFNTIKELKEKGWSYTikASMLEIYNETIRDLLAPGNAPQkklE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 166 IQlREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLeqRGRTPSRlprpaaGHLLV 245
Cdd:cd01366 156 IR-HDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI--SGRNLQT------GEISV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 246 SKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGdpqRRGSHIPYRDSKITRILKDSLGGNAKTVMIAC 325
Cdd:cd01366 227 GKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR---QKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVN 303
|
330 340
....*....|....*....|....*.
gi 568947408 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 |
5.03e-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: 5.03e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 16 VRVALRVRPLLPKELLHGHQSCLRVEPERgRITLGRD---RHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNATVFA 92
Cdd:cd01369 4 IKVVCRFRPLNELEVLQGSKSIVKFDPED-TVVIATSetgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTIFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 93 YGQTGSGKTYTMgeasVASLHEDE-QGIIPRAMAEAFKLIDEND-LLDCLVHVSYLELYKEEFRDLLEVgtaSRD-IQLR 169
Cdd:cd01369 83 YGQTSSGKTYTM----EGKLGDPEsMGIIPRIVQDIFETIYSMDeNLEFHVKVSYFEIYMEKIRDLLDV---SKTnLSVH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 170 EDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTpsrlprpaAGHLLVSKFH 249
Cdd:cd01369 156 EDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVE--------TEKKKSGKLY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 250 FVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSPS 329
Cdd:cd01369 228 LVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK--THIPYRDSKLTRILQDSLGGNSRTTLIICCSPS 305
|
330 340
....*....|....*....|
gi 568947408 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 |
8.04e-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: 8.04e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 15 PVRVALRVRPLLPKELLHGHQSCLRVEPERGRITLG-RDRHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNATVFAY 93
Cdd:cd01373 2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSkPPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 94 GQTGSGKTYTM-GEAS--VASLHEDeQGIIPRAMAEAFKLID-----ENDLLDCLVHVSYLELYKEEFRDLLEvgTASRD 165
Cdd:cd01373 82 GQTGSGKTYTMwGPSEsdNESPHGL-RGVIPRIFEYLFSLIQrekekAGEGKSFLCKCSFLEIYNEQIYDLLD--PASRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 166 IQLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSrlprpaAGHLLV 245
Cdd:cd01373 159 LKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKAC------FVNIRT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 246 SKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGD-PQRRGSHIPYRDSKITRILKDSLGGNAKTVMIA 324
Cdd:cd01373 233 SRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvAHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIA 312
|
330 340 350
....*....|....*....|....*....|..
gi 568947408 325 CVSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:cd01373 313 NVHPSSKCFGETLSTLRFAQRAKLIKNKAVVN 344
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
55-356 |
4.91e-85 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 289.33 E-value: 4.91e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 55 FGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLHEDEQGIIPRAMAEAFKLIDEN 134
Cdd:COG5059 58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTM------SGTEEEPGIIPLSLKELFSKLEDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 135 DLLDCL-VHVSYLELYKEEFRDLLEVGTASRDIqlREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRL 213
Cdd:COG5059 132 SMTKDFaVSISYLEIYNEKIYDLLSPNEESLNI--REDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 214 SSRSHTVFTVTLEQRGRTPSRLPRpaaghllvSKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQ 293
Cdd:COG5059 210 SSRSHSIFQIELASKNKVSGTSET--------SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKK 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568947408 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 |
3.87e-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: 3.87e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 15 PVRVALRVRPLLPKELLHGHQSCLRVE--------PERGRITLGRDR-------HFGFHVVLGEDTGQEAVYQACVQPLL 79
Cdd:cd01368 2 PVKVYLRVRPLSKDELESEDEGCIEVInsttvvlhPPKGSAANKSERnggqketKFSFSKVFGPNTTQKEFFQGTALPLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 80 EAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLHEDEQGIIPRAMAEAFKLIDENDlldclVHVSYLELYKEEFRDLLEV 159
Cdd:cd01368 82 QDLLHGKNGLLFTYGVTNSGKTYTM------QGSPGDGGILPRSLDVIFNSIGGYS-----VFVSYIEIYNEYIYDLLEP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 160 GTASRD-----IQLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQrgrtpsr 234
Cdd:cd01368 151 SPSSPTkkrqsLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQ------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 235 LPRPAAGHLL-------VSKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRG--SHIPYRDSK 305
Cdd:cd01368 224 APGDSDGDVDqdkdqitVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGtnKMVPFRDSK 303
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 568947408 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 |
3.52e-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: 3.52e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 15 PVRVALRVRPLLPKELLHGHQ--------SCLRVEPERGRITLGR--DRH-FGFHVVLGEDTGQEAVYQACVQPLLEAFF 83
Cdd:cd01367 1 KIKVCVRKRPLNKKEVAKKEIdvvsvpskLTLIVHEPKLKVDLTKyiENHtFRFDYVFDESSSNETVYRSTVKPLVPHIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 84 EGFNATVFAYGQTGSGKTYTMGEASvaSLHEDEQGIIPRAMAEAFKLIDE-NDLLDCLVHVSYLELYKEEFRDLLEVGTa 162
Cdd:cd01367 81 EGGKATCFAYGQTGSGKTYTMGGDF--SGQEESKGIYALAARDVFRLLNKlPYKDNLGVTVSFFEIYGGKVFDLLNRKK- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 163 srDIQLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLeqrgrtpsrlpRPAAGH 242
Cdd:cd01367 158 --RVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL-----------RDRGTN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 243 LLVSKFHFVDLAGSER-VLKTGSTGERLKESIQINSTLLALGNVISALGDPQrrgSHIPYRDSKITRILKDSL-GGNAKT 320
Cdd:cd01367 225 KLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNK---AHIPFRGSKLTQVLKDSFiGENSKT 301
|
330 340
....*....|....*....|....*
gi 568947408 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 |
7.64e-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: 7.64e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 15 PVRVALRVRPLLPKELLHGHQSCLRVEPERgRITLGRDRHFG------FHVVLGEDTGQEAVYQACVQPLLEAFFEGFNA 88
Cdd:cd01376 1 NVRVAVRVRPFVDGTAGASDPSCVSGIDSC-SVELADPRNHGetlkyqFDAFYGEESTQEDIYAREVQPIVPHLLEGQNA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 89 TVFAYGQTGSGKTYTM-GeasvaslHEDEQGIIPRAMAEAFKLIDENDLLDClVHVSYLELYKEEFRDLLEVgtASRDIQ 167
Cdd:cd01376 80 TVFAYGSTGAGKTFTMlG-------SPEQPGLMPLTVMDLLQMTRKEAWALS-FTMSYLEIYQEKILDLLEP--ASKELV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 168 LREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRT-PSRLPRpaaghllvS 246
Cdd:cd01376 150 IREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLaPFRQRT--------G 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRgshIPYRDSKITRILKDSLGGNAKTVMIACV 326
Cdd:cd01376 222 KLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPR---IPYRDSKLTRLLQDSLGGGSRCIMVANI 298
|
330 340
....*....|....*....|.
gi 568947408 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 568947408 55 FGFHVVLgEDTGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMGEASVASLHedeQGIIPRAMAEAFKLIDEN 134
Cdd:cd01375 50 FKFDGVL-HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENYKH---RGIIPRALQQVFRMIEER 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 135 DLLDCLVHVSYLELYKEEFRDLL----EVGTASRDIQLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHF 210
Cdd:cd01375 126 PTKAYTVHVSYLEIYNEQLYDLLstlpYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTM 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 211 NRLSSRSHTVFTVTLEQRGRTPSrlprpaAGHLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALG 290
Cdd:cd01375 206 NKNSSRSHCIFTIHLEAHSRTLS------SEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALS 279
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568947408 291 DPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASR 345
Cdd:cd01375 280 DKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASR 332
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
10-356 |
8.70e-59 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 222.89 E-value: 8.70e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 10 GAEEAPVRVALRVRPLLPKEllhghQSCLRVEPERGRITLGRDRHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNAT 89
Cdd:PLN03188 94 GVSDSGVKVIVRMKPLNKGE-----EGEMIVQKMSNDSLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 90 VFAYGQTGSGKTYTM-GEASVAS---LHEDEQGIIPRAMAEAFKLIDENDL------LDCLVHVSYLELYKEEFRDLLEv 159
Cdd:PLN03188 169 VFAYGQTGSGKTYTMwGPANGLLeehLSGDQQGLTPRVFERLFARINEEQIkhadrqLKYQCRCSFLEIYNEQITDLLD- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 160 gTASRDIQLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSrlprPA 239
Cdd:PLN03188 248 -PSQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVA----DG 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 240 AGHLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRGS--HIPYRDSKITRILKDSLGGN 317
Cdd:PLN03188 323 LSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKqrHIPYRDSRLTFLLQESLGGN 402
|
330 340 350
....*....|....*....|....*....|....*....
gi 568947408 318 AKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:PLN03188 403 AKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVN 441
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
707-1203 |
4.36e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.30 E-value: 4.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 707 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQ----EAERVRAELCEGQRQLRELEGREPQDA 782
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiarLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 783 SERSRLQEFRKRVAAAQSQVQVLKEK-KQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEM 861
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAElAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 862 NKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsvvSLEQQQKIEEQKKWLDQEMEKVLQQRRALEEL-GEE 940
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE-------EAELEEEEEALLELLAELLEEAALLEAALAELlEEL 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 941 LRKREVILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEksgQLRQGSAQNQQQIRGEIDTLRQEKD 1020
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA---ALEAALAAALQNIVVEDDEVAAAAI 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1021 SLLKQ----RLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEM--NLMAKLS 1094
Cdd:COG1196 564 EYLKAakagRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAalRRAVTLA 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1095 YLSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNVQLLLQ 1174
Cdd:COG1196 644 GRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
|
490 500
....*....|....*....|....*....
gi 568947408 1175 QGRDHLGEGLADSKRQYEARIHALEKELG 1203
Cdd:COG1196 724 EALEEQLEAEREELLEELLEEEELLEEEA 752
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
744-1215 |
3.13e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.60 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 744 RQHSQRIRELEQEAERVRAELCEGQRQLRELEGREpqdASERSRLQEFRKRVAAAQSQVQVLKEKKQATE----RLVSLS 819
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAEL---EELRLELEELELELEEAQAEEYELLAELARLEqdiaRLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 820 AQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSG 899
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 900 SNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKtglESKRLRSSQALNEDIVRV 979
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE---EAELEEEEEALLELLAEL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 980 SSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKL-RQGSLLSPEEERTLFQLDEAIEALD 1058
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLaGAVAVLIGVEAAYEAALEAALAAAL 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1059 AAIEYKNE--AITCRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSE-------- 1128
Cdd:COG1196 549 QNIVVEDDevAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDtllgrtlv 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1129 ---LEMQLEEQQRLVY-WLEVALERQRLEMDRQLTLQQKEH--------EQNVQLLLQQGRDHLGEGLADSKRQYEARIH 1196
Cdd:COG1196 629 aarLEAALRRAVTLAGrLREVTLEGEGGSAGGSLTGGSRREllaalleaEAELEELAERLAEEELELEEALLAEEEEERE 708
|
490
....*....|....*....
gi 568947408 1197 ALEKELGRHMWINQELKQK 1215
Cdd:COG1196 709 LAEAEEERLEEELEEEALE 727
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
730-1067 |
2.04e-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: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 730 GELVRTG---------KAAQALNRQhsQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASE----RSRLQEFRKRVA 796
Cdd:TIGR02168 652 GDLVRPGgvitggsakTNSSILERR--REIEELEEKIEELEEKIAELEKALAELRKELEELEEEleqlRKELEELSRQIS 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 797 AAQSQVQVLKEKkqaTERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHE 876
Cdd:TIGR02168 730 ALRKDLARLEAE---VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 877 QQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQ 956
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 957 EKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRqgsaQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQG 1036
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE----LRLEGLEVRIDNLQERLSEEYSLTLEEAEALENK 962
|
330 340 350
....*....|....*....|....*....|....*..
gi 568947408 1037 SLLSPEE-ERTLFQLDEAIEA-----LDAAIEYKNEA 1067
Cdd:TIGR02168 963 IEDDEEEaRRRLKRLENKIKElgpvnLAAIEEYEELK 999
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
712-1135 |
9.14e-12 |
|
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: 69.66 E-value: 9.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 712 QQKIREL-AINIRMKEELIGELVRTGKAAQALNRQHSQrIRELEQEAERVRAELCEGQRQL-------RELEGREPQDAS 783
Cdd:TIGR04523 217 ESQISELkKQNNQLKDNIEKKQQEINEKTTEISNTQTQ-LNQLKDEQNKIKKQLSEKQKELeqnnkkiKELEKQLNQLKS 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 784 ERSRL-----QEFRKRVaaaQSQVQVLKEKKQATERLVSlsaQSETRLQELERNVQLMRrqqgqlqrrlreetEQKRRLE 858
Cdd:TIGR04523 296 EISDLnnqkeQDWNKEL---KSELKNQEKKLEEIQNQIS---QNNKIISQLNEQISQLK--------------KELTNSE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 859 TEMNKRQhrvKELElkhEQQQKILKIKTEEIAAFQRKRRSGSNGSvvSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEEL 937
Cdd:TIGR04523 356 SENSEKQ---RELE---EKQNEIEKLKKENQSYKQEIKNLESQIN--DLESKiQNQEKLNQQKDEQIKKLQQEKELLEKE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 938 GEELRKrEVILAKKE--ALMQEKTGLES-----KRLRSSQ-----ALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQ 1005
Cdd:TIGR04523 428 IERLKE-TIIKNNSEikDLTNQDSVKELiiknlDNTRESLetqlkVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1006 QqIRGEIDTLRQEKDSLL-------KQRLEIDSKLRQ--GSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITcrqrvlr 1076
Cdd:TIGR04523 507 E-LEEKVKDLTKKISSLKekiekleSEKKEKESKISDleDELNKDDFELKKENLEKEIDEKNKEIEELKQTQK------- 578
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 568947408 1077 asaSLLSqcemnlmaklsylSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEE 1135
Cdd:TIGR04523 579 ---SLKK-------------KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
705-1216 |
1.99e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.94 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 705 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQ------ALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGRE 778
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELKELKEKAEeyiklsEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 779 PQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETR-LQELERNVQLMRRQQGQLQRRLREETEQKRRL 857
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLtPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 858 ETEMNKRQHRVKEL------------ELKHEQQQKILKIKTEEIAafqrkrrsgsngsvvsleqqqKIEEQKKWLDQEME 925
Cdd:PRK03918 418 KKEIKELKKAIEELkkakgkcpvcgrELTEEHRKELLEEYTAELK---------------------RIEKELKEIEEKER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 926 KVlqqRRALEELGEELRKREVILAKKEALMQektgLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLR--QGSAQ 1003
Cdd:PRK03918 477 KL---RKELRELEKVLKKESELIKLKELAEQ----LKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKslKKELE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1004 NQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEertlfqLDEAIEALDAAIEYKNEAITCRQRvLRASASLLS 1083
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE------LEERLKELEPFYNEYLELKDAEKE-LEREEKELK 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1084 QCEMNLMAKLSYLSSSETRallckyfdkVVTLREEQHQQQIAFSElemqlEEQQRlvywlevaLERQRLEMDRQLTLQQK 1163
Cdd:PRK03918 623 KLEEELDKAFEELAETEKR---------LEELRKELEELEKKYSE-----EEYEE--------LREEYLELSRELAGLRA 680
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 568947408 1164 EHEQnvqllLQQGRDHLGEGLADSKRQYEARIHALE--KELGRHMWINQELKQKL 1216
Cdd:PRK03918 681 ELEE-----LEKRREEIKKTLEKLKEELEEREKAKKelEKLEKALERVEELREKV 730
|
|
| 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 568947408 18 VALRVRPLLpkellhghqsclRVEPERGRITLGRDRHFGFHvvlgedTGQEAVYqACVQPLLEAFFEGFN-ATVFAYGQT 96
Cdd:cd01363 1 VLVRVNPFK------------ELPIYRDSKIIVFYRGFRRS------ESQPHVF-AIADPAYQSMLDGYNnQSIFAYGES 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 97 GSGKTYTMgeasvaslhedeQGIIPRAMAEAFklidendlldclvhvSYLELYKEEFRDLLEvgtasrdiqlreddrgnv 176
Cdd:cd01363 62 GAGKTETM------------KGVIPYLASVAF---------------NGINKGETEGWVYLT------------------ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 177 vlcgvkEVDVEGLDEVLSLLEMGNAARhTGATHFNRLSSRSHTVFTVtleqrgrtpsrlprpaaghllvskfhFVDLAGS 256
Cdd:cd01363 97 ------EITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI--------------------------LLDIAGF 143
|
250 260 270
....*....|....*....|....*....|..
gi 568947408 257 ERvlktgstgerlkesiqINSTLLALGNVISA 288
Cdd:cd01363 144 EI----------------INESLNTLMNVLRA 159
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
748-1062 |
2.73e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 748 QRIRELEQEAERVR--AELcegQRQLRELEGREpqdasersRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETR 825
Cdd:COG1196 200 RQLEPLERQAEKAEryREL---KEELKELEAEL--------LLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 826 LQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsvv 905
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE------- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 906 slEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLRSSQALnEDIVRVSSRLEH 985
Cdd:COG1196 342 --LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE-EAEEALLERLER 418
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568947408 986 LEKELSEKsgqlrqgsAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIE 1062
Cdd:COG1196 419 LEEELEEL--------EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
708-1035 |
5.07e-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: 67.35 E-value: 5.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 708 LAQAQQKIRELAINIRMKEELIGELvrtgkaaqalNRQHSQ---RIRELEQEAERVRAELCEGQRQLRELEgREPQdase 784
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQNNKIISQL----------NEQISQlkkELTNSESENSEKQRELEEKQNEIEKLK-KENQ---- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 785 rSRLQEFRKrvaaAQSQVQVLKEKKQATERLvslSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKR 864
Cdd:TIGR04523 381 -SYKQEIKN----LESQINDLESKIQNQEKL---NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 865 QHRVKELELKHEQQQKILKIKTEEIAAFQRKrrsgsngsvvsLEQQQKIEEQKKwldQEMEKVLQQRRALEELGEELRKR 944
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQN-----------LEQKQKELKSKE---KELKKLNEEKKELEEKVKDLTKK 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 945 -EVILAKKEALMQEKTGLESKrLRSsqaLNEDIVRVSSRL--EHLEKELSEKsgqlrqgsaqNQqqirgEIDTLRQEKDS 1021
Cdd:TIGR04523 519 iSSLKEKIEKLESEKKEKESK-ISD---LEDELNKDDFELkkENLEKEIDEK----------NK-----EIEELKQTQKS 579
|
330
....*....|....
gi 568947408 1022 LLKQRLEIDSKLRQ 1035
Cdd:TIGR04523 580 LKKKQEEKQELIDQ 593
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
800-1084 |
7.30e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 7.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 800 SQVQVLKEKKQATERLVSLSAQSETRLQELE-RNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQ 878
Cdd:COG1196 200 RQLEPLERQAEKAERYRELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 879 QKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRAL-EELGEELRKREVILAKKEALMQE 957
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELeEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 958 KTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQlrqgsAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGS 1037
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL-----AAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 568947408 1038 LLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQ 1084
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
748-1084 |
9.88e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 9.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 748 QRIRELEQEAERVRAELCEGQRQLRELEgrepQDASERSRLQEFRKRVAAAQSQVQV--LKEKKQATERLVSLSAQSETR 825
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSLE----RQAEKAERYKELKAELRELELALLVlrLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 826 LQELERnvqlmrrqqgqlqrrlreeteQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVV 905
Cdd:TIGR02168 255 LEELTA---------------------ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 906 SLEQQQKIEEQkkwLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEH 985
Cdd:TIGR02168 314 LERQLEELEAQ---LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 986 LEKELSEKSGQLRQGSAQnQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLlsPEEERTLFQLDEAIEALDAAIEYKN 1065
Cdd:TIGR02168 391 LELQIASLNNEIERLEAR-LERLEDRRERLQQEIEELLKKLEEAELKELQAEL--EELEEELEELQEELERLEEALEELR 467
|
330
....*....|....*....
gi 568947408 1066 EAITCRQRVLRASASLLSQ 1084
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQ 486
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
716-1062 |
1.74e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.86 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 716 RELAINIRMKEeLIGELVRTGKAAQALNRQHSQRI---RELEQEAERVRAELCEGQRQLrelegrepqdASERSRLQEFR 792
Cdd:TIGR02169 633 RRLMGKYRMVT-LEGELFEKSGAMTGGSRAPRGGIlfsRSEPAELQRLRERLEGLKREL----------SSLQSELRRIE 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 793 KRVAAAQSQVQVlkekkqATERLVSLSAQSETRLQELERNVQLMRRQQgqlqRRLREETEQKRRLETEMNKRQHRVKELE 872
Cdd:TIGR02169 702 NRLDELSQELSD------ASRKIGEIEKEIEQLEQEEEKLKERLEELE----EDLSSLEQEIENVKSELKELEARIEELE 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 873 LK-HEQQQKILKIKT-------EEIAA---FQRKRRSGSNGSVVSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEELGEE 940
Cdd:TIGR02169 772 EDlHKLEEALNDLEArlshsriPEIQAelsKLEEEVSRIEARLREIEQKlNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 941 LRKR-EVILAKKEALMQEktgLESKRLRSSQalnedivrVSSRLEHLEKELSEKSGQLRQgSAQNQQQIRGEIDTLR--- 1016
Cdd:TIGR02169 852 IEKEiENLNGKKEELEEE---LEELEAALRD--------LESRLGDLKKERDELEAQLRE-LERKIEELEAQIEKKRkrl 919
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 568947408 1017 ---QEKDSLLKQRL-EIDSKLRQGSlLSPEEERTLFQLDEAIEALDAAIE 1062
Cdd:TIGR02169 920 selKAKLEALEEELsEIEDPKGEDE-EIPEEELSLEDVQAELQRVEEEIR 968
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
849-1228 |
3.73e-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: 64.69 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 849 EETEQKRRlETEMN-----------KRQhrVKELELKHEQQQKILKIKTEEiaafQRKRRSGSNGSVVSL-EQQQKIEEQ 916
Cdd:TIGR02168 175 KETERKLE-RTRENldrledilnelERQ--LKSLERQAEKAERYKELKAEL----RELELALLVLRLEELrEELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 917 KKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLrssQALNEDIVRVSSRLEHLEKELSEKSGQ 996
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI---SRLEQQKQILRERLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 997 LRQGSAQNQQQIRgEIDTLRQEKDSLLKQRLEIDSKLrqgsllsPEEERTLFQLDEAIEALDAAIEYKNEAItcrqrvlr 1076
Cdd:TIGR02168 325 LEELESKLDELAE-ELAELEEKLEELKEELESLEAEL-------EELEAELEELESRLEELEEQLETLRSKV-------- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1077 asASLLSQcEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERqrleMDR 1156
Cdd:TIGR02168 389 --AQLELQ-IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELER----LEE 461
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568947408 1157 QLTLQQKEHEQNVQLLLQQGRDHlgegladskRQYEARIHALEKELGRHMWINQELKQKLSAGSTAGQSRGC 1228
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAEREL---------AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV 524
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
708-1216 |
4.03e-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: 64.69 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 708 LAQAQQKIRELAINIRMKEELI-------GELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQ 780
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLeelrlevSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 781 DASERSRLQEFRKRVAAAQSQVQV-LKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLET 859
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEeLESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 860 EMNKRQHRVKEL-ELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQ-QQKIEEQKKWLDQEMEKVLQQRRALEEL 937
Cdd:TIGR02168 408 RLERLEDRRERLqQEIEELLKKLEEAELKELQAELEELEEELEELQEELERlEEALEELREELEEAEQALDAAERELAQL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 938 GEELRKREVILAKKEALMQEKTGLESKRLRSSQALNE--DIVRVSSRLEH-LEKELSEKSGQLrqgSAQNQQQIRGEIDT 1014
Cdd:TIGR02168 488 QARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVlsELISVDEGYEAaIEAALGGRLQAV---VVENLNAAKKAIAF 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1015 LRQE---KDSLLKQRLEIDSKLRQGSLLSPEEER----TLFQLDEAIEALDAAIEY--------KNEAITCRQRV-LRAS 1078
Cdd:TIGR02168 565 LKQNelgRVTFLPLDSIKGTEIQGNDREILKNIEgflgVAKDLVKFDPKLRKALSYllggvlvvDDLDNALELAKkLRPG 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1079 ASLLSQcEMNLMAK--LSYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLE---VALERQRLE 1153
Cdd:TIGR02168 645 YRIVTL-DGDLVRPggVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEeelEQLRKELEE 723
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568947408 1154 MDRQLTLQQKE---HEQNVQLLLQQGRDHLGE--GLADSKRQYEARIHALEKELGRHMWINQELKQKL 1216
Cdd:TIGR02168 724 LSRQISALRKDlarLEAEVEQLEERIAQLSKEltELEAEIEELEERLEEAEEELAEAEAEIEELEAQI 791
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
709-1035 |
4.98e-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: 64.31 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 709 AQAQQKIR-----------ELAINIRMKEELIGELVRTGKAAQALNRQHSQ---RIRELEQEAERVRAELCEGQRQLREL 774
Cdd:TIGR02168 207 RQAEKAERykelkaelrelELALLVLRLEELREELEELQEELKEAEEELEEltaELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 775 EGREPQDASERSRL----QEFRKRVAAAQSQVQV----LKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRR 846
Cdd:TIGR02168 287 QKELYALANEISRLeqqkQILRERLANLERQLEEleaqLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 847 LREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsvvslEQQQKIEEQKKWLDQEMEK 926
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER---------LQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 927 VLQQRRALEELGEELRKR-EVILAKKEALMQEKTGLESKRlrssQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSA--Q 1003
Cdd:TIGR02168 438 LQAELEELEEELEELQEElERLEEALEELREELEEAEQAL----DAAERELAQLQARLDSLERLQENLEGFSEGVKAllK 513
|
330 340 350
....*....|....*....|....*....|..
gi 568947408 1004 NQQQIRGEIDtlrqekdsLLKQRLEIDSKLRQ 1035
Cdd:TIGR02168 514 NQSGLSGILG--------VLSELISVDEGYEA 537
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
16-157 |
1.91e-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: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 16 VRVALRVRPLLPKELlhghqsclRVEPERGRITLGRDRH----FGFHVVLGEDTGQEAVYQACVQpLLEAFFEGFNATVF 91
Cdd:pfam16796 22 IRVFARVRPELLSEA--------QIDYPDETSSDGKIGSknksFSFDRVFPPESEQEDVFQEISQ-LVQSCLDGYNVCIF 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568947408 92 AYGQTGSGKTYTMgeasvaslhedeqgiIPRAMAEAFKLIDENDLLDCL-VHVSYLELYKEEFRDLL 157
Cdd:pfam16796 93 AYGQTGSGSNDGM---------------IPRAREQIFRFISSLKKGWKYtIELQFVEIYNESSQDLL 144
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
796-1041 |
5.43e-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: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 796 AAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKH 875
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 876 EQQQKILKIKTEEIAAFQRKR-RSGSNGSVVSLEQQQKIEEQKKWLdQEMEKVLQQRRA-LEELGEELRKREVILAKKEA 953
Cdd:COG4942 93 AELRAELEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRL-QYLKYLAPARREqAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 954 LMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQgSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKL 1033
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE-LQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....*...
gi 568947408 1034 RQGSLLSP 1041
Cdd:COG4942 251 LKGKLPWP 258
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
703-1034 |
1.43e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 703 ASEWRLAQAQQKIRELAiniRMKEELIGELVRTGKAAQALNR--QHSQRIRELEQEAERVRAELCEGQRQLRELEgrEPQ 780
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEA---KKADEAKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKKADEAKKAEEAKKAD--EAK 1540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 781 DASERSRLQEFRK--RVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRrlreETEQKRRLE 858
Cdd:PTZ00121 1541 KAEEKKKADELKKaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM----KAEEAKKAE 1616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 859 TEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKW--LDQEMEKVLQQRRALEE 936
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKK 1696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 937 LGEELRKREViLAKKEALMQEKtgleSKRLRSSQALNEDIVRVSSRLEHLEKELSE----------KSGQLRQGSAQNQQ 1006
Cdd:PTZ00121 1697 EAEEAKKAEE-LKKKEAEEKKK----AEELKKAEEENKIKAEEAKKEAEEDKKKAEeakkdeeekkKIAHLKKEEEKKAE 1771
|
330 340 350
....*....|....*....|....*....|
gi 568947408 1007 QIRGEIDTLRQE--KDSLLKQRLEIDSKLR 1034
Cdd:PTZ00121 1772 EIRKEKEAVIEEelDEEDEKRRMEVDKKIK 1801
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
707-1084 |
1.84e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 707 RLAQAQQKIRELAINIRMKEELIGELVRTGK---AAQALNRQHSQRIRELEQ--EAERVRAELCEGQRQLRELEGREPQD 781
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEeleELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 782 ASERSRLQEFRKRVAAAQSQVQVLKEkkQATERLVSLSAQSETRLQELERNVQlmrrqqgQLQRRLREETEQKRRLETEM 861
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQE--ELEELLEQLSLATEEELQDLAEELE-------ELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 862 NKRQHRVKELELKHEQQQKILKIKTEEIAAF------------------------------------------QRKRRSG 899
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsliltiagvlflvlgllallflllarEKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 900 SNGSVVSLEQQQKIEEQK-------------------KWLDQEMEKVLQQRRALEELGEELRkREVILAKKEALMQEKTG 960
Cdd:COG4717 303 EAEELQALPALEELEEEEleellaalglppdlspeelLELLDRIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 961 LESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQ--------QQIRGEIDTLRQEKDSLLKQRLEIDSK 1032
Cdd:COG4717 382 EDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeeleeelEELEEELEELEEELEELREELAELEAE 461
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 568947408 1033 LRQgsllsPEEERTLFQLDEAIEALDAAIEYKNEAItcrqRVLRASASLLSQ 1084
Cdd:COG4717 462 LEQ-----LEEDGELAELLQELEELKAELRELAEEW----AALKLALELLEE 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
703-1019 |
1.94e-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: 59.31 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 703 ASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQ---RIRELEQEAERVRAELCEGQRQLRELEGREp 779
Cdd:TIGR02169 210 AERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKlteEISELEKRLEEIEQLLEELNKKIKDLGEEE- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 780 qDASERSRLQEFRKRVAAAQSQVqvlKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLET 859
Cdd:TIGR02169 289 -QLRVKEKIGELEAEIASLERSI---AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 860 EMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGE 939
Cdd:TIGR02169 365 ELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 940 ELRKRevILAKKEALMQEKTGLESKRlrssqalnEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEK 1019
Cdd:TIGR02169 445 DKALE--IKKQEWKLEQLAADLSKYE--------QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
750-1135 |
2.09e-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: 58.93 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 750 IRELEQEAERVRAELCEGQRQLRELEGREPQDASERSRLQefrkrvaaaqsqvqvlKEKKQATERLVSLSAQSETRLQEL 829
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLR----------------REREKAERYQALLKEKREYEGYEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 830 ERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQ-QQKILKIKTEEIAAFQRKRRSGSnGSVVSLE 908
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELE-AEIASLE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 909 --------QQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRKRevilakKEALMQEktgleskrLRSSQALNEDIVrvs 980
Cdd:TIGR02169 308 rsiaekerELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR------RDKLTEE--------YAELKEELEDLR--- 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 981 SRLEhlekELSEKSGQLRQGSAQNQQqirgEIDTLRQEKDSLLKQRLEIDSKLRqgsllspeeertlfQLDEAIEALDAA 1060
Cdd:TIGR02169 371 AELE----EVDKEFAETRDELKDYRE----KLEKLKREINELKRELDRLQEELQ--------------RLSEELADLNAA 428
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568947408 1061 IEYKNEAITCRQRVLRASASLLSQCEMNLMaklsylsssETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEE 1135
Cdd:TIGR02169 429 IAGIEAKINELEEEKEDKALEIKKQEWKLE---------QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
724-1003 |
3.01e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 724 MKEELIGELVRTGKAAQAlnrQHSQRIRELEQEAERVRAELCEGQRQLRELEGRepqdaseRSRLQEFRKRVAAAQSQVQ 803
Cdd:PRK03918 186 KRTENIEELIKEKEKELE---EVLREINEISSELPELREELEKLEKEVKELEEL-------KEEIEELEKELESLEGSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 804 VLKEKKQATERLVslsAQSETRLQELERNVQlmrrqqgqLQRRLREETEQKRRLETEMNKRQHRVKELElkheqqqKILK 883
Cdd:PRK03918 256 KLEEKIRELEERI---EELKKEIEELEEKVK--------ELKELKEKAEEYIKLSEFYEEYLDELREIE-------KRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 884 IKTEEIAAFQRKrrsgsngsvvsLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLES 963
Cdd:PRK03918 318 RLEEEINGIEER-----------IKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTP 386
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568947408 964 KRlrssqaLNEDIVRVSSRLEHLEKELSE---KSGQLRQGSAQ 1003
Cdd:PRK03918 387 EK------LEKELEELEKAKEEIEEEISKitaRIGELKKEIKE 423
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
697-894 |
3.13e-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: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 697 QAPAAMASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEg 776
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 777 repqdASERSRLQEFRKRVAAAQ-----SQVQVL---KEKKQATERLVSLSAQSETR----------LQELERNVQLMRR 838
Cdd:COG4942 97 -----AELEAQKEELAELLRALYrlgrqPPLALLlspEDFLDAVRRLQYLKYLAPARreqaeelradLAELAALRAELEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568947408 839 QQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQR 894
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
705-1203 |
7.91e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 7.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 705 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQ---RIRELEQEAERVRAELCEGQRQLRELEGREPQD 781
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEElekELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 782 ASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLEtem 861
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE--- 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 862 nkrqhrvkELELKHEQQQKILKIKTEeiaaFQRKRRSGSNGSVVSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEELGEE 940
Cdd:PRK03918 356 --------ELEERHELYEEAKAKKEE----LERLKKRLTGLTPEKLEKElEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 941 LRK----------------REVILAKKEALMQEKTgLESKRLRSSQALNEDIVR-VSSRLEHLEKELSEKSGQLRqgsaq 1003
Cdd:PRK03918 424 LKKaieelkkakgkcpvcgRELTEEHRKELLEEYT-AELKRIEKELKEIEEKERkLRKELRELEKVLKKESELIK----- 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1004 nQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQ----------GSLLSPEEErtLFQLDEAIEALDAAIEYKNEAITCRQR 1073
Cdd:PRK03918 498 -LKELAEQLKELEEKLKKYNLEELEKKAEEYEklkekliklkGEIKSLKKE--LEKLEELKKKLAELEKKLDELEEELAE 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1074 VLRASASLLSQCEMNLMAKLSYLSSSETRALLCKyfDKVVTLREEQHQQQIAFSELEMQLEEQQRlvywLEVALERQRLE 1153
Cdd:PRK03918 575 LLKELEELGFESVEELEERLKELEPFYNEYLELK--DAEKELEREEKELKKLEEELDKAFEELAE----TEKRLEELRKE 648
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 568947408 1154 MDR-QLTLQQKEHEQNVQLLLQQGRDHLG-----EGLADSKRQYEARIHALEKELG 1203
Cdd:PRK03918 649 LEElEKKYSEEEYEELREEYLELSRELAGlraelEELEKRREEIKKTLEKLKEELE 704
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
932-1236 |
8.36e-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: 8.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 932 RALEELGEELRKREvilaKKEALMQEKTGLESKRLRSSQALNEdivrVSSRLEHLEKELSEKSGQLRQgSAQNQQQIRGE 1011
Cdd:TIGR02169 668 FSRSEPAELQRLRE----RLEGLKRELSSLQSELRRIENRLDE----LSQELSDASRKIGEIEKEIEQ-LEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1012 IDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAA--------IEYKNEAITCRQRVLRASASLLS 1083
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsripeIQAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1084 QCEMNLMAKLSYLSSS----ETRALLCKyfDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLE---VALERQRLEMDR 1156
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEiqelQEQRIDLK--EQIKSIEKEIENLNGKKEELEEELEELEAALRDLEsrlGDLKKERDELEA 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1157 QLT-LQQKEHEQNVQllLQQGRDHLGEgLADSKRQYEARIHALEKELGRHMWINQELkqkLSAGSTAGQSRGCERRSLCL 1235
Cdd:TIGR02169 897 QLReLERKIEELEAQ--IEKKRKRLSE-LKAKLEALEEELSEIEDPKGEDEEIPEEE---LSLEDVQAELQRVEEEIRAL 970
|
.
gi 568947408 1236 E 1236
Cdd:TIGR02169 971 E 971
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
813-1192 |
1.00e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 56.90 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 813 ERLVSLSAQSETRLQEL--ERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRqhrvKELELKhEQQQKILKIKTEEIA 890
Cdd:pfam02463 154 RRLEIEEEAAGSRLKRKkkEALKKLIEETENLAELIIDLEELKLQELKLKEQAK----KALEYY-QLKEKLELEEEYLLY 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 891 AFQRKRrsgsngsvvsLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLRSSQ 970
Cdd:pfam02463 229 LDYLKL----------NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 971 ALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKD-SLLKQRLEIDSKLRQGSLLSPEEERTLFQ 1049
Cdd:pfam02463 299 KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEiKREAEEEEEEELEKLQEKLEQLEEELLAK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1050 LDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNLMAKLS--------------YLSSSETRALLCKYFDKVVTL 1115
Cdd:pfam02463 379 KKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEekkeeleileeeeeSIELKQGKLTEEKEELEKQEL 458
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568947408 1116 REEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNVQLLLQQGRDHLGEGLADSKRQYE 1192
Cdd:pfam02463 459 KLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG 535
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
927-1192 |
1.20e-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: 56.60 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 927 VLQQRRALEELGEELrkrEVILAKKEALMQEKTGLESKRlrssQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQ 1006
Cdd:TIGR02168 672 ILERRREIEELEEKI---EELEEKIAELEKALAELRKEL----EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1007 ------QIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASAS 1080
Cdd:TIGR02168 745 leeriaQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1081 LLSQCEMNLMAKLSYLSssETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDrQLTL 1160
Cdd:TIGR02168 825 RLESLERRIAATERRLE--DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE-ELSE 901
|
250 260 270
....*....|....*....|....*....|..
gi 568947408 1161 QQKEHEQNVQlLLQQGRDHLGEGLADSKRQYE 1192
Cdd:TIGR02168 902 ELRELESKRS-ELRRELEELREKLAQLELRLE 932
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
587-1068 |
1.26e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 587 EEVSSEQQVVSGKEVKAEVLAQADKLRSA-----SSTTSEEEGEEEEEEEEEEEEPPRRTLYLRRNGISNWSQRAGLSPG 661
Cdd:PTZ00121 1258 EEARMAHFARRQAAIKAEEARKADELKKAeekkkADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKK 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 662 SPPDRKGPEVCPEEPAAAIPAPQAVGSGKVPVQTRQAPAAMASEWRLAQAQQK-----IRELAINIRMKEELIGELVRTG 736
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkkadeAKKKAEEDKKKADELKKAAAAK 1417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 737 KAAQALNR--QHSQRIRELEQEAERVR-----AELCEGQRQLREL-----EGREPQD----ASERSRLQEFRKRVAAAQS 800
Cdd:PTZ00121 1418 KKADEAKKkaEEKKKADEAKKKAEEAKkadeaKKKAEEAKKAEEAkkkaeEAKKADEakkkAEEAKKADEAKKKAEEAKK 1497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 801 QVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLEtEMNKRQHRVKELELKHEQQQK 880
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKAEEAKKAEEDK 1576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 881 ILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLD-----QEMEKVLQQRRALEEL----------GEELRKRE 945
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaEELKKAEEEKKKVEQLkkkeaeekkkAEELKKAE 1656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 946 VILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKElSEKSGQLRQGSAQNQ---QQIRGEiDTLRQEKDSL 1022
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE-AKKAEELKKKEAEEKkkaEELKKA-EEENKIKAEE 1734
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 568947408 1023 LKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAI 1068
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
740-1201 |
1.32e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 740 QALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLS 819
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 820 AQSEtRLQELERNVQlmrrqqgqlqrRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSG 899
Cdd:COG4717 129 PLYQ-ELEALEAELA-----------ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 900 SNGSVVSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGL----ESKRLRSSQALNE 974
Cdd:COG4717 197 LAEELEELQQRlAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLallgLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 975 DIVRVSSRLEHLEKELSEKSGQLRQgSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLrqgsllSPEEERTLFQLDEAI 1054
Cdd:COG4717 277 GVLFLVLGLLALLFLLLAREKASLG-KEAEELQALPALEELEEEELEELLAALGLPPDL------SPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1055 EALDAAIEYKNEAITcRQRVLRASASLLSQCEMnlmaklsylSSSETRALLCKYFDKVVTLREEqhqqqiaFSELEMQLE 1134
Cdd:COG4717 350 QELLREAEELEEELQ-LEELEQEIAALLAEAGV---------EDEEELRAALEQAEEYQELKEE-------LEELEEQLE 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568947408 1135 E-----QQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNV-------QLLLQQGRDHLGEGLADSKRQYEARIHALEKE 1201
Cdd:COG4717 413 EllgelEELLEALDEEELEEELEELEEELEELEEELEELReelaeleAELEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
694-1066 |
3.51e-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: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 694 QTRQAPAAMASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRE 773
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 774 LEGREPQDASE----RSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLRE 849
Cdd:COG1196 426 LEEALAELEEEeeeeEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 850 ETEQKRRLETEMNKR----------------------------QHRVKELELKHEQQQKILKIKTEEIAAF--------- 892
Cdd:COG1196 506 FLEGVKAALLLAGLRglagavavligveaayeaaleaalaaalQNIVVEDDEVAAAAIEYLKAAKAGRATFlpldkirar 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 893 ---QRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLRSS 969
Cdd:COG1196 586 aalAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 970 QALNEDivrvSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQ 1049
Cdd:COG1196 666 SRRELL----AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
410
....*....|....*..
gi 568947408 1050 LDEAIEALDAAIEYKNE 1066
Cdd:COG1196 742 LEEEELLEEEALEELPE 758
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
700-1221 |
5.35e-07 |
|
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: 53.98 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 700 AAMASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQR---IRELEQEAERVRAELCEGQRQL----- 771
Cdd:pfam05557 35 KASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYleaLNKKLNEKESQLADAREVISCLknels 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 772 ---RELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLmRRQQGQLQRRLR 848
Cdd:pfam05557 115 elrRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQS-QEQDSEIVKNSK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 849 EETEQKRRLETEMNKRQHRVKELelkHEQQQKILKIKtEEIAAFQRKrrsgsngsvvsLEQQQKIEEQKKWLDQEMEKVL 928
Cdd:pfam05557 194 SELARIPELEKELERLREHNKHL---NENIENKLLLK-EEVEDLKRK-----------LEREEKYREEAATLELEKEKLE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 929 QQRRALEELG----------EELRKREVILAKKE-ALMQEKTGLES--KRLRSSQALNEDIVRV-SSRLEHLEKELSEKS 994
Cdd:pfam05557 259 QELQSWVKLAqdtglnlrspEDLSRRIEQLQQREiVLKEENSSLTSsaRQLEKARRELEQELAQyLKKIEDLNKKLKRHK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 995 GQLRQgsaqNQQQIRgeidTLRQEKDsLLKQRLE-IDSKLRqgsllspEEERTLFQLDEAIEALDAAIEYKNEAITCRQR 1073
Cdd:pfam05557 339 ALVRR----LQRRVL----LLTKERD-GYRAILEsYDKELT-------MSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQ 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1074 V---LRASASLLSQCEMnLMAKLSYLSSSETRALLCKYFDKVVTLREEqhqqqiaFSELEMQLEEQQRLVYWLEVALERQ 1150
Cdd:pfam05557 403 LsvaEEELGGYKQQAQT-LERELQALRQQESLADPSYSKEEVDSLRRK-------LETLELERQRLREQKNELEMELERR 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568947408 1151 rlemdrqlTLQQKEHEQNVQLLlqqgrdHLGEG-LADSKRQYEARIHALEKELGRHMWINQELKQKLSAGST 1221
Cdd:pfam05557 475 --------CLQGDYDPKKTKVL------HLSMNpAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLR 532
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
708-1178 |
5.66e-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: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 708 LAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQR---IRELEQEAERVRAElCEGQ--RQLRELEGREP--- 779
Cdd:pfam15921 383 LADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRnmeVQRLEALLKAMKSE-CQGQmeRQMAAIQGKNEsle 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 780 QDASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSlsaQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLET 859
Cdd:pfam15921 462 KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVS---DLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKN 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 860 EMNKRQHRVKE---LELKHEQQQKILKIKTEEIAAFQRkrRSGSNGSVVSLEQQQKIEEQKKWLDQEMEkvLQQRRALEE 936
Cdd:pfam15921 539 EGDHLRNVQTEceaLKLQMAEKDKVIEILRQQIENMTQ--LVGQHGRTAGAMQVEKAQLEKEINDRRLE--LQEFKILKD 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 937 lGEELRKREvILAKKEALMQEKTGL---ESKRLRS--------SQALNE------DIVRVSSRLEHLEKELSEKSGQLRQ 999
Cdd:pfam15921 615 -KKDAKIRE-LEARVSDLELEKVKLvnaGSERLRAvkdikqerDQLLNEvktsrnELNSLSEDYEVLKRNFRNKSEEMET 692
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1000 GSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDeaieALDAAIEYKNEAITC---RQRVLR 1076
Cdd:pfam15921 693 TTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQID----ALQSKIQFLEEAMTNankEKHFLK 768
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1077 ASASLLSQcemnlmaKLSYLSSSETRALlckyfdkvvtlreeqhqqqiafSELEMQLEEQQRL---VYWLEVALERQRLE 1153
Cdd:pfam15921 769 EEKNKLSQ-------ELSTVATEKNKMA----------------------GELEVLRSQERRLkekVANMEVALDKASLQ 819
|
490 500
....*....|....*....|....*
gi 568947408 1154 MDRQLTLQQKEHEQNVQLLLQQGRD 1178
Cdd:pfam15921 820 FAECQDIIQRQEQESVRLKLQHTLD 844
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
696-956 |
6.89e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.97 E-value: 6.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 696 RQAPAAMASEWRLAQAQQKIRELAINIRMKEELIGELVRTgkaAQALNRQHSQRIR--ELEQEAERVRA-ELCEGQRQLR 772
Cdd:pfam17380 314 RRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI---RQEERKRELERIRqeEIAMEISRMRElERLQMERQQK 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 773 ELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATE-RLVSLSAQSETRLQELERnVQLMRRQQGQLQRRLREET 851
Cdd:pfam17380 391 NERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEaRQREVRRLEEERAREMER-VRLEEQERQQQVERLRQQE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 852 EQKRRLETEMNKRQHRVKELElkhEQQQKILKIKTEE----IAAFQRKRR-----SGSNGSVVSLEQQQKIEEQKKWLDQ 922
Cdd:pfam17380 470 EERKRKKLELEKEKRDRKRAE---EQRRKILEKELEErkqaMIEEERKRKllekeMEERQKAIYEEERRREAEEERRKQQ 546
|
250 260 270
....*....|....*....|....*....|....
gi 568947408 923 EMEKVLQQRRALEELGEELRKREVILAKKEALMQ 956
Cdd:pfam17380 547 EMEERRRIQEQMRKATEERSRLEAMEREREMMRQ 580
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
705-1202 |
6.95e-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: 53.91 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 705 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGR--EPQDA 782
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRleELEEQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 783 SE--RSRLQEFRKRVAAAQSQVQVLKEKKQATE-RLVSLSAQSETRLQELERN-VQLMRRQQGQLQRRLREETEQKRRLE 858
Cdd:TIGR02168 381 LEtlRSKVAQLELQIASLNNEIERLEARLERLEdRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 859 TEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRR--SGSNGSVVSLEQQQK------------IEEQKKWlDQEM 924
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQEnlEGFSEGVKALLKNQSglsgilgvlselISVDEGY-EAAI 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 925 EKVL-------------QQRRALEELGEELRKREVILA---KKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLE---- 984
Cdd:TIGR02168 540 EAALggrlqavvvenlnAAKKAIAFLKQNELGRVTFLPldsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkals 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 985 ----------------HLEKELSE-------------KSGQLRQGSAQNQQQI---RGEIDTLRQEK------------- 1019
Cdd:TIGR02168 620 yllggvlvvddldnalELAKKLRPgyrivtldgdlvrPGGVITGGSAKTNSSIlerRREIEELEEKIeeleekiaeleka 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1020 -DSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEykneaiTCRQRVLRASASLLSQcEMNLMAKLSYLSS 1098
Cdd:TIGR02168 700 lAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE------QLEERIAQLSKELTEL-EAEIEELEERLEE 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1099 SETRALLCKyfDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDrQLTLQQKEHEQNVQLLLQQGRD 1178
Cdd:TIGR02168 773 AEEELAEAE--AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE-SLERRIAATERRLEDLEEQIEE 849
|
570 580
....*....|....*....|....*.
gi 568947408 1179 --HLGEGLADSKRQYEARIHALEKEL 1202
Cdd:TIGR02168 850 lsEDIESLAAEIEELEELIEELESEL 875
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
707-995 |
6.99e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 6.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 707 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGR--EPQDASE 784
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlnDLEARLS 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 785 RSRLQEFRKRVAAAQSQVQ----VLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETE 860
Cdd:TIGR02169 790 HSRIPEIQAELSKLEEEVSrieaRLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 861 MNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgSNGSVVSLEQQQK-IEEQKKWLDQEMEKVLQQRRALEELGE 939
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE-LEAQIEKKRKRLSeLKAKLEALEEELSEIEDPKGEDEEIPE 948
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 568947408 940 ELRKREVILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSG 995
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
742-1205 |
8.66e-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: 53.82 E-value: 8.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 742 LNRQHS--QRIRELEQEAERVRAE---LCEGQRQLRELEGR-EPQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATERL 815
Cdd:TIGR00618 371 SCQQHTltQHIHTLQQQKTTLTQKlqsLCKELDILQREQATiDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCT 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 816 VSLSAQSETRLQELERNVQlmrrqqgqlqrrlrEETEQKRRLETeMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRK 895
Cdd:TIGR00618 451 AQCEKLEKIHLQESAQSLK--------------EREQQLQTKEQ-IHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNP 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 896 RRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQrraleelGEELRKREVILAKKEALMQEKTGLESKRLRSSQALNED 975
Cdd:TIGR00618 516 ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQ-------LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPN 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 976 IVRVSSRLEHLEKELSEKSGQLRQgsAQNQQQIRGEIDTLRQEKDSLLKQrleIDSKLRQGSLLSPEEERTLFQLDEAIE 1055
Cdd:TIGR00618 589 LQNITVRLQDLTEKLSEAEDMLAC--EQHALLRKLQPEQDLQDVRLHLQQ---CSQELALKLTALHALQLTLTQERVREH 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1056 ALdAAIEYKNEAITCRQRVLRASASLLSQCEMN---LMAKLSYLSSSETrallckyfdKVVTLREEQHQQQIAFSELEMQ 1132
Cdd:TIGR00618 664 AL-SIRVLPKELLASRQLALQKMQSEKEQLTYWkemLAQCQTLLRELET---------HIEEYDREFNEIENASSSLGSD 733
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568947408 1133 LEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNVQLLLQQGRD--HLGEGLADSKRQYEARIHALEKELGRH 1205
Cdd:TIGR00618 734 LAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAElsHLAAEIQFFNRLREEDTHLLKTLEAEI 808
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
748-1058 |
1.02e-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: 53.44 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 748 QRIRELEQEAE---RVRAELCEGQRQLRELEGREpqdaSERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSET 824
Cdd:pfam02463 173 EALKKLIEETEnlaELIIDLEELKLQELKLKEQA----KKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 825 RLQELERNVQLMRRQqgqlqrrlrEETEQKRRLETEMNKRQHRVKELELKheqqQKILKIKTEEIAAFQRKRRSGSNGSV 904
Cdd:pfam02463 249 EQEEIESSKQEIEKE---------EEKLAQVLKENKEEEKEKKLQEEELK----LLAKEEEELKSELLKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 905 VSLEQ-------------QQKIEEQKKWLD------QEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTG----- 960
Cdd:pfam02463 316 LKESEkekkkaekelkkeKEEIEELEKELKeleikrEAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAklkee 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 961 LESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSG-----QLRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQ 1035
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEileeeEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
330 340
....*....|....*....|...
gi 568947408 1036 GSLLSPEEERTLFQLDEAIEALD 1058
Cdd:pfam02463 476 ETQLVKLQEQLELLLSRQKLEER 498
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
602-1192 |
1.04e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 602 KAEVLAQADKLRSASST----TSEEEGEEEEEEEEEEEEPPRRTLYLRR----NGISNWSQRAGLSPGSPPDRKGPEVCP 673
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDArkaeAARKAEEERKAEEARKAEDAKKAEAVKKaeeaKKDAEEAKKAEEERNNEEIRKFEEARM 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 674 EEPAAAIPAPQAVGSGKVPVQTRQAPAAMASEWRLAQAQQKIREL---AINIRMKEELIGELVRTGKAAQALNRQHSQR- 749
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAkkkAEEAKKADEAKKKAEEAKKKADAAKKKAEEAk 1342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 750 ----IRELEQEAERVRAELCEGQRQLRELEGREP--------QDASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVS 817
Cdd:PTZ00121 1343 kaaeAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkkadaakKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE 1422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 818 LSAQSE--TRLQELERNVQlmrrqQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKI----LKIKTEEI-- 889
Cdd:PTZ00121 1423 AKKKAEekKKADEAKKKAE-----EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkadeAKKKAEEAkk 1497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 890 AAFQRKRRSGSNGSVVSL---EQQQKIEEQKKWLD----QEMEKVLQQRRAlEEL--GEELRKREVILAKKEALMQEKTG 960
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAkkaEEAKKADEAKKAEEakkaDEAKKAEEKKKA-DELkkAEELKKAEEKKKAEEAKKAEEDK 1576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 961 LESKRlRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQgsAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLS 1040
Cdd:PTZ00121 1577 NMALR-KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK--AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1041 PEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNLMAKlsylsssETRALLCKYFDKVVTLREEQH 1120
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE-------ELKKKEAEEKKKAEELKKAEE 1726
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568947408 1121 QQQIAFSELEMQLEEQQRlvywlevALERQRLEMDRQLTLQQ--KEHEQNVQLLLQQGRDHLGEGL--ADSKRQYE 1192
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKK-------KAEEAKKDEEEKKKIAHlkKEEEKKAEEIRKEKEAVIEEELdeEDEKRRME 1795
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
749-1218 |
1.12e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 749 RIRELEQEAERVraelcegQRQLRELEGREPQDASERSRLQEFRKRVAAaqsqvqvLKEKKQATERLVSLSAQSETRLQE 828
Cdd:PRK03918 194 LIKEKEKELEEV-------LREINEISSELPELREELEKLEKEVKELEE-------LKEEIEELEKELESLEGSKRKLEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 829 LERNVQlmrrqqgqlqrrlrEETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEeiaafqrkrrsgsngsvvSLE 908
Cdd:PRK03918 260 KIRELE--------------ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEE------------------YLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 909 QQQKIEEqkkwldqEMEKVLQQRRALEELGEELRKREvilAKKEALMQEKTGLESK--RLRSSQALNEDIVRVSSRLEHL 986
Cdd:PRK03918 308 ELREIEK-------RLSRLEEEINGIEERIKELEEKE---ERLEELKKKLKELEKRleELEERHELYEEAKAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 987 EKELSEKSgqlrqgsaqnQQQIRGEIDTLRQEKDSLLKQRLEIDSKLrqGSLLSPEEERtlfqlDEAIEALDAAieyKNE 1066
Cdd:PRK03918 378 KKRLTGLT----------PEKLEKELEELEKAKEEIEEEISKITARI--GELKKEIKEL-----KKAIEELKKA---KGK 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1067 AITCRqrvlrasASLLSQCEMNLMAKLSyLSSSETRALLCKYFDKVVTLREEqhqqqiaFSELEMQLEEQQRLVYWLEVA 1146
Cdd:PRK03918 438 CPVCG-------RELTEEHRKELLEEYT-AELKRIEKELKEIEEKERKLRKE-------LRELEKVLKKESELIKLKELA 502
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568947408 1147 LERQRLEmdrqltlqQKEHEQNVQLLLQQGRDHlgEGLADSKRQYEARIHALEKELGRhmwiNQELKQKLSA 1218
Cdd:PRK03918 503 EQLKELE--------EKLKKYNLEELEKKAEEY--EKLKEKLIKLKGEIKSLKKELEK----LEELKKKLAE 560
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
721-1048 |
1.30e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.84 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 721 NIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELegrepqdaseRSRLQEFRKRVAAAQS 800
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKEL----------REEAQELREKRDELNE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 801 QVQVLKEKKQAterlvsLSAQSETRLQELERnvqlmrrqqgqlqrrLREETEQKRRLETEMNKRQHRVKELELKheQQQK 880
Cdd:COG1340 72 KVKELKEERDE------LNEKLNELREELDE---------------LRKELAELNKAGGSIDKLRKEIERLEWR--QQTE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 881 ILKIKtEEIAAFQRKRRSGSngsvvSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRK-REVILAKKEALMQEKT 959
Cdd:COG1340 129 VLSPE-EEKELVEKIKELEK-----ELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKElAEEAQELHEEMIELYK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 960 GLESKRlRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRqgsaQNQQQIRGEIDTLR-----QEKDSLLKQRLEIDSKLR 1034
Cdd:COG1340 203 EADELR-KEADELHKEIVEAQEKADELHEEIIELQKELR----ELRKELKKLRKKQRalkreKEKEELEEKAEEIFEKLK 277
|
330
....*....|....
gi 568947408 1035 QGSLLSPEEERTLF 1048
Cdd:COG1340 278 KGEKLTTEELKLLQ 291
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
708-1035 |
1.43e-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: 53.05 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 708 LAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQE----AERVRAELCEGQRQLRELE---GREPQ 780
Cdd:pfam02463 671 LTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAeellADRVQEAQDKINEELKLLKqkiDEEEE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 781 DASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETE 860
Cdd:pfam02463 751 EEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKI 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 861 MNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKR---RSGSNGSVVSLEQQQKIEEQKKWLDQEME-KVLQQRRALEE 936
Cdd:pfam02463 831 KEEELEELALELKEEQKLEKLAEEELERLEEEITKEellQELLLKEEELEEQKLKDELESKEEKEKEEkKELEEESQKLN 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 937 LGEELRKREVILAKKEALMQEKTGLESKRLRSSQALNED---------IVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQ 1007
Cdd:pfam02463 911 LLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEkeennkeeeEERNKRLLLAKEELGKVNLMAIEEFEEKEERY 990
|
330 340 350
....*....|....*....|....*....|
gi 568947408 1008 --IRGEIDTLRQEKDSLLKQRLEIDSKLRQ 1035
Cdd:pfam02463 991 nkDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
728-1167 |
1.59e-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: 52.80 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 728 LIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELcegQRQLRELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKE 807
Cdd:pfam05483 350 VVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMEL---QKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQ 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 808 KKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKEL------------ELKH 875
Cdd:pfam05483 427 FEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELtahcdklllenkELTQ 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 876 EQQQKILKIKTEEIAAFQRKRRSGSngsvvSLEQQQKIEEQKKWLDQEMEKVlqqRRALEELGEELRKReviLAKKEALM 955
Cdd:pfam05483 507 EASDMTLELKKHQEDIINCKKQEER-----MLKQIENLEEKEMNLRDELESV---REEFIQKGDEVKCK---LDKSEENA 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 956 QEKTGLESKRLRSSQALNEDIVRVSSRLEHLEK---ELSEKSGQL-RQGSAQNQQQIRGEIDTLRQEKD-SLLKQRLE-- 1028
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKnieELHQENKALkKKGSAENKQLNAYEIKVNKLELElASAKQKFEei 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1029 IDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEA-ITCRQRVLRASAsllsqcemnLMAKLSYlsssetrallck 1107
Cdd:pfam05483 656 IDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIdKRCQHKIAEMVA---------LMEKHKH------------ 714
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568947408 1108 YFDKVVtlrEEQHQQQIAFSELEmqlEEQQRLVYWLEVALERQRLEM---DRQLTLQQKEHEQ 1167
Cdd:pfam05483 715 QYDKII---EERDSELGLYKNKE---QEQSSAKAALEIELSNIKAELlslKKQLEIEKEEKEK 771
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
734-1034 |
1.78e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.53 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 734 RTGKAAQALNRQHSqRIRELEQEAERVRAELCEGQRQLrELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATE 813
Cdd:pfam12128 605 RLDKAEEALQSARE-KQAAAEEQLVQANGELEKASREE-TFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANE 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 814 RLVSLSAQsetrLQELERNVQLMrrqqgqlqrrLREETEQKRRLETEMNKrqhrvKELELKHEQQQKILKIKtEEIAAfq 893
Cdd:pfam12128 683 RLNSLEAQ----LKQLDKKHQAW----------LEEQKEQKREARTEKQA-----YWQVVEGALDAQLALLK-AAIAA-- 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 894 rkRRSGSNGSVVSLEQQQKIEEQKKWLDQE-MEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLrssqal 972
Cdd:pfam12128 741 --RRSGAKAELKALETWYKRDLASLGVDPDvIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRL------ 812
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568947408 973 nedivrvSSRLEHLEKELSEKSGQLrqgsAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLR 1034
Cdd:pfam12128 813 -------ATQLSNIERAISELQQQL----ARLIADTKLRRAKLEMERKASEKQQVRLSENLR 863
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
708-1028 |
2.36e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.43 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 708 LAQAQQKIRELAINIRMKEELIGELVRTGkaaqalNRQHSQRIRELEQEAERVRAELCEGQRQLRElegrepqdasersR 787
Cdd:pfam15921 283 LTEKASSARSQANSIQSQLEIIQEQARNQ------NSMYMRQLSDLESTVSQLRSELREAKRMYED-------------K 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 788 LQEFRKRVAAAQSQvqvLKEKKQATERLVSLSAQSETRLQELERNVQlmrrqqgqlqrrlreETEQKRRLETEMNKR--- 864
Cdd:pfam15921 344 IEELEKQLVLANSE---LTEARTERDQFSQESGNLDDQLQKLLADLH---------------KREKELSLEKEQNKRlwd 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 865 ---------QHRVKELELKHEQQQK---ILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLqqrr 932
Cdd:pfam15921 406 rdtgnsitiDHLRRELDDRNMEVQRleaLLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVV---- 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 933 aleelgEELRKREVILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELseksgQLRQGSAQNQQQIRGEI 1012
Cdd:pfam15921 482 ------EELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQEL-----QHLKNEGDHLRNVQTEC 550
|
330 340
....*....|....*....|..
gi 568947408 1013 DTLR---QEKD---SLLKQRLE 1028
Cdd:pfam15921 551 EALKlqmAEKDkviEILRQQIE 572
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
695-1069 |
2.72e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.89 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 695 TRQAPAAMASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKA-AQALNRQHSQRI----RELEQEAERVRAELCEG-Q 768
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVvLARLLELQEEPCplcgSCIHPNPARQDIDNPGPlT 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 769 RQLRELEGREPQDASE----RSRLQEFRKRVAAAQSQVQVLKEKKQA-TERLVSLSAQSETRLQELERNVQLMRRQQGQL 843
Cdd:TIGR00618 528 RRMQRGEQTYAQLETSeedvYHQLTSERKQRASLKEQMQEIQQSFSIlTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 844 QRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQ------------QQ 911
Cdd:TIGR00618 608 DMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKEllasrqlalqkmQS 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 912 KIE---------EQKKWLDQEMEKVL--------QQRRALEELGEELRKREVILAK--KEALMQEKTGLESKRL---RSS 969
Cdd:TIGR00618 688 EKEqltywkemlAQCQTLLRELETHIeeydrefnEIENASSSLGSDLAAREDALNQslKELMHQARTVLKARTEahfNNN 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 970 QALNEDIVRvSSRLEHLE-------KELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPE 1042
Cdd:TIGR00618 768 EEVTAALQT-GAELSHLAaeiqffnRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGE 846
|
410 420
....*....|....*....|....*..
gi 568947408 1043 EERTLFQLDEAIEALDAAIEYKNEAIT 1069
Cdd:TIGR00618 847 ITHQLLKYEECSKQLAQLTQEQAKIIQ 873
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
725-1059 |
7.15e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 7.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 725 KEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERSR-----------LQEFRK 793
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDElrereaeleatLRTARE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 794 RVAAAQ------------------SQVQVLKEKKQATERLVSLSAQSETRLQELERNVqlmrrqqgqlqrrlrEETEQKR 855
Cdd:PRK02224 441 RVEEAEalleagkcpecgqpvegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERL---------------ERAEDLV 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 856 RLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALE 935
Cdd:PRK02224 506 EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELK 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 936 ELGEELRKREVILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLE---HLEKELS----EKSGQLRQGSAQNQQQI 1008
Cdd:PRK02224 586 ERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRErkrELEAEFDeariEEAREDKERAEEYLEQV 665
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 568947408 1009 RGEIDTLRQEKDSLLKQRLEIDSKLRQgsLLSPEEERTlfQLDEAIEALDA 1059
Cdd:PRK02224 666 EEKLDELREERDDLQAEIGAVENELEE--LEELRERRE--ALENRVEALEA 712
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
703-944 |
8.07e-06 |
|
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: 50.44 E-value: 8.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 703 ASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELE------- 775
Cdd:TIGR02168 800 ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELEseleall 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 776 ----GREPQDASERSRLQEFRKRVAAAQSQVQvlkEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREET 851
Cdd:TIGR02168 880 neraSLEEALALLRSELEELSEELRELESKRS---ELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEA 956
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 852 EQK-RRLETEMNKRQHRVKELElkheqqqkilkiktEEIAAFqrkrrsgsnGSV--VSLEQQQKIEEQKKWLDQEMEKVL 928
Cdd:TIGR02168 957 EALeNKIEDDEEEARRRLKRLE--------------NKIKEL---------GPVnlAAIEEYEELKERYDFLTAQKEDLT 1013
|
250
....*....|....*.
gi 568947408 929 QQRRALEELGEELRKR 944
Cdd:TIGR02168 1014 EAKETLEEAIEEIDRE 1029
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
712-1184 |
9.08e-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: 50.36 E-value: 9.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 712 QQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRE--LEQEAERVRAELCEGQR--QLRELEGREPQDASERSR 787
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEeeKEKKLQEEELKLLAKEEeeLKSELLKLERRKVDDEEK 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 788 LQEFRKRVAAAQSQVQvlKEKKQATERLVSLSAQSETRLQELERNVQLMRRQqgqlqrrlrEETEQKR-------RLETE 860
Cdd:pfam02463 316 LKESEKEKKKAEKELK--KEKEEIEELEKELKELEIKREAEEEEEEELEKLQ---------EKLEQLEeellakkKLESE 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 861 MNKRQHRVKE--LELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELG 938
Cdd:pfam02463 385 RLSSAAKLKEeeLELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 939 EELRKREVILAKKE---ALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEID-- 1013
Cdd:pfam02463 465 LELKKSEDLLKETQlvkLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKva 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1014 --TLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCR-----QRVLRASASLLSQCE 1086
Cdd:pfam02463 545 isTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNlaqldKATLEADEDDKRAKV 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1087 MNLMAKLSYLSSSETRALlckyfDKVVTLREEQHQQQIAFSELEMQ---LEEQQRLVYWLEVALERQRLEMDRQLTLQQK 1163
Cdd:pfam02463 625 VEGILKDTELTKLKESAK-----AKESGLRKGVSLEEGLAEKSEVKaslSELTKELLEIQELQEKAESELAKEEILRRQL 699
|
490 500
....*....|....*....|.
gi 568947408 1164 EHEQNVQLLLQQGRDHLGEGL 1184
Cdd:pfam02463 700 EIKKKEQREKEELKKLKLEAE 720
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
778-1035 |
9.52e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 778 EPQDASER-SRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQK-R 855
Cdd:COG4913 219 EEPDTFEAaDALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAElE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 856 RLETEMNKRQHRVKELELKHEQQQkilkiktEEIAAFQRKRRSgsngsvVSLEQQQKIEEQKKWLDQEMEKVLQQRRALE 935
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALR-------EELDELEAQIRG------NGGDRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 936 ELGEELrkrevilakKEALMQEKTGLESKRLRSSQALNEdivrVSSRLEHLEKELSEKSGQLRQGsaqnqqqiRGEIDTL 1015
Cdd:COG4913 366 ALLAAL---------GLPLPASAEEFAALRAEAAALLEA----LEEELEALEEALAEAEAALRDL--------RRELREL 424
|
250 260
....*....|....*....|
gi 568947408 1016 RQEKDSLLKQRLEIDSKLRQ 1035
Cdd:COG4913 425 EAEIASLERRKSNIPARLLA 444
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
835-1067 |
9.96e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 9.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 835 LMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRsgsngsvvslEQQQKIE 914
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR----------ALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 915 EQKKWLDQEMEKVLQQRRALEELGEELRKREVILAK-------KEALMQEKTGLESKRLRSSQALN-------EDIVRVS 980
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAELLRALYRlgrqpplALLLSPEDFLDAVRRLQYLKYLAparreqaEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 981 SRLEHLEKELSEKSGQLRQGSAQNQQQiRGEIDTLRQEKDSLLKQrLEIDSKLRQGSLLSPEEERTlfQLDEAIEALDAA 1060
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEE-RAALEALKAERQKLLAR-LEKELAELAAELAELQQEAE--ELEALIARLEAE 235
|
....*..
gi 568947408 1061 IEYKNEA 1067
Cdd:COG4942 236 AAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
922-1062 |
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 568947408 922 QEMEKVLQQRRALE---ELGEELRKREVILAKKEALM--------QEKTGLESKRLRSSQA----LNEDIVRVSSRLEHL 986
Cdd:COG4913 242 EALEDAREQIELLEpirELAERYAAARERLAELEYLRaalrlwfaQRRLELLEAELEELRAelarLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568947408 987 EKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIE 1062
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE 397
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
707-834 |
3.47e-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: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 707 RLAQAQQKIRELAINIRMKEELIGELVRTGkAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERS 786
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQSP-VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ 312
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568947408 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 ... |
852-1218 |
4.31e-05 |
|
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: 48.09 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 852 EQKRRLETEMNKRQhrvKELELKHEQQQKILK--IKTEEIAAFQRKRRSGSNGSVVSLEQQQKI-EEQKKWLDQEMEKVL 928
Cdd:TIGR04523 117 EQKNKLEVELNKLE---KQKKENKKNIDKFLTeiKKKEKELEKLNNKYNDLKKQKEELENELNLlEKEKLNIQKNIDKIK 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 929 QQRRALEEL-----------------GEELRKREVILAK-KEALMQEKTGLESKRLRSSQALNEdivrVSSRLEHLEKEL 990
Cdd:TIGR04523 194 NKLLKLELLlsnlkkkiqknkslesqISELKKQNNQLKDnIEKKQQEINEKTTEISNTQTQLNQ----LKDEQNKIKKQL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 991 SEKSGQLRQGSAQ-----NQ-QQIRGEIDTLRQEK----DSLLKQRLE-IDSKLRQGSLLSPEEERTLFQLDEAIEALDA 1059
Cdd:TIGR04523 270 SEKQKELEQNNKKikeleKQlNQLKSEISDLNNQKeqdwNKELKSELKnQEKKLEEIQNQISQNNKIISQLNEQISQLKK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1060 AIEYKNEAITCRQRVLRASASLLSQCEMNlmaKLSYLSSSetrallckyfdkvvtlreEQHQQQIafSELEMQLEEQqrl 1139
Cdd:TIGR04523 350 ELTNSESENSEKQRELEEKQNEIEKLKKE---NQSYKQEI------------------KNLESQI--NDLESKIQNQ--- 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1140 vywlevalERQRLEMDRQLTLQQKEH---EQNVQLLLQQGRDhlgegLADSKRQYEARIHALEKELGRHMWINQELKQKL 1216
Cdd:TIGR04523 404 --------EKLNQQKDEQIKKLQQEKellEKEIERLKETIIK-----NNSEIKDLTNQDSVKELIIKNLDNTRESLETQL 470
|
..
gi 568947408 1217 SA 1218
Cdd:TIGR04523 471 KV 472
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
744-1073 |
4.47e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 48.03 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 744 RQHSQRIRELEQEAERVRAELCEGQRQLRELEgrepqDASERSRLQEFRKRVAAAQSQVQVLKEKKQATErlvslsaqse 823
Cdd:COG5185 271 GENAESSKRLNENANNLIKQFENTKEKIAEYT-----KSIDIKKATESLEEQLAAAEAEQELEESKRETE---------- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 824 TRLQELERNVQLMRRQQGQLQRRLREETEQ------KRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRR 897
Cdd:COG5185 336 TGIQNLTAEIEQGQESLTENLEAIKEEIENivgeveLSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTL 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 898 SgsngsvvslEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEEL-RKREVILAKKEALMQEKTGLESKRLRSSqalNEDI 976
Cdd:COG5185 416 K---------AADRQIEELQRQIEQATSSNEEVSKLLNELISELnKVMREADEESQSRLEEAYDEINRSVRSK---KEDL 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 977 vrvSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLlkqrleiDSKLRQGSLLSPEEERTLFQLDEAIEA 1056
Cdd:COG5185 484 ---NEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESL-------KDFMRARGYAHILALENLIPASELIQA 553
|
330
....*....|....*..
gi 568947408 1057 LDAAIEYKNEAITCRQR 1073
Cdd:COG5185 554 SNAKTDGQAANLRTAVI 570
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
703-956 |
5.36e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.81 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 703 ASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDA 782
Cdd:pfam15921 552 ALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 783 SERSRLqefrkrVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETE----QKRRLE 858
Cdd:pfam15921 632 LEKVKL------VNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNklkmQLKSAQ 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 859 TEMNKRQHRVKELELK--HEQQ-----QKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQR 931
Cdd:pfam15921 706 SELEQTRNTLKSMEGSdgHAMKvamgmQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEK 785
|
250 260
....*....|....*....|....*
gi 568947408 932 RALEELGEELRKREVILAKKEALMQ 956
Cdd:pfam15921 786 NKMAGELEVLRSQERRLKEKVANME 810
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
709-1182 |
5.38e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.73 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 709 AQAQQKIRElaINIRMKEELIGELVRTGKAAQALNRQHSQRiRELEQEAERVR------AELCEGQRQLR-ELEGREPQD 781
Cdd:TIGR00606 545 MDKDEQIRK--IKSRHSDELTSLLGYFPNKKQLEDWLHSKS-KEINQTRDRLAklnkelASLEQNKNHINnELESKEEQL 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 782 AS-------------ERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSA--------------QSETRLQELERNVQ 834
Cdd:TIGR00606 622 SSyedklfdvcgsqdEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTdenqsccpvcqrvfQTEAELQEFISDLQ 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 835 LMRRQQgqlqrrlreETEQKRrLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVvslEQQQKIE 914
Cdd:TIGR00606 702 SKLRLA---------PDKLKS-TESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ---RLKNDIE 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 915 EQKKWL-----DQEMEKVLQQR-RALEELGEELRKREVILAKKEALMQEKTGleskrLRSSQALNEdivRVSSRLEHLEK 988
Cdd:TIGR00606 769 EQETLLgtimpEEESAKVCLTDvTIMERFQMELKDVERKIAQQAAKLQGSDL-----DRTVQQVNQ---EKQEKQHELDT 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 989 ELSEksGQLRQGSAQNQQQirgEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAI 1068
Cdd:TIGR00606 841 VVSK--IELNRKLIQDQQE---QIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLE 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1069 TCRQRVLRASASLLSQCEM-NLMAKLSYLSSSETRALLCKY----FDKVVTLREEQ-HQQQIAFSELEMQLEEQQRLVYW 1142
Cdd:TIGR00606 916 TFLEKDQQEKEELISSKETsNKKAQDKVNDIKEKVKNIHGYmkdiENKIQDGKDDYlKQKETELNTVNAQLEECEKHQEK 995
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 568947408 1143 LEVALERQRLEMDRQltlQQKEHEQNVQLLLQQGRDHLGE 1182
Cdd:TIGR00606 996 INEDMRLMRQDIDTQ---KIQERWLQDNLTLRKRENELKE 1032
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
725-1067 |
1.12e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 725 KEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAelCEGQRQLRELEGREPQDASERSRLQEFRKRVAAAQsqvqv 804
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARK--AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAK----- 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 805 lkeKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETemnkrQHRVKELELKHEQQQKILKI 884
Cdd:PTZ00121 1177 ---KAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEA-----VKKAEEAKKDAEEAKKAEEE 1248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 885 KT-EEIAAFQRKRRSgsngSVVSLEQQQKIEEQKKwlDQEMEKVLQQRRAlEELGEELRKREVILAKKEAlMQEKTGLES 963
Cdd:PTZ00121 1249 RNnEEIRKFEEARMA----HFARRQAAIKAEEARK--ADELKKAEEKKKA-DEAKKAEEKKKADEAKKKA-EEAKKADEA 1320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 964 KRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQiRGEIDTLRQE----KDSLLKQRLEIDSKLRQGSLL 1039
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE-KAEAAEKKKEeakkKADAAKKKAEEKKKADEAKKK 1399
|
330 340
....*....|....*....|....*...
gi 568947408 1040 SPEEERTLFQLDEAIEALDAAIEYKNEA 1067
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEAKKKA 1427
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
602-1171 |
1.42e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 602 KAEVLAQADKLRSASSTTSEEEGEEEEEEEE----EEEEPPRRTLYLRRNGIsnwSQRAGLSPGSPPDRKGPEVCPEEPA 677
Cdd:PTZ00121 1117 AEEAKKKAEDARKAEEARKAEDARKAEEARKaedaKRVEIARKAEDARKAEE---ARKAEDAKKAEAARKAEEVRKAEEL 1193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 678 AAIPAPQAVGSGKVPVQTRQAPAA-MASEWRLAQAQQKIREL---------AINIRMKEEL-------IGELVRTGKAAQ 740
Cdd:PTZ00121 1194 RKAEDARKAEAARKAEEERKAEEArKAEDAKKAEAVKKAEEAkkdaeeakkAEEERNNEEIrkfeearMAHFARRQAAIK 1273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 741 ALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGR--EPQDASE-RSRLQEFRKRVAAAQSQVQVLKEKKQATERLVS 817
Cdd:PTZ00121 1274 AEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKaeEAKKADEaKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 818 LSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLEtEMNKRQHRVK----ELELKHEQQQKI--LKIKTEEIAA 891
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD-EAKKKAEEDKkkadELKKAAAAKKKAdeAKKKAEEKKK 1432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 892 FQRKRRSGSNGSVVSlEQQQKIEEQKKwlDQEMEKVLQQRRALEEL---GEELRKREVilAKKEALMQEKTGLESKRLRS 968
Cdd:PTZ00121 1433 ADEAKKKAEEAKKAD-EAKKKAEEAKK--AEEAKKKAEEAKKADEAkkkAEEAKKADE--AKKKAEEAKKKADEAKKAAE 1507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 969 SQALNEDIVRV--SSRLEHLEK-ELSEKSGQLRQGSAQNQQQIRGEIDTLR--QEKDSLLKQRLEIDSK---LRQGSLLS 1040
Cdd:PTZ00121 1508 AKKKADEAKKAeeAKKADEAKKaEEAKKADEAKKAEEKKKADELKKAEELKkaEEKKKAEEAKKAEEDKnmaLRKAEEAK 1587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1041 PEEER---TLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEmnlmaKLSYLSSSETRallckyfdKVVTLRE 1117
Cdd:PTZ00121 1588 KAEEArieEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE-----QLKKKEAEEKK--------KAEELKK 1654
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 568947408 1118 EQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRlEMDRQLTLQQKEHEQNVQL 1171
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK-KAAEALKKEAEEAKKAEEL 1707
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
708-1056 |
2.15e-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: 45.94 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 708 LAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGR------EPQD 781
Cdd:pfam01576 168 LAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQlakkeeELQA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 782 A-----SERSRLQEFRKRVAAAQSQVQVLKE--------KKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLR 848
Cdd:pfam01576 248 AlarleEETAQKNNALKKIRELEAQISELQEdleseraaRNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQ 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 849 EETEQKRRLETEMNKRQHRVKELELKHEQQQKILkikTEEIAAFQRKRrsgsngsvVSLEQ-QQKIEEQKKWLDQEMeKV 927
Cdd:pfam01576 328 EVTELKKALEEETRSHEAQLQEMRQKHTQALEEL---TEQLEQAKRNK--------ANLEKaKQALESENAELQAEL-RT 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 928 LQQRRALEElgeelRKREvilaKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSE---KSGQLRQGSAQN 1004
Cdd:pfam01576 396 LQQAKQDSE-----HKRK----KLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEaegKNIKLSKDVSSL 466
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 568947408 1005 QQQIRGEIDTLRQEKdsllKQRLEIDSKLRQgsllsPEEERT--LFQLDEAIEA 1056
Cdd:pfam01576 467 ESQLQDTQELLQEET----RQKLNLSTRLRQ-----LEDERNslQEQLEEEEEA 511
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
754-1166 |
2.32e-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: 45.94 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 754 EQEAERVRAELCEGQRQLRELEGREPQDASERSRLQEfrkrvaAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNV 833
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQE------QLQAETELCAEAEEMRARLAARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 834 QlmrrqqgqlqrrlrEETEQKRRLETEMNKRQHRVKELELKHEqqqkilkiktEEIAAFQRKRRSGsngsvVSLEQQ-QK 912
Cdd:pfam01576 85 E--------------EEEERSQQLQNEKKKMQQHIQDLEEQLD----------EEEAARQKLQLEK-----VTTEAKiKK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 913 IEEQKKWLDQEMEKVLQQRRALEE--------LGEELRKR-----------------EVILAKKEALMQEKTGLESKRLR 967
Cdd:pfam01576 136 LEEDILLLEDQNSKLSKERKLLEEriseftsnLAEEEEKAkslsklknkheamisdlEERLKKEEKGRQELEKAKRKLEG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 968 SSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDsLLKQRLEIDSKLRQGSLLSPEEERTL 1047
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE-LEAQISELQEDLESERAARNKAEKQR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1048 FQLDEAIEALDAAIEYKNEAiTCRQRVLRasasllSQCEMNLmAKLSYLSSSETRAllckyFDKVVTLREEQHQQqiAFS 1127
Cdd:pfam01576 295 RDLGEELEALKTELEDTLDT-TAAQQELR------SKREQEV-TELKKALEEETRS-----HEAQLQEMRQKHTQ--ALE 359
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 568947408 1128 ELEMQLEEQQRLVYWLE---VALERQRLEMDRQL-TLQQKEHE 1166
Cdd:pfam01576 360 ELTEQLEQAKRNKANLEkakQALESENAELQAELrTLQQAKQD 402
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
745-1081 |
2.49e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 745 QHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERSR---LQEFRKRVAAAQSQVQ-VLKEKKQATERLVSLSA 820
Cdd:PRK11281 77 RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLStlsLRQLESRLAQTLDQLQnAQNDLAEYNSQLVSLQT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 821 QSE----------TRLQELerNVQLMRRQQGQLQRRLreetEQKRRLETEMnkrqhrvKELELKHEQQQKILKIKTEEIA 890
Cdd:PRK11281 157 QPEraqaalyansQRLQQI--RNLLKGGKVGGKALRP----SQRVLLQAEQ-------ALLNAQNDLQRKSLEGNTQLQD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 891 AFQrKRRSGSNgsvvslEQQQKIEEQKKWLdQEMekVLQQRRAL-EELGEELRKREVI-------LAKKEalMQEKTGLE 962
Cdd:PRK11281 224 LLQ-KQRDYLT------ARIQRLEHQLQLL-QEA--INSKRLTLsEKTVQEAQSQDEAariqanpLVAQE--LEINLQLS 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 963 SKRLRSSQALNE---DIVRVSSRLEHL---EKELSEKSGQLrQGSAQ-----NQQQ------------------IRGEID 1013
Cdd:PRK11281 292 QRLLKATEKLNTltqQNLRVKNWLDRLtqsERNIKEQISVL-KGSLLlsrilYQQQqalpsadliegladriadLRLEQF 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1014 TLRQEKDSLLKQRLEIDSKLR-QGSLLSPEEERTLFQ--------LDEAIEALDAAIeykNEAITC---RQRVLRASASL 1081
Cdd:PRK11281 371 EINQQRDALFQPDAYIDKLEAgHKSEVTDEVRDALLQllderrelLDQLNKQLNNQL---NLAINLqlnQQQLLSVSDSL 447
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
850-992 |
2.67e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 850 ETEQKRRLETEMNKRQHRVKELELkhEQQQKILKIKTEEIAAFQRKRRSgsngsvvsLEQQQKIEEQKK-WLDQEMEKVL 928
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEALL--EAKEEIHKLRNEFEKELRERRNE--------LQKLEKRLLQKEeNLDRKLELLE 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568947408 929 QQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLRSSQALNEDIVRvSSRLEHLEKELSE 992
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAK-EILLEKVEEEARH 169
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
849-1067 |
3.04e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 849 EETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKR--RSGSNGSVVSLEQQ-QKIEE--QKKWLDQE 923
Cdd:COG1340 54 ELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELaeLNKAGGSIDKLRKEiERLEWrqQTEVLSPE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 924 MEKVLQQRraLEELGEELRKREVILAKKEALMQEKTGLESKRLRSSQaLNEDIvrvssrlehleKELSEKSGQLRqgsaQ 1003
Cdd:COG1340 134 EEKELVEK--IKELEKELEKAKKALEKNEKLKELRAELKELRKEAEE-IHKKI-----------KELAEEAQELH----E 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568947408 1004 NQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQgslLSPEEERTLFQLDEAIEALDAAIEYKNEA 1067
Cdd:COG1340 196 EMIELYKEADELRKEADELHKEIVEAQEKADE---LHEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
709-1029 |
3.33e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.89 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 709 AQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERSRL 788
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 789 QEFRKRVAAAQsqvqvlkekkqaterlvslsAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRV 868
Cdd:pfam07888 114 SEEKDALLAQR--------------------AAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 869 KELELKHEQQQKILKIKTEEiaaFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVIL 948
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKE---FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 949 AKKEALMQEKTGLESKRLRSSQALNEdivrvsSRLE--HLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQR 1026
Cdd:pfam07888 251 RKVEGLGEELSSMAAQRDRTQAELHQ------ARLQaaQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLS 324
|
...
gi 568947408 1027 LEI 1029
Cdd:pfam07888 325 AEL 327
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
755-1202 |
3.42e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 755 QEAERVRAELCEGQRQLR-ELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATERlVSLSAQSETRLQELERNv 833
Cdd:pfam01576 422 SESERQRAELAEKLSKLQsELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETR-QKLNLSTRLRQLEDERN- 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 834 qlmrrqqgQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKI 913
Cdd:pfam01576 500 --------SLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 914 EEQKKWLDQEMEKVL----QQRRALEELGEELRKREVILAKKEALmqeKTGLESKRLRSSQALNEDIVRVSSrlehLEKE 989
Cdd:pfam01576 572 EKTKNRLQQELDDLLvdldHQRQLVSNLEKKQKKFDQMLAEEKAI---SARYAEERDRAEAEAREKETRALS----LARA 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 990 LSEKSGQLRQGSAQNQQQiRGEIDTLRQEKDSLLKQRLEIDsKLRQGSLLSPEEERTlfQLDEAIEALDAAIEYKneait 1069
Cdd:pfam01576 645 LEEALEAKEELERTNKQL-RAEMEDLVSSKDDVGKNVHELE-RSKRALEQQVEEMKT--QLEELEDELQATEDAK----- 715
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1070 crQRVLRASASLLSQCEMNLMAKLSylSSSETRALLCKYFDKVVTLREEQHQQ-----------QIAFSELEMQLE---- 1134
Cdd:pfam01576 716 --LRLEVNMQALKAQFERDLQARDE--QGEEKRRQLVKQVRELEAELEDERKQraqavaakkklELDLKELEAQIDaank 791
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1135 ------------EQQRLVYWLEvaLERQRLEMDRQLTlQQKEHEQNVQLL--------------------LQQGRDHLGE 1182
Cdd:pfam01576 792 greeavkqlkklQAQMKDLQRE--LEEARASRDEILA-QSKESEKKLKNLeaellqlqedlaaserarrqAQQERDELAD 868
|
490 500 510
....*....|....*....|....*....|
gi 568947408 1183 GLA----------DSKRQYEARIHALEKEL 1202
Cdd:pfam01576 869 EIAsgasgksalqDEKRRLEARIAQLEEEL 898
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
968-1202 |
3.58e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 968 SSQALNEDIVRVSSRLEHLEKELSEKSGQLRQgSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRqgsllspEEERTL 1047
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRIRALEQELA-------ALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1048 FQLDEAIEALDAAIEYKNEAItcrQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYF-DKVVTLREEQHQQQIAF 1126
Cdd:COG4942 86 AELEKEIAELRAELEAQKEEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568947408 1127 SELEMQLEEQQRLVYWLEVALERQRlemdRQLTLQQKEHEQNVQLLLQQGRDHLGE--GLADSKRQYEARIHALEKEL 1202
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEER----AALEALKAERQKLLARLEKELAELAAElaELQQEAEELEALIARLEAEA 236
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
789-1081 |
5.32e-04 |
|
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: 44.44 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 789 QEFRKRVAAAQSQVQVLKEK-KQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHR 867
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKqAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 868 VKELELKHEQQQKILKikteeiaafqrkrrsgsngsvvsLEQQQKIEEQKKWLDQEMEKVLQQRRALEEL--GEELRKRE 945
Cdd:pfam12128 680 ANERLNSLEAQLKQLD-----------------------KKHQAWLEEQKEQKREARTEKQAYWQVVEGAldAQLALLKA 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 946 VILAKKEALMQEKTGLESKRLRSSQALNEDIVRVsSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQ 1025
Cdd:pfam12128 737 AIAARRSGAKAELKALETWYKRDLASLGVDPDVI-AKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQ 815
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1026 RLEIDSKLR--QGSL--LSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASL 1081
Cdd:pfam12128 816 LSNIERAISelQQQLarLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATL 875
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
949-1202 |
6.20e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 949 AKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELseksgqlrQGSAQNQQQIRGEIDTLRQEKDSLLKQRLE 1028
Cdd:PRK11281 48 LNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQL--------AQAPAKLRQAQAELEALKDDNDEETRETLS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1029 IDSkLRQgslLSPEEERTLFQLDEAIEALDaaiEYKNEAITCRQRVLRASASllsqcemnlmaklsyLSSSETRAllcky 1108
Cdd:PRK11281 120 TLS-LRQ---LESRLAQTLDQLQNAQNDLA---EYNSQLVSLQTQPERAQAA---------------LYANSQRL----- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1109 fdkvvtlreeqhqQQIAfSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNVQL--LLQQGRDHLgeglad 1186
Cdd:PRK11281 173 -------------QQIR-NLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLqdLLQKQRDYL------ 232
|
250
....*....|....*.
gi 568947408 1187 skrqyEARIHALEKEL 1202
Cdd:PRK11281 233 -----TARIQRLEHQL 243
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
740-1025 |
9.88e-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: 43.66 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 740 QALNRQHSQRIRELEQEAERVRAELCEGQRQL----RELEGREP-------QDASERSRLQEFRKRVAAAQSQVQVLKE- 807
Cdd:pfam10174 453 ERLKEQREREDRERLEELESLKKENKDLKEKVsalqPELTEKESslidlkeHASSLASSGLKKDSKLKSLEIAVEQKKEe 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 808 ---------KKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQ 878
Cdd:pfam10174 533 csklenqlkKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 879 QKILKIKTEEIAAFQRKRRSGSNG----------SVVSLEQQQKIEEqkkwLDQEMEKVLQQrraLEELGEELRKREVIL 948
Cdd:pfam10174 613 MKEQNKKVANIKHGQQEMKKKGAQlleearrredNLADNSQQLQLEE----LMGALEKTRQE---LDATKARLSSTQQSL 685
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568947408 949 AKKEALmqektgLESKRLRSSQALNEdivRVSSRLEHLEKELSEKSGQ--LRQGSAQNQQQIRGEIDTLRQEKDSLLKQ 1025
Cdd:pfam10174 686 AEKDGH------LTNLRAERRKQLEE---ILEMKQEALLAAISEKDANiaLLELSSSKKKKTQEEVMALKREKDRLVHQ 755
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
749-1200 |
1.19e-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: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 749 RIRELEQEAERVRAELCEGQRQLRELEGREPQDASERSRLQ-----------EFRKRVAAAQSQVQVL-KEKKQATERLV 816
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQlekvtteakikKLEEDILLLEDQNSKLsKERKLLEERIS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 817 SLS---AQSETRLQELE--RNVQLMRRQQGQLQRRLREETEQ-----KRRLETEMNKRQHRVKELELKHEQQQKILKIKT 886
Cdd:pfam01576 163 EFTsnlAEEEEKAKSLSklKNKHEAMISDLEERLKKEEKGRQelekaKRKLEGESTDLQEQIAELQAQIAELRAQLAKKE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 887 EEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEME-------KVLQQRRALEELGEELR----------------- 942
Cdd:pfam01576 243 EELQAALARLEEETAQKNNALKKIRELEAQISELQEDLEseraarnKAEKQRRDLGEELEALKteledtldttaaqqelr 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 943 -KREVILAK-KEALMQEKTGLESK----RLRSSQALNEdivrVSSRLEHLE--KELSEKSgqlRQGSAQNQQQIRGEIDT 1014
Cdd:pfam01576 323 sKREQEVTElKKALEEETRSHEAQlqemRQKHTQALEE----LTEQLEQAKrnKANLEKA---KQALESENAELQAELRT 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1015 LRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNLMAKLS 1094
Cdd:pfam01576 396 LQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQE 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1095 YLsSSETRALLcKYFDKVVTLREEQhqqqiafSELEMQLEEQQRlvywLEVALERQRLEMDRQLTLQQKEHEQNVQLL-- 1172
Cdd:pfam01576 476 LL-QEETRQKL-NLSTRLRQLEDER-------NSLQEQLEEEEE----AKRNVERQLSTLQAQLSDMKKKLEEDAGTLea 542
|
490 500
....*....|....*....|....*...
gi 568947408 1173 LQQGRDHLGEGLADSKRQYEARIHALEK 1200
Cdd:pfam01576 543 LEEGKKRLQRELEALTQQLEEKAAAYDK 570
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
732-1182 |
1.19e-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: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 732 LVRTGKAAQALNRQHSQRIRELEQ--EAERVRAELCEGQRQLRELEGrEPQDASERSRLQEFrkrvaAAQSQVQVLKEKK 809
Cdd:TIGR00618 148 LLPQGEFAQFLKAKSKEKKELLMNlfPLDQYTQLALMEFAKKKSLHG-KAELLTLRSQLLTL-----CTPCMPDTYHERK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 810 QATERLVslsAQSETRLQELERNvqlmrrqqGQLQRRLREETEQKRRLETEMNKRQHRVKELElkheqqqkilkiktEEI 889
Cdd:TIGR00618 222 QVLEKEL---KHLREALQQTQQS--------HAYLTQKREAQEEQLKKQQLLKQLRARIEELR--------------AQE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 890 AAFQrkrrsgsngsvvslEQQQKIEEQKKWL-----DQEMEKVLQQR-RALEELGEELRKREVILAKKEALMQEKTGLES 963
Cdd:TIGR00618 277 AVLE--------------ETQERINRARKAAplaahIKAVTQIEQQAqRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 964 KRLRSSQALN-EDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPE 1042
Cdd:TIGR00618 343 QRRLLQTLHSqEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1043 EERtLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQHQ- 1121
Cdd:TIGR00618 423 QGQ-LAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQe 501
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568947408 1122 QQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKehEQNVQLLLQQGRDHLGE 1182
Cdd:TIGR00618 502 EPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETS--EEDVYHQLTSERKQRAS 560
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
707-1241 |
1.33e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 707 RLAQAQQKIRELAINIRMKEELIGELVRTgkaaqalnrqhsqrIRELEQEAERVRAELC----EGQRQLRELEGREPQDA 782
Cdd:pfam10174 220 QLQPDPAKTKALQTVIEMKDTKISSLERN--------------IRDLEDEVQMLKTNGLlhteDREEEIKQMEVYKSHSK 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 783 SERSRLQEFRKRVAAAQSQVQVLKEKkqaterLVSLSAQSETRLQELErnvqlmrrqqgqlqrRLREETEQKrrlETEMN 862
Cdd:pfam10174 286 FMKNKIDQLKQELSKKESELLALQTK------LETLTNQNSDCKQHIE---------------VLKESLTAK---EQRAA 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 863 KRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsvvsleQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELR 942
Cdd:pfam10174 342 ILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKST----------LAGEIRDLKDMLDVKERKINVLQKKIENLQEQLR 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 943 KREVILA-KKEALmqektgleskrlrssQALNEDIVRVSSRLEHLEKELSEKS---GQLRQGSAQNQQQIRGEIDTLRQE 1018
Cdd:pfam10174 412 DKDKQLAgLKERV---------------KSLQTDSSNTDTALTTLEEALSEKEriiERLKEQREREDRERLEELESLKKE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1019 -KDslLKQRLEI--DSKLRQGSLLSPEEERT------LFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMN- 1088
Cdd:pfam10174 477 nKD--LKEKVSAlqPELTEKESSLIDLKEHAsslassGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNp 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1089 -LMAKLSYLSSSETRallckYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQL----TLQQK 1163
Cdd:pfam10174 555 eINDRIRLLEQEVAR-----YKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVanikHGQQE 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1164 EHEQNVQLLLQQGRDHLGEGLADSKRQYEARIHALEKelgrhmwINQEL---KQKLSAGSTAGQSRGCERRSLCLENRQC 1240
Cdd:pfam10174 630 MKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEK-------TRQELdatKARLSSTQQSLAEKDGHLTNLRAERRKQ 702
|
.
gi 568947408 1241 L 1241
Cdd:pfam10174 703 L 703
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
693-1135 |
1.36e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 693 VQTRQAPAAMASEWRlaQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAEL----CEGQ 768
Cdd:PRK02224 233 RETRDEADEVLEEHE--ERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAglddADAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 769 RQLRELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKEKkqaTERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLR 848
Cdd:PRK02224 311 AVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRED---ADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 849 EETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSN-----------GSVVSLEQQQKIEEQK 917
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARErveeaealleaGKCPECGQPVEGSPHV 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 918 KWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLRSSqalnedivRVSSRLEHLEKELSEKSGQL 997
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERRE--------DLEELIAERRETIEEKRERA 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 998 RQGSAQNQqqirgEIDTLRQEK-DSLLKQRLEIDSKLRQGSLLspeeERTLFQLDEAIEALDAAIEYKNEAITCRQRVLR 1076
Cdd:PRK02224 540 EELRERAA-----ELEAEAEEKrEAAAEAEEEAEEAREEVAEL----NSKLAELKERIESLERIRTLLAAIADAEDEIER 610
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568947408 1077 ASASLLSQCEMNLMAKLSYLSSSETRALLCKYFD--KVVTLREEQHQQQIAFSELEMQLEE 1135
Cdd:PRK02224 611 LREKREALAELNDERRERLAEKRERKRELEAEFDeaRIEEAREDKERAEEYLEQVEEKLDE 671
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
744-965 |
1.58e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 744 RQHSQRIRELEQEAERVRA-----ELCEGQRQLRELEGREPQDASERSRLQEfrkRVAAAQSQVQVLKEKKQATERlvSL 818
Cdd:COG4913 258 RELAERYAAARERLAELEYlraalRLWFAQRRLELLEAELEELRAELARLEA---ELERLEARLDALREELDELEA--QI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 819 SAQSETRLQELERnvqlmrrqqgqlqrrlreeteQKRRLETEMNKRQHRVKELelkhEQQQKILKIKT-EEIAAFQRKRR 897
Cdd:COG4913 333 RGNGGDRLEQLER---------------------EIERLERELEERERRRARL----EALLAALGLPLpASAEEFAALRA 387
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568947408 898 sgsngsvVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEElgeelrkrevilaKKEALMQEKTGLESKR 965
Cdd:COG4913 388 -------EAAALLEALEEELEALEEALAEAEAALRDLRR-------------ELRELEAEIASLERRK 435
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
797-1202 |
1.60e-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: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 797 AAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVkelelkhe 876
Cdd:pfam05483 322 ATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL-------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 877 qqqkilkiktEEIAAFqrkrrsgSNGSVVSLEQQQKIEEQKkwldqemEKVLQQRRALEELGEELRKREvilakkealmQ 956
Cdd:pfam05483 394 ----------EEMTKF-------KNNKEVELEELKKILAED-------EKLLDEKKQFEKIAEELKGKE----------Q 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 957 EKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLrqgsaqnqqqirgeidtlrqEKDSLlkQRLEIDSKLRQG 1036
Cdd:pfam05483 440 ELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL--------------------EKEKL--KNIELTAHCDKL 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1037 SLlspeEERTLFQldeaiEALDAAIEYKNEA---ITCRQRVLRASASL--LSQCEMNLMAKLSYlsssetrallckyfdk 1111
Cdd:pfam05483 498 LL----ENKELTQ-----EASDMTLELKKHQediINCKKQEERMLKQIenLEEKEMNLRDELES---------------- 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1112 vvtLREEQHQQQiafSELEMQL---EEQQRLVYWLEVALERQRLEMDRQ---LTLQQKEHEQNVQLLLQQGRDHLGEGLA 1185
Cdd:pfam05483 553 ---VREEFIQKG---DEVKCKLdksEENARSIEYEVLKKEKQMKILENKcnnLKKQIENKNKNIEELHQENKALKKKGSA 626
|
410
....*....|....*....
gi 568947408 1186 DSKR--QYEARIHALEKEL 1202
Cdd:pfam05483 627 ENKQlnAYEIKVNKLELEL 645
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
795-957 |
1.61e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 795 VAAAQSQVQVLKEK-KQATERLVSLSAQSETRLQELERnvqlmrrqqgqlqrrLREETEQ-KRRLETEMNKRQHRVKELE 872
Cdd:PRK00409 504 IEEAKKLIGEDKEKlNELIASLEELERELEQKAEEAEA---------------LLKEAEKlKEELEEKKEKLQEEEDKLL 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 873 LKHEQQ-QKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKwLDQEMEKV----LQQRRALEEL--GEELR--- 942
Cdd:PRK00409 569 EEAEKEaQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKR-LNKANEKKekkkKKQKEKQEELkvGDEVKyls 647
|
170 180
....*....|....*....|
gi 568947408 943 ---KREV--ILAKKEALMQE 957
Cdd:PRK00409 648 lgqKGEVlsIPDDKEAIVQA 667
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
862-1055 |
1.63e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 862 NKRQHRVKELELKHEQQQKILKIKTEEIAAFQR------KRRSGSNGSVVSLEQQQKieEQKKWLDQEMEKVLQQRRALE 935
Cdd:TIGR04523 29 NKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKnlnkdeEKINNSNNKIKILEQQIK--DLNDKLKKNKDKINKLNSDLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 936 ELGEELR-KREVILAKKEalmqektglESKRL-RSSQALNEDIVRVSSRLEHLEKELSEKSGQLRqgsaqnqqQIRGEID 1013
Cdd:TIGR04523 107 KINSEIKnDKEQKNKLEV---------ELNKLeKQKKENKKNIDKFLTEIKKKEKELEKLNNKYN--------DLKKQKE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568947408 1014 TLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIE 1055
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQ 211
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
705-992 |
1.64e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 705 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALnRQHSQRIREL---EQEAERVRAELCEGQRQLRELEgrepqd 781
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYswdEIDVASAEREIAELEAELERLD------ 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 782 aSERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEM 861
Cdd:COG4913 682 -ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 862 NKRQHRVKElELKHEQQQKILKIKTEE------IAAFQRKRRSGSNGSVVSLEQqqkIEEQKKWLDQemekvlQQRRALE 935
Cdd:COG4913 761 DAVERELRE-NLEERIDALRARLNRAEeeleraMRAFNREWPAETADLDADLES---LPEYLALLDR------LEEDGLP 830
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 568947408 936 ELGEELRKrevilAKKEALMQEKTGLeskrlrsSQALNEDIVRVSSRLEHLEKELSE 992
Cdd:COG4913 831 EYEERFKE-----LLNENSIEFVADL-------LSKLRRAIREIKERIDPLNDSLKR 875
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
748-944 |
1.73e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 748 QRIRELEQEAERVRAELCEGQRQLRELEGREpqdASERSRLQEFRKRVAAAQSQVQVLKEK-KQATERLVSLSAQSEtrL 826
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARL---EAAKTELEDLEKEIKRLELEIEEVEARiKKYEEQLGNVRNNKE--Y 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 827 QELERnvqlmrrqqgqlqrrlrEETEQKRRLEtemnKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRsgsngsvvs 906
Cdd:COG1579 92 EALQK-----------------EIESLKRRIS----DLEDEILELMERIEELEEELAELEAELAELEAELE--------- 141
|
170 180 190
....*....|....*....|....*....|....*....
gi 568947408 907 lEQQQKIEEQKKWLDQEMEKVLQQRRALEE-LGEELRKR 944
Cdd:COG1579 142 -EKKAELDEELAELEAELEELEAEREELAAkIPPELLAL 179
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
744-1028 |
2.38e-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: 41.97 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 744 RQHSQRIRELEQEAERVRAELCEGQRQLRELE---GREPQDASERSRLQE----FRKRVAAAQSQVQVLKEK-KQAteRL 815
Cdd:pfam15742 65 KQAQQKLLDSTKMCSSLTAEWKHCQQKIRELElevLKQAQSIKSQNSLQEklaqEKSRVADAEEKILELQQKlEHA--HK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 816 VSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMN---------------------KRQHRVKELELK 874
Cdd:pfam15742 143 VCLTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNelqqqvrslqdkeaqlemtnsQQQLRIQQQEAQ 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 875 HEQQQKILKIKTEEIAAfqrkrrsgsngsvvsleqQQKIEEQKKWLDQEMEKVLQQ-RRALEELGEELRKRevilakKEA 953
Cdd:pfam15742 223 LKQLENEKRKSDEHLKS------------------NQELSEKLSSLQQEKEALQEElQQVLKQLDVHVRKY------NEK 278
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568947408 954 LMQEKTGLEskrlRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQnQQQIRGEIDTLRQEKDSLLKQRLE 1028
Cdd:pfam15742 279 HHHHKAKLR----RAKDRLVHEVEQRDERIKQLENEIGILQQQSEKEKAF-QKQVTAQNEILLLEKRKLLEQLTE 348
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
719-1067 |
2.38e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 719 AINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQdasERSRLQEFRKRVAAA 798
Cdd:COG4372 23 GILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE---LNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 799 QSQVQVLKEKKQATERLVslsAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELE---LKH 875
Cdd:COG4372 100 QEELESLQEEAEELQEEL---EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEqelQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 876 EQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEEL-GEELRKREVILAKKEAL 954
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALlDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 955 MQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLR 1034
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330 340 350
....*....|....*....|....*....|...
gi 568947408 1035 QGSLLSPEEERTLFQLDEAIEALDAAIEYKNEA 1067
Cdd:COG4372 337 AELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
907-1201 |
2.92e-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: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 907 LEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRKREvilAKKEALMQEKTGLESKRLRSSQALNEDIVR------VS 980
Cdd:COG3096 343 LRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAE---ARLEAAEEEVDSLKSQLADYQQALDVQQTRaiqyqqAV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 981 SRLEHLEK-----ELSEKSGQLRQGSAQNQQQirgEIDTLRQEkdslLKQRLEIDSKLRQgsllspeeertlfQLDEAIE 1055
Cdd:COG3096 420 QALEKARAlcglpDLTPENAEDYLAAFRAKEQ---QATEEVLE----LEQKLSVADAARR-------------QFEKAYE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1056 AL---------DAAIEYKNEAItCRQRVLRASASLLSQCEMNLmAKLSYLSSSETRAL-----LCKYFDKVVT----LRE 1117
Cdd:COG3096 480 LVckiageverSQAWQTARELL-RRYRSQQALAQRLQQLRAQL-AELEQRLRQQQNAErlleeFCQRIGQQLDaaeeLEE 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1118 EQHQQQIAFSELEMQLEEQQrlvywlEVALE-RQRLEmdrQLTLQQKEHEQ------NVQLLLQQGRDHLGEGLADSKRQ 1190
Cdd:COG3096 558 LLAELEAQLEELEEQAAEAV------EQRSElRQQLE---QLRARIKELAArapawlAAQDALERLREQSGEALADSQEV 628
|
330
....*....|.
gi 568947408 1191 YEARIHALEKE 1201
Cdd:COG3096 629 TAAMQQLLERE 639
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
787-1062 |
2.94e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 787 RLQEFRKRVAAAQSQVQVLKEKKQatERLVSLSAQSE--------TRLQELErnvqlmrrqqgqlqRRLREETEQKRRLE 858
Cdd:PRK02224 163 KLEEYRERASDARLGVERVLSDQR--GSLDQLKAQIEekeekdlhERLNGLE--------------SELAELDEEIERYE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 859 TEMNKRQHRVKELEL---KHEQQQKILKIKTEEIAafqrkrrsgsngsvvslEQQQKIEEQKKWLDQEMEKVLQQRRALE 935
Cdd:PRK02224 227 EQREQARETRDEADEvleEHEERREELETLEAEIE-----------------DLRETIAETEREREELAEEVRDLRERLE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 936 ELGEELRKrevilakkealMQEKTGLESKrlrSSQALNEDIVRVSSRLEHLEKELSEKSgqLRQGSAQNQ-QQIRGEIDT 1014
Cdd:PRK02224 290 ELEEERDD-----------LLAEAGLDDA---DAEAVEARREELEDRDEELRDRLEECR--VAAQAHNEEaESLREDADD 353
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568947408 1015 LRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIE 1062
Cdd:PRK02224 354 LEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
709-916 |
3.35e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 709 AQAQQKIRELAINIrmkEELIGELvrtgkaaQALNRQHSQRIRELE---QEAERVRAELcegQRQLRELEGREpqdASER 785
Cdd:PRK00409 505 EEAKKLIGEDKEKL---NELIASL-------EELERELEQKAEEAEallKEAEKLKEEL---EEKKEKLQEEE---DKLL 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 786 SRL-QEFRKRVAAAqsqvqvlkekKQATERLVSlsaqsetRLQELERnvqlmrrqqgqlqrrlREETEQKRRLETEMNKR 864
Cdd:PRK00409 569 EEAeKEAQQAIKEA----------KKEADEIIK-------ELRQLQK----------------GGYASVKAHELIEARKR 615
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568947408 865 qhrvkeLELKHEQQQKILKIKTEEIAAFQ-----RKRRSGSNGSVVSLEQQQKIEEQ 916
Cdd:PRK00409 616 ------LNKANEKKEKKKKKQKEKQEELKvgdevKYLSLGQKGEVLSIPDDKEAIVQ 666
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
707-1206 |
4.50e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 707 RLAQAQQKIRELAINIRMKEELIgELVRTGKAAQALNRQHsQRIRELEQEAERVRAELCEGQRQLRELEGREpqDASERS 786
Cdd:COG4913 256 PIRELAERYAAARERLAELEYLR-AALRLWFAQRRLELLE-AELEELRAELARLEAELERLEARLDALREEL--DELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 787 RLQEFRKRVAAAQSQVQVLKEKKQATERLvslSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQH 866
Cdd:COG4913 332 IRGNGGDRLEQLEREIERLERELEERERR---RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 867 rvkELELKHEQQQKILKIKTEEIAAFQRkRRSGSNGSVVS----LEQQQKI---------------EEQKKWLDQeMEKV 927
Cdd:COG4913 409 ---EAEAALRDLRRELRELEAEIASLER-RKSNIPARLLAlrdaLAEALGLdeaelpfvgelievrPEEERWRGA-IERV 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 928 L---------------QQRRALEE--LGEELRKREVILAKKEALMQ--------EKtgLESKR------LRSSQALNEDI 976
Cdd:COG4913 484 LggfaltllvppehyaAALRWVNRlhLRGRLVYERVRTGLPDPERPrldpdslaGK--LDFKPhpfrawLEAELGRRFDY 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 977 VRVSS--RLEHLEKELSeKSGQLRQGSAqnqqqiRGEIDTLRQEKDSLL-----KQRLEIDSKLRQgsllspEEERTLFQ 1049
Cdd:COG4913 562 VCVDSpeELRRHPRAIT-RAGQVKGNGT------RHEKDDRRRIRSRYVlgfdnRAKLAALEAELA------ELEEELAE 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1050 LDEAIEALDAAIEYKNEAITCRQRVLRAS------ASLLSQCEmNLMAKLSYLSSSEtrallckyfDKVVTLREEQHQQQ 1123
Cdd:COG4913 629 AEERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIA-ELEAELERLDASS---------DDLAALEEQLEELE 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 1124 IAFSELEMQLEEQQRLVYWLEVALERQRLEMDR-QLTLQQKEHEQNV-----------QLLLQQGRDHLGEGLADSKRQY 1191
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDElQDRLEAAEDLARLelralleerfaAALGDAVERELRENLEERIDAL 778
|
570
....*....|....*
gi 568947408 1192 EARIHALEKELGRHM 1206
Cdd:COG4913 779 RARLNRAEEELERAM 793
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
748-951 |
7.10e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.46 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 748 QRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERSRLQEFRKRVAAAQsqvqvlkEKKQATERLVSLSAQSETRLQ 827
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRERE-------ELQREEERLVQKEEQLDARAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 828 ELErnvqlmrrqqgqlqrrlreetEQKRRLETEMNKRQHRVKELELKHEQQQKILKIkteeiaafqrkrrsgsngsVVSL 907
Cdd:PRK12705 99 KLD---------------------NLENQLEEREKALSARELELEELEKQLDNELYR-------------------VAGL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568947408 908 EQQQKIEEQKKWLDQEMEKVLQQR--RALEELGEELRKREVILAKK 951
Cdd:PRK12705 139 TPEQARKLLLKLLDAELEEEKAQRvkKIEEEADLEAERKAQNILAQ 184
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
709-958 |
7.30e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.88 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 709 AQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERSRL 788
Cdd:pfam17380 400 AARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 789 QEFRKRVAAAQSQVQVLKEKkqaterlvslsaqsetrlqELERNVQLMrrqqgqlqrrlREETEQKRRLETEMNKRQHRV 868
Cdd:pfam17380 480 EKEKRDRKRAEEQRRKILEK-------------------ELEERKQAM-----------IEEERKRKLLEKEMEERQKAI 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 869 KElelkhEQQQKILkikteeiaafQRKRRsgsngsvvsleQQQKIEEQKKwLDQEMEKVLQQRRALEELGeelRKREVIL 948
Cdd:pfam17380 530 YE-----EERRREA----------EEERR-----------KQQEMEERRR-IQEQMRKATEERSRLEAME---REREMMR 579
|
250
....*....|
gi 568947408 949 AKKEALMQEK 958
Cdd:pfam17380 580 QIVESEKARA 589
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
738-970 |
8.01e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 40.51 E-value: 8.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 738 AAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGR-EPQDASERSRLQEFRKrvaaaqsqvQVLKEKKQATERLV 816
Cdd:pfam07111 471 PAPPVDADLSLELEQLREERNRLDAELQLSAHLIQQEVGRaREQGEAERQQLSEVAQ---------QLEQELQRAQESLA 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 817 SLSAQSETRLQelernvqlmrrqqgqlqrRLREETEQKRRLETEMNKRQH--------RVKELELKHEQQQKILKIKTEE 888
Cdd:pfam07111 542 SVGQQLEVARQ------------------GQQESTEEAASLRQELTQQQEiygqalqeKVAEVETRLREQLSDTKRRLNE 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 889 IAAFQRKrrsgsngSVVSLEQQQKIEEQKKWLDQEMEKVlqQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLRS 968
Cdd:pfam07111 604 ARREQAK-------AVVSLRQIQHRATQEKERNQELRRL--QDEARKEEGQRLARRVQELERDKNLMLATLQQEGLLSRY 674
|
..
gi 568947408 969 SQ 970
Cdd:pfam07111 675 KQ 676
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
915-1066 |
8.07e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 915 EQKKWLDQEMEKVLQQRRALEELGEELRKREVIL--------AKKEALMQEKTGL--ESKRLRSS-QALNEDIVRVSSRL 983
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELneelkelaEKRDELNAQVKELreEAQELREKrDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 984 EHLEKELSEKSGQLRQGSAQNQQQI--RGEIDTLRQEKDSLLKQrleidsklRQGSLLSPEEERTLF----QLDEAIEAL 1057
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNkaGGSIDKLRKEIERLEWR--------QQTEVLSPEEEKELVekikELEKELEKA 152
|
....*....
gi 568947408 1058 DAAIEYKNE 1066
Cdd:COG1340 153 KKALEKNEK 161
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
710-951 |
8.56e-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: 40.39 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 710 QAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEgrepqdaSERSRLQ 789
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN-------EEKKELE 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 790 EfrkRVAAAQSQVQVLKEKKQAterLVSLSAQSETRLQELERNVQLMrrqqgqlqrrlrEETEQKRRLETEMNKRQHRVK 869
Cdd:TIGR04523 510 E---KVKDLTKKISSLKEKIEK---LESEKKEKESKISDLEDELNKD------------DFELKKENLEKEIDEKNKEIE 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 870 ELEL-------KHEQQQKILKIKTEEIAAFqRKRRSGSNGSVVSLEQQ--------QKIEEQKKWLDQEMEKVLQQRRAL 934
Cdd:TIGR04523 572 ELKQtqkslkkKQEEKQELIDQKEKEKKDL-IKEIEEKEKKISSLEKElekakkenEKLSSIIKNIKSKKNKLKQEVKQI 650
|
250
....*....|....*..
gi 568947408 935 EELGEELRKREVILAKK 951
Cdd:TIGR04523 651 KETIKEIRNKWPEIIKK 667
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
725-1045 |
8.65e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 725 KEELIGELVRTGKAAQALNRQHSQ---RIRELEQEAERVRAELcegQRQLRELEGREPQDASERSRLQEFRKRVAAAQSQ 801
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKalfELDKLQEELEQLREEL---EQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 802 VQ-VLKEKKQATERLVSLSAQSETRLQELERnvqlMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELK-HEQQQ 879
Cdd:COG4372 89 LQaAQAELAQAQEELESLQEEAEELQEELEE----LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQlESLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 880 KILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWL-----DQEMEKVLQQRRALEELGEELRKREVILAKKEAL 954
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAeklieSLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 955 MQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLR 1034
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
330
....*....|.
gi 568947408 1035 QGSLLSPEEER 1045
Cdd:COG4372 325 AKKLELALAIL 335
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
747-1084 |
9.24e-03 |
|
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: 40.49 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 747 SQRIRELEQEAERVRAELCEGQRQLRELEgrepqdasersrlqefrkrvAAAQSQVQVLKEKKQatERLVSLSAQSETRL 826
Cdd:pfam15921 223 SKILRELDTEISYLKGRIFPVEDQLEALK--------------------SESQNKIELLLQQHQ--DRIEQLISEHEVEI 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 827 QELERNVQLMRRQQGQLQRRLREETEQKRR-----------LETEMNKRQHRVKE----LELKHEQQQKILKIKTEEIAA 891
Cdd:pfam15921 281 TGLTEKASSARSQANSIQSQLEIIQEQARNqnsmymrqlsdLESTVSQLRSELREakrmYEDKIEELEKQLVLANSELTE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 892 FQRKRRSGSNGSVVSLEQQQKI------EEQKKWLDQEMEKVLQQRR-----ALEELGEELRKREVILAKKEALMQ---- 956
Cdd:pfam15921 361 ARTERDQFSQESGNLDDQLQKLladlhkREKELSLEKEQNKRLWDRDtgnsiTIDHLRRELDDRNMEVQRLEALLKamks 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 957 EKTGLESKRLRSSQALNEDIVRVSSRLEHLE--KELSEKSGQ---LRQGSAQNQQQIRGEIDTLRQEKD--------SLL 1023
Cdd:pfam15921 441 ECQGQMERQMAAIQGKNESLEKVSSLTAQLEstKEMLRKVVEeltAKKMTLESSERTVSDLTASLQEKEraieatnaEIT 520
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568947408 1024 KQRLEIDSKLRQGSLLSPEEERtLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQ 1084
Cdd:pfam15921 521 KLRSRVDLKLQELQHLKNEGDH-LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQ 580
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
863-1067 |
9.40e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 863 KRQHRVKELELKhEQQQKILKIKTEEIAAFQRKRRsgsngsvvsLEQQQKIEEQKkwldQEMEKVLQQRRA-LEELGEEL 941
Cdd:PRK12704 26 KKIAEAKIKEAE-EEAKRILEEAKKEAEAIKKEAL---------LEAKEEIHKLR----NEFEKELRERRNeLQKLEKRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 942 RKREVILAKK-EALMQEKTGLESKRlrssqalnedivrvsSRLEHLEKELSEKsgqlrqgsaqnqqqiRGEIDTLRQEkd 1020
Cdd:PRK12704 92 LQKEENLDRKlELLEKREEELEKKE---------------KELEQKQQELEKK---------------EEELEELIEE-- 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568947408 1021 slLKQRLEIDSKlrqgslLSPEEERTLfQLDEAIEAL--DAAI---EYKNEA 1067
Cdd:PRK12704 140 --QLQELERISG------LTAEEAKEI-LLEKVEEEArhEAAVlikEIEEEA 182
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
699-818 |
9.77e-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: 9.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947408 699 PAAMASEWRLAQAQQKIRELAINIRMKEELIGELvrtgkaaQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGRE 778
Cdd:COG2433 399 REKEHEERELTEEEEEIRRLEEQVERLEAEVEEL-------EAELEEKDERIERLERELSEARSEERREIRKDREISRLD 471
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 568947408 779 PQDASERSRLQEFRKRVAAAQSQVQVLKE--KKQATERLVSL 818
Cdd:COG2433 472 REIERLERELEEERERIEELKRKLERLKElwKLEHSGELVPV 513
|
|
| |
